Information on EC 4.2.2.3 - poly(beta-D-mannuronate) lyase

New: Word Map on EC 4.2.2.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
4.2.2.3
-
RECOMMENDED NAME
GeneOntology No.
poly(beta-D-mannuronate) lyase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
-
-
-
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Alginovibrio aquatilis
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Azotobacter phage A22, Azotobacter phage A31
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Azotobacter vinelandii phage, Bacillus circulans, Bacillus sp.
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
enzyme seems to have 6 substrate binding sites, also performs reaction of EC 4.2.2.11
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
also performs reaction of EC 4.2.2.11, the enzyme molecule shows a cleft which might bear the active site with a tryptophan residue being involved in the catalytic reaction
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
alginate lyase activity and mannuronan C-5-epimerase activity of the bifunctional enzyme might use the same active site
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
His192 is an active site residue, essential for activity
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
substrate binding site structure, active site cleft, catalytic mechanism
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
A1-II with a glove-like beta-sandwich as a basic scaffold forms a cleft covered with two lid loops (L1/L2). Loop flexibility for substrate binding and structural determinants for broad substrate recognition and catalytic reaction is shown. The two loops associate mutually over the cleft through the formation of a hydrogen bond between their edges (Asn141 and Asn199)
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues, substrate binding mode, overview
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
substrate binding, strutural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
enzyme seems to have 6 substrate binding sites, also performs reaction of EC 4.2.2.11
-
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Alteromonas sp. H-4, Azotobacter chroococcum 4A1M, Bacillus sp. ATB-1015, Photobacterium sp. ATCC 43367 Alg-A
-
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
also performs reaction of EC 4.2.2.11, the enzyme molecule shows a cleft which might bear the active site with a tryptophan residue being involved in the catalytic reaction
Pseudoalteromonas sp. 272
-
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
beta-elimination mechanism, substrate binding and catalytic site
Pseudomonas aeruginosa FRDI, Pseudomonas alginovora XO17
-
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
substrate binding, strutural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
Saccharophagus degradans DSM 17024
-
-
Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends.
show the reaction diagram
residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues, substrate binding mode, overview
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alginate degradation
-
-
Fructose and mannose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
poly[(1->4)-beta-D-mannuronide] lyase
The enzyme from the bacterium Sphingomonas sp. strain A1 cleaves alginate producing di- and trisaccharides with an unsaturated uronyl residue at the non-reducing terminus.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(poly alpha-l-guluronate) lyase
-
-
A1 alginate lyase
-
-
A1m
Agarivorans sp.
-
A1mU
Agarivorans sp.
isoform
A9mC
isoform
A9mC
Vibrio sp. A9m, Vibrio sp. JAM-A9m
isoform
-
A9mL
isoform
A9mL
Vibrio sp. A9m, Vibrio sp. JAM-A9m
isoform
-
A9mT
; isoform
A9mT
Vibrio sp. A9m, Vibrio sp. JAM-A9m
; isoform
-
AAlyase
Pseudoalteromonas sp. 272
-
;
-
AL2
-
-
alg
Agarivorans sp.
gene name
Alg-A
Photobacterium sp. ATCC 43367 Alg-A
-
-
-
Alg17C
Saccharophagus degradans DSM 17024
-
-
Alg7D
-
gene name
alginase I
-
-
alginate lyase
Agarivorans sp.
-
alginate lyase
Agarivorans sp.
-
alginate lyase
Alginovibrio aquatilis
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
-
-
-
alginate lyase
Alteromonas sp. H-4
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
Azotobacter phage A22, Azotobacter phage A31
-
-
alginate lyase
Azotobacter vinelandii phage, Bacillus circulans, Bacillus sp.
-
-
alginate lyase
Bacillus sp. ATB-1015
-
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
Fucus spp.
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
Ishige sp.
-
-
alginate lyase
-
-
alginate lyase
Klebsiella pneumoniae SM0524
-
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
Photobacterium sp. ATCC 43367 Alg-A
-
-
-
alginate lyase
-
-
alginate lyase
Pseudoalteromonas atlantica AR06
-
-
-
alginate lyase
-
-
alginate lyase
Pseudoalteromonas sp. 272
-
;
-
alginate lyase
-
-
-
alginate lyase
Pseudomonas aeruginosa FRDI
-
-
alginate lyase
-
-
alginate lyase
Pseudomonas alginovora X017
-
-
-
alginate lyase
Pseudomonas alginovora XO17
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
Pseudomonas sp. N7151-6
-
-
-
alginate lyase
-
-
alginate lyase
-
-
alginate lyase
Saccharophagus degradans DSM 17024
-
-
alginate lyase
-
-
alginate lyase
Stenotrophomas maltophilia
-
alginate lyase
Stenotrophomas maltophilia KJ-2
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
Streptomyces sp. ALG-5
-
-
-
alginate lyase
-
-
alginate lyase
-
alginate lyase
-
-
alginate lyase
Vibrio sp. JAM-A9m
-
-
alginate lyase
-
;
-
alginate lyase A
-
-
alginate lyase A
Pseudomonas fluorescens HZJ216
-
-
-
alginate lyase A1-II
-
-
alginate lyase A1-II'
-
-
alginate lyase A1-II'
-
alginate lyase A1-III
-
alginate lyase AlyPEEC
-
-
alginate lyase Atu3025
-
-
alginate lyase Atu3025
Agrobacterium tumefaciens C58
-
-
-
alginate lyase B
-
-
alginate lyase B
Pseudomonas fluorescens HZJ216
-
-
-
alginate lyase C
-
-
alginate lyase C
Pseudomonas fluorescens HZJ216
-
-
-
alginate lyase I
-
-
-
-
alginate lyase VI
-
-
-
-
alginate lyase1-III
-
-
AlgL
-
-
-
-
AlgL
Bacillus sp. ATB-1015
-
-
-
AlgL
-
-
AlgL
Pseudomonas aeruginosa AlgL
-
-
-
AlgL
Pseudomonas aeruginosa FRDI
-
-
Aly28
-
isoform
Aly32
-
isoform
Aly35
-
isoform
AlyA
Klebsiella pneumoniae SM0524
-
-
-
AlyA1
-
isoform
AlyA2
-
isoform
AlyA3
-
isoform
AlyA5
Zobellia galactanivorans DSM 12802
-
-
AlyV5
-
-
AlyV5
-
-
-
AlyVI
-
-
-
Atu3025
member of the polysaccharide lyase family 15
Atu3025
Agrobacterium tumefaciens C58
-
-
-
EC 4.2.99.4
-
-
formerly
-
endo-type alginate lyase
-
-
endolytic poly(M) lyase
-
-
endolytic polymannuronate lyase
-
-
exotype alginate lyase
-
-
exotype alginate lyase
-
exotype alginate lyase
Agrobacterium tumefaciens C58
-
-
-
KJ-2 alginate lyase
Stenotrophomas maltophilia
-
KJ-2 alginate lyase
Stenotrophomas maltophilia KJ-2
-
-
lyase AlyA
-
-
lyase AlyA
Klebsiella pneumoniae SM0524
-
-
-
lyase, alginate
-
-
-
-
Lysis protein
-
M block-specific polymannuronate lyase
-
mannuronate alginate lyase
-
-
-
-
MJ-3 alginate lyase
-
oligoalginate lyase
-
-
oligoalginate lyase
-
-
oligoalginate lyase
-
oligoalginate lyase
-
-
PL-5 alginate lyase
-
PM lyase
Pseudoalteromonas atlantica AR06
-
-
-
poly(1,4-beta-D-mannuronide) lyase
-
-
-
-
poly(beta-D-1,4-mannuronide) lyase
-
-
-
-
Poly(beta-D-mannuronate) lyase
-
-
-
-
poly(M) lyase
-
-
poly(M) lyase
-
-
Poly(mana) alginate lyase
-
-
-
-
poly(mana)alginate lyase
-
-
-
-
polymannuronate lyase
Agarivorans sp.
-
polymannuronate lyase
-
-
polymannuronate lyase
-
-
polymannuronate lyase
-
-
polymannuronate lyase
-
-
-
polyMG-specific alginate lyase
Stenotrophomas maltophilia
-
polyMG-specific alginate lyase
Stenotrophomas maltophilia KJ-2
-
-
protein PA1167
-
-
protein PA1167
Pseudomonas aeruginosa AlgL
-
-
-
SP2
-
-
-
-
MJ-3 alginate lyase
-
-
additional information
-
AkAly28 and AkAly33 belong to polysaccharide lyase family 14
additional information
the enzyme belongs to the polysaccharide-lyase-family 14, PL-14
additional information
-
enzyme belongs to the family of secreted Ca2+-dependent epimerases
CAS REGISTRY NUMBER
COMMENTARY
86922-62-5
-
9024-15-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Agarivorans sp.
; strain JAM-A1m
UniProt
Manually annotated by BRENDA team
Agarivorans sp.
strain JAM-A1m
UniProt
Manually annotated by BRENDA team
; strain JAM-A1m
UniProt
Manually annotated by BRENDA team
strain JAM-A1m
UniProt
Manually annotated by BRENDA team
; polysaccharide lyase family 15
UniProt
Manually annotated by BRENDA team
Agrobacterium tumefaciens C58
strain C58
-
-
Manually annotated by BRENDA team
Alginovibrio aquatilis
-
-
-
Manually annotated by BRENDA team
extracellular isozyme; strain H-4, several isozymes with homo- or heterogenous substrate specificities
SwissProt
Manually annotated by BRENDA team
strain 272, bifunctional enzyme
-
-
Manually annotated by BRENDA team
strain 272, bifunctional enzyme
-
-
Manually annotated by BRENDA team
Alteromonas sp. H-4
extracellular isozyme; strain H-4, several isozymes with homo- or heterogenous substrate specificities
SwissProt
Manually annotated by BRENDA team
enzyme belongs to polysaccharide lyase family 14; two alginate lyase isozymes, AkAly28 and AkAly33
-
-
Manually annotated by BRENDA team
isolated from brown alga Dictyota dichotoma; isolated from brown seaweed
-
-
Manually annotated by BRENDA team
strain ATCC 4412, gene algL
SwissProt
Manually annotated by BRENDA team
Azotobacter chroococcum 4A1M
strain 4A1M
-
-
Manually annotated by BRENDA team
Azotobacter phage A22
-
-
-
Manually annotated by BRENDA team
Azotobacter phage A31
-
-
-
Manually annotated by BRENDA team
alginate lyase precursor; recombinant
SwissProt
Manually annotated by BRENDA team
bifunctional enzyme comprising alginate lyase activity as well as mannuronan C-5-epimerase activity
-
-
Manually annotated by BRENDA team
bifunctional enzyme, also possesses epimerase activity
SwissProt
Manually annotated by BRENDA team
strain ATCC 9046
-
-
Manually annotated by BRENDA team
Azotobacter vinelandii phage
-
-
-
Manually annotated by BRENDA team
Azotobacter vinelandii phage
distinct from the enzyme from the host organism
-
-
Manually annotated by BRENDA team
strain JBH2, strain 1351, groups 3,4,5,8
-
-
Manually annotated by BRENDA team
ATB-1015
-
-
Manually annotated by BRENDA team
strain ATB-1015
-
-
Manually annotated by BRENDA team
Bacillus sp. ATB-1015
ATB-1015
-
-
Manually annotated by BRENDA team
Bacillus sp. ATB-1015
strain ATB-1015
-
-
Manually annotated by BRENDA team
isolated from Chlorella sp. strain NC64A, gene cl2
SwissProt
Manually annotated by BRENDA team
marine mussel
-
-
Manually annotated by BRENDA team
Dollabella auricola
-
-
-
Manually annotated by BRENDA team
Fucus spp.
-
-
-
Manually annotated by BRENDA team
abalone, alginase I
-
-
Manually annotated by BRENDA team
pink abalone
-
-
Manually annotated by BRENDA team
california red abalone
-
-
Manually annotated by BRENDA team
Ishige sp.
-
-
-
Manually annotated by BRENDA team
isolated from rotten seaweed
AB489222
GenBank
Manually annotated by BRENDA team
Isoptericola halotolerans CGMCC5336
isolated from rotten seaweed
AB489222
GenBank
Manually annotated by BRENDA team
gene alyA; polysaccharide lyase family 7 lyase
-
-
Manually annotated by BRENDA team
subsp. aerogenes, isolated from the gut of abalone from the South Sea near Yeosu in the Republic of Korea
UniProt
Manually annotated by BRENDA team
Klebsiella pneumoniae SM0524
gene alyA; polysaccharide lyase family 7 lyase
-
-
Manually annotated by BRENDA team
brown algae
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola
-
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola ATCC 51442
-
-
-
Manually annotated by BRENDA team
brown algae
-
-
Manually annotated by BRENDA team
marine mussel
-
-
Manually annotated by BRENDA team
strain ATCC 433367, marine bacterium
SwissProt
Manually annotated by BRENDA team
Photobacterium sp. ATCC 43367 Alg-A
Alg-A
-
-
Manually annotated by BRENDA team
Pseudoalteromonas atlantica AR06
strain AR06
-
-
Manually annotated by BRENDA team
bifunctional enzyme, actitivies against poly(beta-D-mannuronate), EC 4.2.2.3, and poly(alpha-L-guluronate), EC 4.2.2.11; from marine rotten kelp from a kelp culture field at the seashore of Yantai, China
-
-
Manually annotated by BRENDA team
strain 272, bifunctional enzyme
-
-
Manually annotated by BRENDA team
strain 272, bifunctional enzyme AAlyase
-
-
Manually annotated by BRENDA team
strain CY24
-
-
Manually annotated by BRENDA team
Pseudoalteromonas sp. 272
strain 272, bifunctional enzyme
-
-
Manually annotated by BRENDA team
Pseudoalteromonas sp. 272
strain 272, bifunctional enzyme AAlyase
-
-
Manually annotated by BRENDA team
bifunctional enzyme, actitivies against poly(beta-D-mannuronate), EC 4.2.2.3, and poly(alpha-L-guluronate), EC 4.2.2.11; from marine rotten kelp from a kelp culture field at the seashore of Yantai, China
-
-
Manually annotated by BRENDA team
; strain FRDI
SwissProt
Manually annotated by BRENDA team
AlgL; protein PA1167
-
-
Manually annotated by BRENDA team
gene algL, encoded on the algD operon, AlgD/8/44/K/E/G/X/L/I/J/F/A
SwissProt
Manually annotated by BRENDA team
mucoid strains FRD1 and 144M from the lungs of patients with cystic fibrosis
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
Pseudomonas aeruginosa AlgL
AlgL
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa CF1/M1
CF1/M1
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa FRDI
strain FRDI
SwissProt
Manually annotated by BRENDA team
strain XO17, constitutive enzyme expression, recombinant enzyme
SwissProt
Manually annotated by BRENDA team
Pseudomonas alginovora X017
-
-
-
Manually annotated by BRENDA team
Pseudomonas alginovora XO17
strain XO17, constitutive enzyme expression, recombinant enzyme
SwissProt
Manually annotated by BRENDA team
; isolated from brown seaweed in the Yellow Sea of China
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens HZJ216
; isolated from brown seaweed in the Yellow Sea of China
-
-
Manually annotated by BRENDA team
OS-ALG-9
-
-
Manually annotated by BRENDA team
strain N7151-6
-
-
Manually annotated by BRENDA team
strain QD03
Uniprot
Manually annotated by BRENDA team
Pseudomonas sp. HZJ 216
-
-
-
Manually annotated by BRENDA team
Pseudomonas sp. N7151-6
strain N7151-6
-
-
Manually annotated by BRENDA team
strain QD03
Uniprot
Manually annotated by BRENDA team
pv. syringae
SwissProt
Manually annotated by BRENDA team
gene alg17C
UniProt
Manually annotated by BRENDA team
Saccharophagus degradans DSM 17024
-
UniProt
Manually annotated by BRENDA team
; isolated from fermented brown seaweed with salted and fermented anchovy, sea mustard, Undaria pinnatifida
UniProt
Manually annotated by BRENDA team
isozymes ALY I-III
-
-
Manually annotated by BRENDA team
strain A1
SwissProt
Manually annotated by BRENDA team
strain A1
SwissProt
Manually annotated by BRENDA team
strain A1, 3 isoforms A1-I, A1-II, and A1-III
-
-
Manually annotated by BRENDA team
strain A1, 3 isoforms A1-I, A1-II, and A1-III of alginate lyase, 1 oligoalginate lyase
-
-
Manually annotated by BRENDA team
strain A1, isozyme A1-II
-
-
Manually annotated by BRENDA team
strain A1, isozyme A1-III
-
-
Manually annotated by BRENDA team
; isolated from fermented brown seaweed with salted and fermented anchovy, sea mustard, Undaria pinnatifida
UniProt
Manually annotated by BRENDA team
Stenotrophomas maltophilia
-
UniProt
Manually annotated by BRENDA team
Stenotrophomas maltophilia KJ-2
-
UniProt
Manually annotated by BRENDA team
strain A5, isolated from banana rhizosphere
-
-
Manually annotated by BRENDA team
strain A5, isolated from banana rhizosphere
-
-
Manually annotated by BRENDA team
Streptomyces sp. ALG-5
-
-
-
Manually annotated by BRENDA team
2 isozymes
-
-
Manually annotated by BRENDA team
enzyme form SP2
-
-
Manually annotated by BRENDA team
isoenzyme SP1 and SP2
-
-
Manually annotated by BRENDA team
uncultured bacterium Alg-A
Alg-A
-
-
Manually annotated by BRENDA team
brown algae
-
-
Manually annotated by BRENDA team
strain ATCC 17749
-
-
Manually annotated by BRENDA team
; isoform A9mT; strain JAM-A9m
UniProt
Manually annotated by BRENDA team
gene alyVI
-
-
Manually annotated by BRENDA team
isoform A9mC; strain JAM-A9m
UniProt
Manually annotated by BRENDA team
isoform A9mL; strain JAM-A9m
UniProt
Manually annotated by BRENDA team
mutant strain 510-64. Alginate lyase activity was increased by 3.87fold over that of the parent strain
-
-
Manually annotated by BRENDA team
sequence contains a putative signal sequence of 23 amino acids
-
-
Manually annotated by BRENDA team
strain QY101
SwissProt
Manually annotated by BRENDA team
strain QY102
-
-
Manually annotated by BRENDA team
strain YWA
-
-
Manually annotated by BRENDA team
Vibrio sp. 510
-
-
-
Manually annotated by BRENDA team
sequence contains a putative signal sequence of 23 amino acids
-
-
Manually annotated by BRENDA team
Vibrio sp. JAM-A9m
isoform A9mC; strain JAM-A9m
UniProt
Manually annotated by BRENDA team
Vibrio sp. JAM-A9m
isoform A9mL; strain JAM-A9m
UniProt
Manually annotated by BRENDA team
Vibrio sp. JAM-A9m
isoform A9mT; strain JAM-A9m
UniProt
Manually annotated by BRENDA team
strain QY101
SwissProt
Manually annotated by BRENDA team
gene alyVI
-
-
Manually annotated by BRENDA team
strain YWA
-
-
Manually annotated by BRENDA team
Zobellia galactanivorans DSM 12802
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the polysaccharide-lyase-family 14, PL-14, primary structure analysis
evolution
-
AkAly28 and AkAly33 belong to polysaccharide lyase family 14, N-terminal and internal amino-acid sequences analysis, overview
evolution
-
AlyA belongs to the polysaccharide lyase family 7
evolution
-
N-terminal sequence analysis suggest that aly-SJ02 may be an alginate lyase of polysaccharide lyase family 18
evolution
-
sequence comparison of the PL-5 alginate lyase
evolution
AlgL belong to the polysaccharide family 5
evolution
the enzyme belongs to the the PL-17 family
evolution
-
the enzyme belongs to the to the polysaccharide lyase-7 family
evolution
the enzyme belongs to the family PL-14
evolution
AlyA5 belongs to the PL7 family, subfamily 5, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism
evolution
the enzyme belongs to the polysaccharide lyase PL7 family. Structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases, evolutionary relationships and structure-based hierarchy in the classification, overview
evolution
Klebsiella pneumoniae SM0524
-
AlyA belongs to the polysaccharide lyase family 7
-
evolution
-
N-terminal sequence analysis suggest that aly-SJ02 may be an alginate lyase of polysaccharide lyase family 18
-
evolution
Saccharophagus degradans DSM 17024
-
the enzyme belongs to the polysaccharide lyase PL7 family. Structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases, evolutionary relationships and structure-based hierarchy in the classification, overview
-
evolution
Zobellia galactanivorans DSM 12802
-
AlyA5 belongs to the PL7 family, subfamily 5, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism
-
malfunction
-
strains lacking alyA3 germinate poorly compared to wild type cells
metabolism
the enzyme is involved in the biosynthesis of alginate
metabolism
-
alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity, in vitro modeling, overview
physiological function
herbivorous marine gastropods such as abalone and sea hare ingest brown algae as a major diet and degrade the dietary alginate with alginate lyase in their digestive fluid
physiological function
-
the marine alginate lyase from Streptomyces sp. ALG-5 specifically degrades poly-G block of alginate
physiological function
-
AlgL serves to degrade mislocalized alginate that is trapped in the periplasmic space
physiological function
Streptomyces sp. ALG-5
-
the marine alginate lyase from Streptomyces sp. ALG-5 specifically degrades poly-G block of alginate
-
metabolism
-
AlgL is required for for alginate biosynthesis
additional information
-
structure-fucntion analysis, superposition of the open and closed lid loops suggests that the conformational change results in near-rigid-body motion, The open-closed movement of the lid loop decreases the accessible surface area by covering the active-site cleft., overview
additional information
-
homology modeling using structure of family 7 alginate lyase from Sphingomonas sp. A1, structure-affinity relationships of aliginate lyase alyVI with its substrate, molecular docking, molecular dynamics simulations and binding free energy calculations, overview. Residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues
additional information
secondary structure comparison of AlyA5 and AlyA1PL7
additional information
-
homology modeling using structure of family 7 alginate lyase from Sphingomonas sp. A1, structure-affinity relationships of aliginate lyase alyVI with its substrate, molecular docking, molecular dynamics simulations and binding free energy calculations, overview. Residues Asn138, Arg143, Asn217, and Lys308 are involved in the catalytic reaction, and van der Waals interactions are responsible for binding with the catalytic His200 and Tyr312 residues
-
additional information
Zobellia galactanivorans DSM 12802
-
secondary structure comparison of AlyA5 and AlyA1PL7
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-deoxy-l-erythro-hex-4-ene-pyranosyluronate-(mannuronate)2-mannuronic acid
?
show the reaction diagram
-
bound in the active cleft at subsites -3 to +1, the glycosidic linkage is cleaved existed between subsites -1 and +1
-
-
?
acetyl-beta1,4-D-mannuronic acid
?
show the reaction diagram
Azotobacter phage A22
-
-
-
-
?
acetylated poly-beta1,4-D-mannuronic acid
?
show the reaction diagram
endolytic activity
-
-
?
alginate
oligouronides
show the reaction diagram
-
-
-
?
alginate
oligouronides
show the reaction diagram
-
-
-
?
alginate
oligouronides
show the reaction diagram
-
-
-
?
alginate
oligouronides
show the reaction diagram
Azotobacter vinelandii phage
-
-
a series of oligouronides each containing a terminal 4-deoxy-alpha-L-erythrohex-4-enopyranuronosyl residue
?
alginate
oligouronides
show the reaction diagram
-
mannuronate blocks in alginate
-
?
alginate
oligouronides
show the reaction diagram
-
mannuronate blocks in alginate
-
?
alginate
oligouronides
show the reaction diagram
-
cleavage of mannuronate blocks in exo manner, 11fold preference for mannuronate blocks over guluronate blocks
-
?
alginate
oligouronides
show the reaction diagram
-
mannuronic acid-rich alginate, the degree of degradation of alginate is roughly proportional to the mannuronic acid content
-
?
alginate
oligouronides
show the reaction diagram
-
high-molecular weight alginate
-
?
alginate
oligouronides
show the reaction diagram
-
attacks preferentially mannuronate-rich moieties of the alginate molecule
-
?
alginate
oligouronides
show the reaction diagram
-
1,4-beta-D-mannuronan block regions of alginate
-
?
alginate
oligouronides
show the reaction diagram
-
dimeric through hexameric uronides possessing DELTA-4,5-unsaturated nonreducing terminal residues
-
?
alginate
oligouronides
show the reaction diagram
-
splits glycosidic bonds only between two mannuronic acid residues
-
?
alginate
oligouronides
show the reaction diagram
-
degradation of a greater percentage of the mannuronic acid-rich fractions than of glucuronic acid-rich fractions or the original alginate
-
?
alginate
oligouronides
show the reaction diagram
-
preferential splitting of the glycosidic bond between two mannuronide residues in the alginic acid
-
?
alginate
oligouronides
show the reaction diagram
alginate rich in mannuronic acids, the enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid bonds and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-beta-D-mannuronic acid bonds and alpha-L-guluronic acid-alpha-L-guluronic acid-bonds
-
?
alginate
oligouronides
show the reaction diagram
-
high affinity towards mannuronate-rich domains
-
?
alginate
oligouronides
show the reaction diagram
-
high affinity towards mannuronate-rich domains
unsaturated oligomers mostly composed of mannuronic acid as final product
?
alginate
oligouronides
show the reaction diagram
Bacillus sp. ATB-1015
-
-
-
?
alginate
oligosaccharides of 4-7 monomers
show the reaction diagram
-
substrate from brown algae Macrocystis pyrifera rich in polymannuronate and polyguluronate, cleavage sequences are G-/-MM and/or G-/-GM
-
?
alginate
?
show the reaction diagram
-
-
-
-
?
alginate
?
show the reaction diagram
-
-
-
-
?
alginate
?
show the reaction diagram
-
-
-
?
alginate
?
show the reaction diagram
-
-
-
?
alginate
?
show the reaction diagram
-
a heteropolysaccharides of alpha-L-guluronate and beta-D-mannuronate
-
-
?
alginate
?
show the reaction diagram
-
recombinant and native wild-type enzymes show similar activity levels
-
-
?
alginate
?
show the reaction diagram
-
substrate of alginate lyase isozymes A1-I, A1-II, and A1-III, incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III
-
-
?
alginate
?
show the reaction diagram
-
the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production
-
-
?
alginate
?
show the reaction diagram
-
Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58
-
-
?
alginate
?
show the reaction diagram
-
the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere)
-
-
?
alginate
?
show the reaction diagram
-
Atu3025 is an exotype family PL-15 alginate lyase
-
-
?
alginate
?
show the reaction diagram
can degrade alginate and mannuronate blocks, but hardly degrades guluronate blocks. In particular, AlgL can degrade acetylated alginate of Pseudomonas aeruginosa FRD1
-
-
?
alginate
?
show the reaction diagram
-
HdAlex can degrade not only unsaturated trisaccharide but also alginate and mannuronate-rich polymers. HdAlex degrades the alginate polymer in an exolytic manner
-
-
?
alginate
?
show the reaction diagram
-
substrate specificity for polyguluronate units in the alginate molecules
-
-
?
alginate
?
show the reaction diagram
-
the alginate lyase has the specificity for poly G block
-
-
?
alginate
?
show the reaction diagram
-
the enzyme is specific for hydrolyzing poly-beta-D-1,4-mannuronate in alginate
-
-
?
alginate
?
show the reaction diagram
-
highest activity toward poly(M)-rich substrate, moderate activity toward sodium alginate and weak activity toward poly(MG)-rich substrate, no activity toward poly (G)-rich substrate
major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides
-
?
alginate
?
show the reaction diagram
Agarivorans sp.
preferably degrades M blocks
-
-
?
alginate
?
show the reaction diagram
-
specific for cleaving at the beta-1,4 glycosidic bond between polyM and polyG blocks of sodium alginate, producing homopolymeric blocks of polyM and polyG. Enzyme is inefficient in the degradation of polyM and polyG
-
-
?
alginate
?
show the reaction diagram
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11
-
-
?
alginate
?
show the reaction diagram
-
AlgL lacks of stereospecificity, in that it is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate. The enzyme is able to remove the C5 proton from both mannuronate and guluronate, which are C5 epimers. Exhaustive digestion of alginate by AlgL generates dimeric and trimeric products, analysis by 1H NMR spectroscopy and mass spectrometry. AlgL operates as an exopolysaccharide lyase
-
-
?
alginate
?
show the reaction diagram
-
the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5
-
-
?
alginate
?
show the reaction diagram
Agrobacterium tumefaciens C58
-
Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58, Atu3025 is an exotype family PL-15 alginate lyase
-
-
?
alginate
?
show the reaction diagram
-
the enzyme is specific for hydrolyzing poly-beta-D-1,4-mannuronate in alginate
-
-
?
alginate
?
show the reaction diagram
Isoptericola halotolerans CGMCC5336
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11
-
-
?
alginate
?
show the reaction diagram
-
the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere), substrate specificity for polyguluronate units in the alginate molecules
-
-
?
alginate
?
show the reaction diagram
preferably degrades M blocks
-
-
?
alginate
oligosaccharides
show the reaction diagram
-
-
-
?
alginate
oligosaccharides
show the reaction diagram
-
-
-
?
alginate
oligosaccharides
show the reaction diagram
-
-
di-, tri-, tetra-, and pentasaccharide fragments
?
alginate
oligosaccharides
show the reaction diagram
a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
endolytic activity, intracellular isozymes also show hydrolase activity on alginate, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
Littorina sp., Dollabella auricola
-
endolytic activity, preference for M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
endolytic actvity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
endolyticc activity, enzyme prefers to cleave G-M and M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
enzyme prefers to cleave M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
isozyme A1-II and A1-I: endolytic cleavage of the glycosidic bonds, beta-elimination reaction, A1-II shows a preference for polyguluronate instead of polymannuronate
A1-I produces mainly di- and trisaccharides, A1-II produces mainly tri- and tetrasaccharides
?
alginate
oligosaccharides
show the reaction diagram
-
isozyme A1-II performs endolytic cleavage of the glycosidic bonds, beta-elimination reaction, and shows a preference for polyguluronate instead of polymannuronate
isozyme A1-II produces mainly tri- and tetrasaccharides
?
alginate
oligosaccharides
show the reaction diagram
-
weak activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
AlgL plays a main role in alginate depolymerization
-
?
alginate
oligosaccharides
show the reaction diagram
-
increased expression of alginate lyase in mucoid strain 8830 leads to alginate degradation and increased cell detachment. When expressed from a regulated promoter, the alginate lyase can induce enhanced sloughing of cells because of degradation of the alginate. Possible role for lyase in the development of bacterial growth films
-
?
alginate
oligosaccharides
show the reaction diagram
-
the biological function of AlgL to degrade alginates that fail to become exported out of the cell and thereby become stranded in the periplasmic space. At high levels of alginate synthesis in the absence of AlgL, such stranded polymers may accumulate in the periplasm to such an extent that the integrity of the cell is lost, leading to toxic effects
-
?
alginate
oligosaccharides
show the reaction diagram
-
the enzyme is involved in alginate production
-
?
alginate
oligosaccharides
show the reaction diagram
-
Arg146, Gln189, His191, and Tyr284 form an active center
-
?
alginate
oligosaccharides
show the reaction diagram
enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-alpha-L-guluronic acid or alpha-L-guluronic acid-beta-D-mannuronic acid bonds
-
?
alginate
oligosaccharides
show the reaction diagram
-
protein PA1167 acts preferably on heteropolymeric regions endolytically
-
?
alginate
oligosaccharides
show the reaction diagram
enzyme lyase appears to be poly-guluronate lyase degrading poly-G block preferentially than poly-M block. The degraded products are determined to be di-, tri-, tetra- and pentasaccharides
-
?
alginate
oligosaccharides
show the reaction diagram
Bacillus sp. ATB-1015
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview, a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Vibrio sp. 510
-
-
di-, tri-, tetra-, and pentasaccharide fragments
?
alginate
oligosaccharides
show the reaction diagram
Pseudomonas alginovora XO17
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview, a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Alteromonas sp. H-4
endolytic activity, intracellular isozymes also show hydrolase activity on alginate, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview, a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Photobacterium sp. ATCC 43367 Alg-A
-
endolytic actvity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview, a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Pseudomonas aeruginosa AlgL
-
AlgL plays a main role in alginate depolymerization, protein PA1167 acts preferably on heteropolymeric regions endolytically
-
?
alginate
oligosaccharides
show the reaction diagram
Pseudomonas aeruginosa FRDI
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
oligosaccharides
show the reaction diagram
Azotobacter chroococcum 4A1M
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated disaccharides + unsaturated trisaccharides
show the reaction diagram
-
main products
?
alginate
algino-oligosaccharide
show the reaction diagram
-
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
Agarivorans sp.
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
when alginate is added at an initial concentration of more than 0.8%, the maximal degradation rate of alginate is obtained
-
?
alginate
algino-oligosaccharide
show the reaction diagram
isoform A9mT favorably degrades mannuronate polymer in alginate, the relative activities for alginate, beta-D-mannuronic acid, 1,4 linked alpha-L-guluronic acid, and 1,4 linked alpha-L-guluronic acid/beta-D-mannuronic acid blocks are 100%, 75%, 21%, and 15%, respectively, under the standard assay conditions at pH 7.5
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
isoforms AlyA1, AlyA2, and AlyA3 preferably cleave the bond between guluronic acid and mannuronic acid, resulting in a guluronic acid residue at the new reducing end, but isoform AlyA3 also degrades the other three possible bonds in alginate
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
recombinant Aly has the capacity to degrade alginate components for protoplast isolation
-
?
alginate
algino-oligosaccharide
show the reaction diagram
Agarivorans sp.
the enzyme degrades alginate by endo fashion, the enzyme degrades favorably mannuronate-guluronate and guluronate-rich fragments in alginate, shows substrate specificity toward beta-D-mannuronic acid blocks of hydrolysed alginate
4-deoxy-L-erythro-hex-4-enopyranosyluronic acids as the non-reducing terminal moiety are contained in the products
?
alginate
algino-oligosaccharide
show the reaction diagram
-
the enzyme preferably degrades poly-beta-D-mannuronic acid-rich substrate, is also able to degrade poly-beta-D-mannuronic acid/poly-alpha-L-guluronic acid block but hardly poly-alpha-L-guluronic acid block
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
?
alginate
algino-oligosaccharide
show the reaction diagram
isoform A9mT favorably degrades mannuronate polymer in alginate, the relative activities for alginate, beta-D-mannuronic acid, 1,4 linked alpha-L-guluronic acid, and 1,4 linked alpha-L-guluronic acid/beta-D-mannuronic acid blocks are 100%, 75%, 21%, and 15%, respectively, under the standard assay conditions at pH 7.5
-
?
alginate
algino-oligosaccharide
show the reaction diagram
-
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
Vibrio sp. JAM-A9m
isoform A9mT favorably degrades mannuronate polymer in alginate, the relative activities for alginate, beta-D-mannuronic acid, 1,4 linked alpha-L-guluronic acid, and 1,4 linked alpha-L-guluronic acid/beta-D-mannuronic acid blocks are 100%, 75%, 21%, and 15%, respectively, under the standard assay conditions at pH 7.5
-
?
alginate
algino-oligosaccharide
show the reaction diagram
Vibrio sp. JAM-A9m
-
-
?
alginate
algino-oligosaccharide
show the reaction diagram
Pseudoalteromonas atlantica AR06
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
?
alginate
algino-oligosaccharide
show the reaction diagram
the enzyme degrades alginate by endo fashion, the enzyme degrades favorably mannuronate-guluronate and guluronate-rich fragments in alginate, shows substrate specificity toward beta-D-mannuronic acid blocks of hydrolysed alginate
4-deoxy-L-erythro-hex-4-enopyranosyluronic acids as the non-reducing terminal moiety are contained in the products
?
alginate
algino-oligosaccharide
show the reaction diagram
-
-
?
alginate
algino-oligosaccharides
show the reaction diagram
-
-
-
?
alginate
algino-monosaccharides
show the reaction diagram
ATU3025 acts on alginate polysaccharides and oligosaccharides exolytically and releases unsaturated monosaccharides from the substrate terminal
-
?
alginic acid
?
show the reaction diagram
-
-
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
-
-
-
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
-
-
enzyme shows activities toward both polyG, i.e.alpha-L-guluronic acid, and polyM, i.e. beta-D-mannuronic acid
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
-
-
products are six different di-and trisaccharides. The enzymatic hydrolysis occurs between two random guluronic acid or/and mannuronic acid residues, and produces one G residue or M residue on the reducing end and an unsaturated residue on the non-reducing end for all products
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
-
alginate lyases A and B have the activities for both M and G blocks. For isoform A, the enzyme activity acting on M block is much more than that of G block, for alginate lyase B, the enzyme activity on M block is slightly higher than that on G block and there is no obvious substrate specificity difference between them
-
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
-
-
enzyme shows activities toward both polyG, i.e.alpha-L-guluronic acid, and polyM, i.e. beta-D-mannuronic acid
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
Pseudomonas sp. HZJ 216
-
-
products are six different di-and trisaccharides. The enzymatic hydrolysis occurs between two random guluronic acid or/and mannuronic acid residues, and produces one G residue or M residue on the reducing end and an unsaturated residue on the non-reducing end for all products
-
?
alpha-L-mannuronyl linkage in alginate
?
show the reaction diagram
Pseudomonas fluorescens HZJ216
-
alginate lyases A and B have the activities for both M and G blocks. For isoform A, the enzyme activity acting on M block is much more than that of G block, for alginate lyase B, the enzyme activity on M block is slightly higher than that on G block and there is no obvious substrate specificity difference between them
-
-
?
beta-D-mannuronyl linkage in alginate
?
show the reaction diagram
-
final degradation products are alginate monosaccharides
-
?
beta-D-mannuronyl linkage in alginate
?
show the reaction diagram
preferably degrades the M block over the G block in alginate
-
-
?
beta-D-mannuronyl linkage in alginate
?
show the reaction diagram
-
final degradation products are alginate monosaccharides
-
?
beta-D-mannuronyl linkage in alginate
?
show the reaction diagram
Vibrio sp. A9m, Vibrio sp. JAM-A9m
preferably degrades the M block over the G block in alginate
-
-
?
beta-D-mannuronyl linkage in alginate
?
show the reaction diagram
Vibrio sp. JAM-A9m
preferably degrades the M block over the G block in alginate
-
-
?
deacetylated polymannuronic acid
?
show the reaction diagram
-
-
-
?
disaccharides of alginate
monosacchrides
show the reaction diagram
-
oligoalginate lyase, oligoalginate lyase, complete depolymerization of alginate
-
?
G-alginate
?
show the reaction diagram
-
purified alpha-L-guluronic acid blocks containing more than 90% alpha-L-guluronic acid
-
-
?
hepta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
hepta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
hepta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
hepta-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
hepta-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
hexa-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
hexa-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
hexa-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
hexa-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
Pseudoalteromonas sp. 272
-
-
-
?
hexa-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
hexa-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
M-alginate
?
show the reaction diagram
-
pure 1-4-linked beta-D-mannuronic acid
-
-
?
nona-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
nona-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
octa-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
octa-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
oligomannuronate
?
show the reaction diagram
Pseudomonas aeruginosa, Pseudomonas aeruginosa CF1/M1
-
hexameric oligomannuronate is the preferred substrate, pentameric oligomannuronates are still accepted, no activity with oligomers shorter than pentamer
-
-
?
penta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
penta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
penta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
penta-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
Pseudoalteromonas sp. 272
-
-
-
?
penta-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
penta-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
poly alpha-L-guluronate
oligo-alpha-1,4-L-guluronate
show the reaction diagram
-
-
-
?
poly beta-D-mannuronate
oligo-beta-1,4-D-mannuronate
show the reaction diagram
-
-
-
?
poly(beta-(1->4)-D-mannuronate)
?
show the reaction diagram
-
-
-
-
?
poly(beta-(1->4)-D-mannuronate)
?
show the reaction diagram
-
-
-
-
-
poly(beta-(1->4)-D-mannuronate)
?
show the reaction diagram
Pseudomonas fluorescens HZJ216
-
-
-
-
?
poly(beta-(1->4)-D-mannuronic acid)
?
show the reaction diagram
190% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
show the reaction diagram
alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. 120% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-L-guluronic acid)
?
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae SM0524
-
alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. In wild-type, ratio of activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) to poly(alpha-L-guluronic acid) is 1.2
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
-
-
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
Agarivorans sp.
-
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
AB489222
-
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
-
about 30% activity compared to alginate
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
the region including T121 of LbAly28 is the recognition of poly(MG) region of alginate
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
-
about 30% activity compared to alginate
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
Isoptericola halotolerans CGMCC5336
AB489222
-
-
-
?
poly(beta-D-mannuronate)
?
show the reaction diagram
-
-
-
?
poly(beta-D-manuronate)
?
show the reaction diagram
-
-
-
?
poly(beta-D-manuronate)
?
show the reaction diagram
AlyDW11 prefers poly(beta-D-mannuronate) as a substrate over poly(alpha-L-guluronate)
-
-
?
poly(beta-D-manuronate)
?
show the reaction diagram
Zobellia galactanivorans DSM 12802
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
show the reaction diagram
Pseudomonas putida, Azotobacter vinelandii phage, Stenotrophomonas maltophilia
-
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
show the reaction diagram
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
show the reaction diagram
Azotobacter phage A31
-
-
-
-
?
poly-alpha-L-guluronate
?
show the reaction diagram
14.9% of the activity with poly-beta-D-mannuronate
-
-
?
poly-alpha-L-guluronic acid
?
show the reaction diagram
-
-
-
-
?
poly-alpha1,4-L-guluronic acid
alpha-D-glucuronate
show the reaction diagram
Pseudoalteromonas sp., Pseudoalteromonas sp. 272
-
-
-
?
poly-alpha1,4-L-guluronic acid
alpha-L-guluronate
show the reaction diagram
-
-
-
?
poly-alpha1,4-L-guluronic acid
alpha-L-guluronate
show the reaction diagram
-
-
?
poly-alpha1,4-L-guluronic acid
alpha-L-guluronate
show the reaction diagram
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase, preference for
-
?
poly-alpha1,4-L-guluronic acid
alpha-L-guluronate
show the reaction diagram
-
weak activity in strain 1351
-
?
poly-alpha1,4-L-guluronic acid
alpha-L-guluronate
show the reaction diagram
Bacillus sp. ATB-1015
-
-
-
?
poly-alpha1,4-L-guluronic acid
alpha-L-guluronate
show the reaction diagram
Pseudoalteromonas sp. 272
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase, preference for
-
?
poly-alpha1,4-L-guluronic acid
?
show the reaction diagram
-
competitive to poly-beta1,4-D-mannuronic acid
-
-
?
poly-alpha1,4-L-guluronic acid
?
show the reaction diagram
endolytic activity, extra- and intracellular isozymes
-
-
?
poly-beta-1,4-D-mannuronate
4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid
show the reaction diagram
-
-
-
?
poly-beta-D-mannuronate
oligomannuronate
show the reaction diagram
-
i.e. alginate, cleavage site structure
-
?
poly-beta-D-mannuronate
?
show the reaction diagram
-
-
-
?
poly-beta-D-mannuronate
?
show the reaction diagram
-
poly-beta-D-mannuronate can be much more easily hydrolyzed by the displayed alginate lyase than poly-alpha-L-guluronic acid and sodium alginate
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
show the reaction diagram
-
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
show the reaction diagram
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
show the reaction diagram
Pseudoalteromonas sp. 272
-
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
show the reaction diagram
Pseudoalteromonas atlantica AR06
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
weak activity
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
low activity
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
deacetylated
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
endolytic activity
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
endolytic activity
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
nonacetylated
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
Littorina sp., Dollabella auricola
-
preference for M-M linkages
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
-
strain JBH2: deacetylated
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
Bacillus sp. ATB-1015
-
deacetylated
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
Pseudomonas alginovora XO17
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
Photobacterium sp. ATCC 43367 Alg-A
-
-
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
Pseudoalteromonas sp. 272
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase
-
?
poly-beta1,4-D-mannuronic acid
beta-D-mannuronate
show the reaction diagram
Pseudomonas aeruginosa FRDI
nonacetylated
-
?
poly-beta1,4-D-mannuronic acid
?
show the reaction diagram
-
competitive to poly-alpha1,4L-guluronic acid
-
-
?
poly-beta1,4-D-mannuronic acid
?
show the reaction diagram
Alteromonas sp., Alteromonas sp. H-4
endolytic activity, extra- and intracellular isozymes
-
-
?
polyguluronan
?
show the reaction diagram
-
70% of the activity with polymannuronan
-
-
?
polymannuronan
?
show the reaction diagram
-
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
show the reaction diagram
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
show the reaction diagram
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
show the reaction diagram
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
show the reaction diagram
-
-
production of a wide range of 4,5-unsaturated oligomannuronic acids, that are further degraded to unsaturated monomer and dimer as final products
?
polymannuronate
4,5-unsaturated oligomannuronic acids
show the reaction diagram
Bacillus sp. ATB-1015
-
-
-
?
polymannuronide
?
show the reaction diagram
-
-
-
-
?
sodium alginate
?
show the reaction diagram
-
-
-
?
sodium alginate
?
show the reaction diagram
-
-
-
?
sodium alginate
?
show the reaction diagram
-
high activity
-
-
?
sodium alginate
?
show the reaction diagram
-
endo-type manner
-
-
?
sodium alginate
?
show the reaction diagram
AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11
-
-
?
sodium alginate
?
show the reaction diagram
brown seaweed alginate (BSWA) as model substrate or baterial alginate purified from the mucoid Pseudomonas aeruginosa clinical isolate FRD1
-
-
?
sodium alginate
?
show the reaction diagram
LC mass and NMR spectrometris product analysis
-
-
?
sodium alginate
?
show the reaction diagram
profiles of alginate oligomers are obtained by digestion of alginate with an alginate lyase AlyDW11, overview. The enzyme has endolytic activity and prefers poly(beta-D-mannuronate) over poly(alpha-L-guluronate)
-
-
?
sodium alginate
?
show the reaction diagram
-
high activity
-
-
?
sodium alginate
?
show the reaction diagram
Zobellia galactanivorans DSM 12802
AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11, LC mass and NMR spectrometris product analysis
-
-
?
sodium alginate
?
show the reaction diagram
Saccharophagus degradans DSM 17024
-
-
-
?
tetra-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
tetra-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
tetra-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
-
-
-
?
tetra-alpha1,4-L-guluronic acid
L-guluronic acid
show the reaction diagram
Pseudoalteromonas sp. 272
-
-
-
?
tetra-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
tetra-beta1,4-D-mannuronic acid
D-mannuronic acid
show the reaction diagram
-
-
-
?
trisaccharides of alginate
monosacchrides
show the reaction diagram
-
oligoalginate lyase, oligoalginate lyase, complete depolymerization of alginate
-
?
MG-alginate
?
show the reaction diagram
-
alginate epimerized by AlgE4 and containing 47% alpha-L-guluronic acid with no alpha-L-guluronic acid blocks, 100% activity
isoforms AlyA1, AlyA2, and AlyA3 produce mainly DELTAG and DELTAGMG as their end products, isoform AlyA3 produces as many trimers as it does dimers and tetramers
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
assay methods, overview
-
-
?
additional information
?
-
-
assay methods, overview
-
-
?
additional information
?
-
assay methods, overview
-
-
?
additional information
?
-
-
assay methods, overview
-
-
?
additional information
?
-
assay methods, overview
-
-
?
additional information
?
-
assay methods, overview, cleaves M-M and M-G linkages, but not G-GM linkages
-
-
?
additional information
?
-
assay methods, overview, enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages
-
-
?
additional information
?
-
cleaves G-MM and G-GM linkages, but nt G-GM linkages
-
-
?
additional information
?
-
Bacillus circulans, Azotobacter vinelandii phage
-
endolytic activity
-
-
?
additional information
?
-
-
endolytic activity, the enzyme possesses 5 subsites in its catalytic center, assay methods, overview
-
-
?
additional information
?
-
enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages
-
-
?
additional information
?
-
no activity with chitin, chitosan, cellulose, and pectin
-
-
?
additional information
?
-
-
no activity with gellan, xanthan, and pectin of A1-I and A1-II
-
-
?
additional information
?
-
-
no activity with triguluronate and trimannuronate, but with tetramers or substrates with longer chain length
-
-
?
additional information
?
-
-
oligoalginate lyase substrate specificity
-
-
?
additional information
?
-
-
preference of M-MM or MM-M cleavage sequences
-
-
?
additional information
?
-
substrate specificity, residues His204 and Trp207 are critical for enzyme activity
-
-
?
additional information
?
-
the enzyme from strain H-4 shows multiple substrate specificities, assay methods, overview
-
-
?
additional information
?
-
-
the enzyme possesses 5 subsites in its catalytic center, assay methods, overview
-
-
?
additional information
?
-
-
induced by native alginate
-
-
-
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme
-
-
?
additional information
?
-
Azotobacter phage A31, Azotobacter phage A22, Asteromyces cruciatus, Corollospora intermedia, Paradendryphiella arenariae
-
biological function of the enzyme
-
-
?
additional information
?
-
biological function of the enzyme, Pseudomonas aeruginosa produces a bacterial alginate which seems to be necessary for cell attachment to the capsule-like biofilm build in lung of infected humans suffering cystic fibrosis
-
-
?
additional information
?
-
A1-1V' has no significant role in alginate metabolism
-
-
-
additional information
?
-
-
activity of AlgL is required for alginate production
-
-
-
additional information
?
-
-
alginate-lyase is not essential for the production of alginate. When this enzyme is present, as in wild-type cells of Azotobacter vinelandii, its role is restricted to a post-polymerization step, with its activity reaching a maximum in the pres-stationary phase of growth
-
-
-
additional information
?
-
the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm, AlgL is a vital part of the alginate transport scaffold, as well as having a role in degrading alginate as a lyase
-
-
-
additional information
?
-
AlgL is an alginate lyase that can degrade newly formed alginate polymers. Mutants of strain FRD1 defective in one of several periplasmic proteins, AlgKGX, for alginate secretion release alginate fragments due to the activity of an alginate lyase in the periplasm, which cleaves the newly formed polymers, overview. AlgK, AlgG, AlgX and AlgL may form a periplasmic scaffold to bring newly synthesized polymers to the outer-membrane porin, AlgE, and protect the polymer from degradation by AlgL
-
-
-
additional information
?
-
-
treatment of the supermucoid biofilm of the supermucoid Pseudomonas aeruginosa strain PDO300DELTAalg8(pBBR1MCS-5:alg8) with alginate lyase results in the breakdown of the microcolony structure, but this treatment had little effect on the mucoid and nonmucoid biofilms
-
-
-
additional information
?
-
-
AkAly28 hardly degrades oligosaccharides smaller than tetrasaccharide, while AkAly33 degrades oligosaccharides larger than disaccharide producing disaccharide and 2-keto-3-deoxy-gluconaldehyde, substrate specificities, production of oligosaccharides, analysis by anion-exchange chromatography, overview
-
-
-
additional information
?
-
-
alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG
-
-
-
additional information
?
-
-
alginate lyase A degrades M and G blocks, and the enzyme activity acting on M block is much more than that of G block, while for alginate lyase B, the enzyme activities on M block are slightly higher than that of G block
-
-
-
additional information
?
-
-
alginate lyases degrade the polysaccharide by cleaving the glycosidic linkages through a beta-elimination reaction. Lyase AlyA is bifunctional and shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). AlyA is endolytic, acting on G-blocks and MG-blocks where G-M linkages are cleaved in the latter substrate. Substrate specificities of diverse enzyme mutants, overview
-
-
-
additional information
?
-
-
enzymatic depolymerization of sodium alginate, the enzyme shows specificity for cleaving at the beta-1,4 glycosidic bond between polyM and polyG blocks of sodium alginate
-
-
-
additional information
?
-
-
preferably degrades poly(M)-rich substrate and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly33 degrades poly(M)-rich substrate into various sizes of oligosaccharides in the reaction time up to 1 h and further degrades the thus formed oligosaccharides to disaccharide and monosaccharide such as alpha-keto acid in the reaction time 2-6 h
-
-
-
additional information
?
-
-
preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation
major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides
-
-
additional information
?
-
-
preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly28 hardly degrades oligosaccharides smaller than tetrasaccharide
-
-
-
additional information
?
-
substrate is sodium alginate originating from Macrocystis pyrifera, preparation of poly(M)-rich, poly(G)-rich, and random substrates thereof
-
-
-
additional information
?
-
substrate specificity of recombinant oligoalginate lyase, overview. Analysis of the final degradation products, overview
-
-
-
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
-
additional information
?
-
-
alginate lyase A1-III is a beta-D-mannuronosyl linkage-specific enzyme that acts on alginate tetrasaccharide as the minimum substrate and produces disaccharides and trisaccharides from alginate
-
-
-
additional information
?
-
-
alginate lyase AlgL catalyzes the cleavage of the polysaccharide alginate through a beta-elimination reaction. AlgL operates preferentially on non-acetylated alginate or its precursor mannuronan. AlgL operates as an exopolysaccharide lyase
-
-
-
additional information
?
-
AlgL is a poly-(beta-D-mannuronate) lyase that preferentially degrades deacetylated polymannuronate via a beta-elimination reaction, resulting in an unsaturated uronic acid at the nonreducing end of the molecule
-
-
-
additional information
?
-
Stenotrophomas maltophilia
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
-
-
-
additional information
?
-
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview
-
-
-
additional information
?
-
the enzyme is an endolytic polymannuronate lyase
-
-
-
additional information
?
-
Stenotrophomas maltophilia
alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.11, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin
-
-
-
additional information
?
-
AlgL is an endolytic enzyme that cleaves the 1-4 glycosidic linkage, resulting in disaccharides and trisaccharides as its major products. Several residues, including His202 and Tyr256, play a role in AlgL activity
-
-
-
additional information
?
-
-
AlyV5 shows activities towards both polyguluronate and polymannuronate, but degrades the former more efficiently. AlyV5 mainly produces disaccharide, trisaccharide and tetrasaccharide from polyguluronate, trisaccharide, tetrasaccharide and pentasaccharide from polymannuronate
-
-
-
additional information
?
-
-
hydrolysis of the crude alginate since beta-elimination on beta-D-mannuronosyluronate or on alpha-L-gulupyranosyluronate produces, in both cases, the nonreducing end 4-deoxy-L-erythro-hex-4-enepyranosyluronate. Products are mainly trisaccharides, followed by tetrasaccharides, disaccharides, and pentasaccharides in descending order, gel filtration, and mass and NMR spectrometric analyses, overview
-
-
-
additional information
?
-
recombinant Alg17C preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid. The enzyme can produce a monomeric sugar acid from alginate by the concerted action of an endo-type alginate lyase and exo-type alginate lyase Alg17C, substrate specificity of Alg17C, overview
-
-
-
additional information
?
-
substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms
-
-
-
additional information
?
-
-
substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms
-
-
-
additional information
?
-
the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure
-
-
-
additional information
?
-
-
the enzyme is active on poly(beta-D-mannuronate) and poly(alpha-L-guluronate), cf. EC 4.2.2.11
-
-
-
additional information
?
-
the enzyme is active on poly-MM, poly-GG, and poly-MG substrates. Exolytic depolymerization of these polysaccharides by alginate lyase yields a monosaccharide and a product containing a DELTA-(4,5)-unsaturated uronic acid moiety. A mixture of alginate di-, tri-, and tetrasaccharides are processed into mono- and disaccharides in the presence of Alg17c. An alginate trisaccharide represents the minimal length substrate for Alg17c, complete processing only of the tri- and tetrasaccharide substrates, substrate specificity and binding structure, Fourier electron density map, overview
-
-
-
additional information
?
-
-
no activity with triguluronate and trimannuronate, but with tetramers or substrates with longer chain length
-
-
?
additional information
?
-
Bacillus sp. ATB-1015
-
biological function of the enzyme
-
-
?
additional information
?
-
substrate specificity of recombinant oligoalginate lyase, overview. Analysis of the final degradation products, overview
-
-
-
additional information
?
-
Stenotrophomas maltophilia KJ-2
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage, alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.11, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin
-
-
-
additional information
?
-
Pseudomonas alginovora XO17
biological function of the enzyme
-
-
?
additional information
?
-
Alteromonas sp. H-4
the enzyme from strain H-4 shows multiple substrate specificities, assay methods, overview, biological function of the enzyme
-
-
?
additional information
?
-
-
AlyV5 shows activities towards both polyguluronate and polymannuronate, but degrades the former more efficiently. AlyV5 mainly produces disaccharide, trisaccharide and tetrasaccharide from polyguluronate, trisaccharide, tetrasaccharide and pentasaccharide from polymannuronate
-
-
-
additional information
?
-
Photobacterium sp. ATCC 43367 Alg-A
-
preference of M-MM or MM-M cleavage sequences, biological function of the enzyme
-
-
?
additional information
?
-
-
alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG
-
-
-
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
-
additional information
?
-
Klebsiella pneumoniae SM0524
-
alginate lyases degrade the polysaccharide by cleaving the glycosidic linkages through a beta-elimination reaction. Lyase AlyA is bifunctional and shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). AlyA is endolytic, acting on G-blocks and MG-blocks where G-M linkages are cleaved in the latter substrate. Substrate specificities of diverse enzyme mutants, overview
-
-
-
additional information
?
-
Vibrio sp. JAM-A9m
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
-
additional information
?
-
Pseudomonas alginovora X017
-
hydrolysis of the crude alginate since beta-elimination on beta-D-mannuronosyluronate or on alpha-L-gulupyranosyluronate produces, in both cases, the nonreducing end 4-deoxy-L-erythro-hex-4-enepyranosyluronate. Products are mainly trisaccharides, followed by tetrasaccharides, disaccharides, and pentasaccharides in descending order, gel filtration, and mass and NMR spectrometric analyses, overview
-
-
-
additional information
?
-
Zobellia galactanivorans DSM 12802
the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure
-
-
-
additional information
?
-
Saccharophagus degradans DSM 17024
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview, the enzyme is active on poly-MM, poly-GG, and poly-MG substrates. Exolytic depolymerization of these polysaccharides by alginate lyase yields a monosaccharide and a product containing a DELTA-(4,5)-unsaturated uronic acid moiety. A mixture of alginate di-, tri-, and tetrasaccharides are processed into mono- and disaccharides in the presence of Alg17c. An alginate trisaccharide represents the minimal length substrate for Alg17c, complete processing only of the tri- and tetrasaccharide substrates, substrate specificity and binding structure, Fourier electron density map, overview
-
-
-
additional information
?
-
Pseudomonas aeruginosa FRDI
assay methods, overview, enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages, enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages, biological function of the enzyme, Pseudomonas aeruginosa produces a bacterial alginate which seems to be necessary for cell attachment to the capsule-like biofilm build in lung of infected humans suffering cystic fibrosis
-
-
?
additional information
?
-
Azotobacter chroococcum 4A1M
-
assay methods, overview, biological function of the enzyme
-
-
?
additional information
?
-
Pseudomonas fluorescens HZJ216
-
alginate lyase A degrades M and G blocks, and the enzyme activity acting on M block is much more than that of G block, while for alginate lyase B, the enzyme activities on M block are slightly higher than that of G block
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-beta1,4-D-mannuronic acid
?
show the reaction diagram
Azotobacter phage A22
-
-
-
-
?
alginate
?
show the reaction diagram
-
incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III
-
-
?
alginate
?
show the reaction diagram
-
the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production
-
-
?
alginate
?
show the reaction diagram
-
Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58
-
-
?
alginate
?
show the reaction diagram
-
the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere)
-
-
?
alginate
?
show the reaction diagram
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11
-
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Q06749
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
O52195, Q9ZFG9
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
O50660
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Q9Z6D6
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Q06749
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Q9QT64
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Q59639
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
P39049
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Q9ZNB7
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
O52195, Q9ZFG9
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
-
AlgL plays a main role in alginate depolymerization
-
?
alginate
oligosaccharides
show the reaction diagram
-
increased expression of alginate lyase in mucoid strain 8830 leads to alginate degradation and increased cell detachment. When expressed from a regulated promoter, the alginate lyase can induce enhanced sloughing of cells because of degradation of the alginate. Possible role for lyase in the development of bacterial growth films
-
?
alginate
oligosaccharides
show the reaction diagram
-
the biological function of AlgL to degrade alginates that fail to become exported out of the cell and thereby become stranded in the periplasmic space. At high levels of alginate synthesis in the absence of AlgL, such stranded polymers may accumulate in the periplasm to such an extent that the integrity of the cell is lost, leading to toxic effects
-
?
alginate
oligosaccharides
show the reaction diagram
-
the enzyme is involved in alginate production
-
?
alginate
oligosaccharides
show the reaction diagram
Bacillus sp. ATB-1015
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Pseudomonas alginovora XO17
Q59639
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Alteromonas sp. H-4
Q9Z6D6
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
oligosaccharides
show the reaction diagram
Photobacterium sp. ATCC 43367 Alg-A
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
?
show the reaction diagram
Agrobacterium tumefaciens C58
-
Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58
-
-
?
alginate
?
show the reaction diagram
Isoptericola halotolerans CGMCC5336
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11
-
-
?
alginate
oligosaccharides
show the reaction diagram
Pseudomonas aeruginosa AlgL
-
AlgL plays a main role in alginate depolymerization
-
?
alginate
?
show the reaction diagram
-
the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere)
-
-
?
alginate
oligosaccharides
show the reaction diagram
Azotobacter chroococcum 4A1M
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
sodium alginate
?
show the reaction diagram
Q59478
-
-
-
?
sodium alginate
?
show the reaction diagram
Zobellia galactanivorans, Zobellia galactanivorans DSM 12802
G0L2Y1
AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11
-
-
?
trisaccharides of alginate
monosacchrides
show the reaction diagram
-
oligoalginate lyase, complete depolymerization of alginate
-
?
disaccharides of alginate
monosacchrides
show the reaction diagram
-
oligoalginate lyase, complete depolymerization of alginate
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
induced by native alginate
-
-
-
additional information
?
-
O50660
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
Q9Z6D6
biological function of the enzyme
-
-
?
additional information
?
-
Q9QT64
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
Q59639
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
P39049
biological function of the enzyme
-
-
?
additional information
?
-
Q9ZNB7
biological function of the enzyme
-
-
?
additional information
?
-
-
biological function of the enzyme
-
-
?
additional information
?
-
O52195, Q9ZFG9
biological function of the enzyme
-
-
?
additional information
?
-
Azotobacter phage A31, Azotobacter phage A22, Asteromyces cruciatus, Corollospora intermedia, Paradendryphiella arenariae
-
biological function of the enzyme
-
-
?
additional information
?
-
Q06749
biological function of the enzyme, Pseudomonas aeruginosa produces a bacterial alginate which seems to be necessary for cell attachment to the capsule-like biofilm build in lung of infected humans suffering cystic fibrosis
-
-
?
additional information
?
-
Q5DWP2
A1-1V' has no significant role in alginate metabolism
-
-
-
additional information
?
-
-
activity of AlgL is required for alginate production
-
-
-
additional information
?
-
-
alginate-lyase is not essential for the production of alginate. When this enzyme is present, as in wild-type cells of Azotobacter vinelandii, its role is restricted to a post-polymerization step, with its activity reaching a maximum in the pres-stationary phase of growth
-
-
-
additional information
?
-
Q06749
the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm, AlgL is a vital part of the alginate transport scaffold, as well as having a role in degrading alginate as a lyase
-
-
-
additional information
?
-
Q06749
AlgL is an alginate lyase that can degrade newly formed alginate polymers. Mutants of strain FRD1 defective in one of several periplasmic proteins, AlgKGX, for alginate secretion release alginate fragments due to the activity of an alginate lyase in the periplasm, which cleaves the newly formed polymers, overview. AlgK, AlgG, AlgX and AlgL may form a periplasmic scaffold to bring newly synthesized polymers to the outer-membrane porin, AlgE, and protect the polymer from degradation by AlgL
-
-
-
additional information
?
-
-
AkAly28 hardly degrades oligosaccharides smaller than tetrasaccharide, while AkAly33 degrades oligosaccharides larger than disaccharide producing disaccharide and 2-keto-3-deoxy-gluconaldehyde, substrate specificities, production of oligosaccharides, analysis by anion-exchange chromatography, overview
-
-
-
additional information
?
-
-
alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG
-
-
-
additional information
?
-
-
alginate lyase A degrades M and G blocks, and the enzyme activity acting on M block is much more than that of G block, while for alginate lyase B, the enzyme activities on M block are slightly higher than that of G block
-
-
-
additional information
?
-
-
alginate lyases degrade the polysaccharide by cleaving the glycosidic linkages through a beta-elimination reaction. Lyase AlyA is bifunctional and shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). AlyA is endolytic, acting on G-blocks and MG-blocks where G-M linkages are cleaved in the latter substrate. Substrate specificities of diverse enzyme mutants, overview
-
-
-
additional information
?
-
-
enzymatic depolymerization of sodium alginate, the enzyme shows specificity for cleaving at the beta-1,4 glycosidic bond between polyM and polyG blocks of sodium alginate
-
-
-
additional information
?
-
-
preferably degrades poly(M)-rich substrate and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly33 degrades poly(M)-rich substrate into various sizes of oligosaccharides in the reaction time up to 1 h and further degrades the thus formed oligosaccharides to disaccharide and monosaccharide such as alpha-keto acid in the reaction time 2-6 h
-
-
-
additional information
?
-
-
preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation
major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides
-
-
additional information
?
-
-
alginate lyase A1-III is a beta-D-mannuronosyl linkage-specific enzyme that acts on alginate tetrasaccharide as the minimum substrate and produces disaccharides and trisaccharides from alginate
-
-
-
additional information
?
-
-
alginate lyase AlgL catalyzes the cleavage of the polysaccharide alginate through a beta-elimination reaction. AlgL operates preferentially on non-acetylated alginate or its precursor mannuronan. AlgL operates as an exopolysaccharide lyase
-
-
-
additional information
?
-
Q06749
AlgL is a poly-(beta-D-mannuronate) lyase that preferentially degrades deacetylated polymannuronate via a beta-elimination reaction, resulting in an unsaturated uronic acid at the nonreducing end of the molecule
-
-
-
additional information
?
-
Stenotrophomas maltophilia
I6P4V6
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
-
-
-
additional information
?
-
Q21FJ0
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview
-
-
-
additional information
?
-
G9MBE4
the enzyme is an endolytic polymannuronate lyase
-
-
-
additional information
?
-
Bacillus sp. ATB-1015
-
biological function of the enzyme
-
-
?
additional information
?
-
Stenotrophomas maltophilia KJ-2
I6P4V6
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
-
-
-
additional information
?
-
Pseudomonas alginovora XO17
Q59639
biological function of the enzyme
-
-
?
additional information
?
-
Alteromonas sp. H-4
Q9Z6D6
biological function of the enzyme
-
-
?
additional information
?
-
Photobacterium sp. ATCC 43367 Alg-A
-
biological function of the enzyme
-
-
?
additional information
?
-
-
alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG
-
-
-
additional information
?
-
Klebsiella pneumoniae SM0524
-
alginate lyases degrade the polysaccharide by cleaving the glycosidic linkages through a beta-elimination reaction. Lyase AlyA is bifunctional and shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). AlyA is endolytic, acting on G-blocks and MG-blocks where G-M linkages are cleaved in the latter substrate. Substrate specificities of diverse enzyme mutants, overview
-
-
-
additional information
?
-
Saccharophagus degradans DSM 17024
Q21FJ0
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview
-
-
-
additional information
?
-
Pseudomonas aeruginosa FRDI
Q06749
biological function of the enzyme, Pseudomonas aeruginosa produces a bacterial alginate which seems to be necessary for cell attachment to the capsule-like biofilm build in lung of infected humans suffering cystic fibrosis
-
-
?
additional information
?
-
Azotobacter chroococcum 4A1M
-
biological function of the enzyme
-
-
?
additional information
?
-
Pseudomonas fluorescens HZJ216
-
alginate lyase A degrades M and G blocks, and the enzyme activity acting on M block is much more than that of G block, while for alginate lyase B, the enzyme activities on M block are slightly higher than that of G block
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
-
stimulates
Ba2+
-
1 mM, 55% activation
Ba2+
-
activating
Ba2+
1 mM, 4.2fold increase in activity
Ba2+
-
1mM, 143% of initial activity; activates
BaCl2
-
stimulates activity, relative activity: 198%
Ca2+
-
stimulates
Ca2+
-
7.5 mM CaCl2 stimulates
Ca2+
at 1 mM, strain 4A1M
Ca2+
-
at 7.5 mM
Ca2+
-
activating
Ca2+
-
required
Ca2+
-
isozyme SP2
Ca2+
-
cations are required
Ca2+
required for activity
Ca2+
-
dependent on
Ca2+
-
optimal activity in presence of Ca2+
Ca2+
-
50 mM, activates
Ca2+
1 mM, 2.5fold increase in activity
Ca2+
-
136% relative activity at 1 mM
Ca2+
-
the activity of isoform AlyA3 is stimulated by Ca2+, an increase by 5fold is observed upon increasing the concentration of Ca2+ from 0.02 mM to 6.3 mM
Ca2+
-
50 mM, isoform A 117%, isoform B 131% of initial activity; activates
Ca2+
-
activates
Ca2+
-
activates
Ca2+
-
1mM, 136% of initial activity; activates
Ca2+
Stenotrophomas maltophilia
required for activity, activates at 1 mM
Ca2+
AB489222
activates
Ca2+
-
required
Ca2+
at least 2 mM Ca2+ in the reaction mixture is essential for the activity
CaCl2
-
optimal at 5-10 mM
CaCl2
-
stimulates activity, relative activity: 176%
CaCl2
-
20% activation at 1 mM
Cd2+
-
stimulates
Co2+
-
1 mM, 80% activation
Co2+
-
-
Co2+
-
activating
Co2+
-
activates
Co2+
-
activates 5% at 2 mM
Co2+
-
1mM, 123% of initial activity; activates
Cs+
-
1 mM, 40% activation
Cs+
Alginovibrio aquatilis
-
-
Cs+
0.2 M, 2500% of initial activity
Cu2+
-
activates
Cu2+
-
activates 4% at 2 mM
Fe2+
-
stimulates
Fe3+
-
147% relative activity at 1 mM
K+
-
1 mM, 15% activation
K+
-
maximal activation at 0.05 M
K+
Alginovibrio aquatilis
-
-
K+
extracellular isozyme
K+
-
cations are required for activity
K+
-
slightly activating
K+
highly activating, activation is synergistic with Mg2+
K+
-
50 mM, activates
K+
1 mM, 4.2fold increase in activity
K+
-
the addition of K+ at a concentration of 50 mM results in a 10% increase in activity level
K+
-
117% relative activity at 50 mM
K+
0.2 M, 2500% of initial activity
K+
-
50 mM, isoform A 132%, isoform B 110% of initial activity; activates
K+
-
1mM, 117% of initial activity; activates
K+
Stenotrophomas maltophilia
activates at over 50 mM
KCl
-
stimulates activity, relative activity: 109%
Li+
-
1 mM, 12% activation
Li+
Alginovibrio aquatilis
-
-
Li+
-
50 mM, activates
Li+
0.2 M, 1880% of initial activity
Mg2+
-
stimulates
Mg2+
-
1 mM, 40% activation
Mg2+
-
maximal activation at 0.06-0.08 M
Mg2+
extracellular isozyme
Mg2+
-
cations are required for activity
Mg2+
-
slightly activating
Mg2+
slightly activating, activation is synergistic with K+
Mg2+
-
50 mM, activates
Mg2+
1 mM, 3.1fold increase in activity
Mg2+
-
the addition of 50 mM Mg2+ leads to a 2fold increase in activity level
Mg2+
-
50 mM, isoform A 116%, isoform B 121%, isoform C 114% of initial activity; activates
Mg2+
-
activates
Mg2+
-
1mM, 126% of initial activity; activates
Mg2+
AB489222
activates
MgCl2
-
stimulates activity, relative activity: 156%
MgCl2
-
15% activation at 1 mM
Mn2+
-
stimulates
Mn2+
-
maximal activation at 0.06-0.08 M
Mn2+
-
-
Mn2+
-
cations are required for activity
Mn2+
-
activating
Mn2+
-
slightly activating
Mn2+
1 mM, 3.2fold increase in activity
Mn2+
-
150% relative activity at 1 mM
Mn2+
-
activates
Mn2+
-
1mM, 116% of initial activity
Mn2+
AB489222
activates
MnCl2
-
stimulates activity, relative activity: 121%
Na+
-
0.2 M NaCl stimulates
Na+
-
maximal activation at 0.05 M
Na+
Alginovibrio aquatilis
-
-
Na+
extracellular isozyme
Na+
-
cations are required for activity
Na+
slightly activating
Na+
-
50 mM, activates
Na+
-
the addition of Na+ at a concentration of 50 mM results in a 10% increase in activity level
Na+
-
280% relative activity at 100 mM
Na+
0.2 M, 2200% of initial activity
Na+
-
is essential for the activity of all the three lyases
Na+
-
1mM, 143% of initial activity; activates
Na+
Stenotrophomas maltophilia
activates at over 50 mM
Na+
-
slight activation
Na+
AB489222
activates
Na2HPO4
-
optimal at 1% w/v
NaCl
activity is optimal at 0.35 M
NaCl
-
0.05-0.075 M required for activity
NaCl
-
0.1-0.2 M required for activity
NaCl
-
required for activity
NaCl
-
0.5 M required
NaCl
-
0.05-0.075 M required for activity
NaCl
-
stimulates activity, relative activity: 113%
NaCl
-
activates at 1.5%
NaCl
-
AkAly28 shows practically no activity in the absence of NaCl and the maximal activity at NaCl concentrations higher than 0.2 M, whereas AkAly33 shows about 20% of maximal activity despite the absence of NaCl and the maximal activity at around 0.1 M NaCl
NaCl
-
2 mM, 110% of initial activity, 100 mM, 193% of initial activity; activates 10% at 2 mM,96% at 150 mM
NaCl
-
aly-SJ02 shows the highest activity in 0.2 M NaCl, and retains more than 75% activity in 1 M NaCl, exhibiting salt-tolerance ability
NaN3
-
1 mM, 20% activation
NH4+
-
1 mM, 12% activation
NH4+
0.2 M, 2270% of initial activity
Ni2+
-
1mM, 110% of initial activity; activates
Rb+
Alginovibrio aquatilis
-
-
Rb+
0.2 M, 2500% of initial activity
Sr2+
-
1mM, 124% of initial activity; activates
sulfate
-
sulfate binding site structure
Zn2+
-
stimulates
Zn2+
1 mM ZnCl2, 92% loss of activity
Zn2+
-
activating
Zn2+
1 mM, enhances activity by 66%
Zn2+
-
enhances activity
Zn2+
Agarivorans sp.
111% relative activity at 1 mM
Zn2+
-
activates 5% at 2 mM
Zn2+
relevance of this zinc ion in catalytic activity, metal-binding protein ligands are His533, Gln551, and Lys573. The metal ion establishes the orientation of His415 and Arg438, which would otherwise be mobile, to set these residues for interactions with substrate
MnCl2
-
12% activation at 1 mM
additional information
-
requires significant levels of salt for maximal activity. Optimal activity at approximately 0.05 M with divalent cation and between 0.3 and 0.4 M with monovalent cation
additional information
Alginovibrio aquatilis
-
no requirement for divalent cations
additional information
-
no metal ion requirement
additional information
no requirement for divalent cations
additional information
not affected by Ca2+, Co2+, Mn2+, and Zn2+
additional information
-
the activities of isoforms AlyA1 and AlyA2 are not affected by addition of similar concentrations of Ca2+
additional information
Sn2+, Ca2+, Mn2+, and Mg2+ do not influence enzyme activity of isoform A9mT
additional information
-
no effect by Li+ at 50 mM
additional information
-
no or poor effects by Mn2+ and Zn2+
additional information
-
Zn2+ has no effect on aly-SJ02 activity
additional information
-
no effect on activity by K+
additional information
-
no effect on enzyme activity by SDS, K+, Li+, and NH4+
additional information
no or poor effects by CaCl2 and NaCl at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
competitive
(NH4)2SO4
-
96% residual activity at 1 mM
1,10-phenanthroline
-
relative activity: 95%
1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate
-
reacts with Asp and Glu residues, causes a slight decrease in activity
2,4,6-Trinitrobenzene sulfonate
-
reacts with Lys residues, causes a slight decrease in activity
AgNO3
-
relative activity: 28%
AlCl3
-
53% inhibition at 1 mM
Ba2+
-
-
Ba2+
-
79% residual activity at 1 mM
Ba2+
-
; 50 mM, isoform A 89%, isoform B 44%, isoform C 42% of initial activity
BaCl2
-
28% inhibition at 1 mM
Butane-2,3-dione
-
reacts with Arg residues, causes a slight decrease in activity
Ca2+
Agarivorans sp.
95% inhibition at 1 mM
Ca2+
-
2 mM, 95% residual activity; 5% inhibition at 2 mM
Cd2+
-
-
Cd2+
-
2 mM, 25% residual activity; 75% inhibition at 2 mM
Co2+
1 mM, 50% inhibition
Co2+
isoform A9mT is inhibited by 14% at 1 mM
Co2+
-
; 50 mM, isoform A 67%, isoform B 66%, isoform C 29% of initial activity
Co2+
Stenotrophomas maltophilia
-
CoCl2
-
relative activity: 717
Cu2+
-
CuCl2
Cu2+
-
-
Cu2+
1 mM, more than 95% inhibition
Cu2+
-
2 mM
Cu2+
1 mM, 18% inhibition
Cu2+
isoform A9mT is inhibited by 16% at 1 mM
Cu2+
-
slightly inhibiting
Cu2+
Stenotrophomas maltophilia
-
CuCl2
-
97% inhibition at 1 mM
CuSO4
Agarivorans sp.
7% inhibition at 1 mM
D-galacturonic acid
-
-
D-glucuronic acid
-
-
dodecylsulfate
-
-
EDTA
-
-
EDTA
-
relative activity: 48%
EDTA
-
the addition of 50 mM EDTA leads to a 3fold decrease in activity level
EDTA
-
56% residual activity at 1 mM
EDTA
Agarivorans sp.
86%inhibition at 5 mM
EDTA
-
2 mM, 15% residual activity; 85% inhibition at 2 mM
EDTA
-
1 mM, 48% of initial activity; 51.7% inhibition at 1 mM
EDTA
Stenotrophomas maltophilia
-
EDTA
-
96% inhibition at 1 mM
EDTA
25% inhibition at 1 mM
EGTA
-
relative activity: 71%
EGTA
Agarivorans sp.
86% inhibition at 5 mM
EGTA
-
77% inhibition at 2 mM
ethylene glycol tetraacetic acid
-
2 mM, 23% residual activity
Fe2+
-
50 mM, no residual activity; complete inhibition of all isozymes at 50 mM
Fe2+
-
2 mM, 30% residual activity; 70% inhibition at 2 mM
Fe3+
-
2 mM
Fe3+
1 mM, complete inhibition
FeCl3
-
92% inhibition at 1 mM
FeSO4
10% inhibition at 1 mM
glutathione
-
2 mM, 23% residual activity; 77% inhibition at 2 mM
Hg2+
-
-
Hg2+
-
40% inhibition at 1 mM of isozyme A1-I and A1-II
Hg2+
1 mM, 30% inhibition
Hg2+
1 mM, more than 95% inhibition
Hg2+
-
2 mM
Hg2+
-
1 mM, 96% inhibition
Hg2+
Agarivorans sp.
80% inhibition at 1 mM
Hg2+
-
2 mM, 10% residual activity; 90% inhibition at 2 mM
Hg2+
Stenotrophomas maltophilia
-
K+
-
67% residual activity at 100 mM
KCl
weak inhibition at 1 mM
Methyl-4-nitrobenzenesulfonate
-
40% reduced activity with recombinant wild-type enzyme, no effect on mutant H192A
Methylmercury chloride
-
-
Mg2+
-
87% residual activity at 1 mM
MgCl2
weak inhibition at 1 mM
MgSO4
weak inhibition at 1 mM
Mn2+
Agarivorans sp.
28% inhibition at 1 mM
Mn2+
Stenotrophomas maltophilia
-
N-bromosuccimide
-
complete loss of activity, reacts with Trp residues
N-bromosuccinimide
-
-
Na+
-
59% residual activity at 900 mM
NaCl
in the presence of 0.2 M NaCl, the residual activities of isoform A9mL from pH 6 to 10 are decreased 40-75% of those observed in the absence of NaCl
Ni2+
1 mM, 27% inhibition
Ni2+
-
67% residual activity at 1 mM
Ni2+
Agarivorans sp.
95% inhibition at 1 mM
Ni2+
isoform A9mT is inhibited by 35% at 1 mM
Ni2+
-
2 mM, 65% residual activity; 35% inhibition at 2 mM
NiCl2
-
33% inhibition at 1 mM
PCMB
-
-
Pd2+
Agarivorans sp.
95% inhibition at 1 mM
PMSF
-
relative activity: 95%
SDS
1 mM, 94% loss of activity
SDS
-
0.05 M
SDS
1 mM, complete inhibition
SDS
-
35% residual activity at 1 mM
SDS
strongly inhibits the enzyme activity by 90%
Sn2+
-
slightly inhibiting
Sr2+
Agarivorans sp.
46% inhibition at 1 mM
Sr2+
isoform A9mT is inhibited by 14% at 1 mM
Sr2+
-
2 mM, 70% residual activity; 30% inhibition at 2 mM
Tetranitromethane
-
reacts with Tyr residues, causes a slight decrease in activity
Zn2+
1 mM ZnCl2 reduces the activity to 7.6% of the control level without Zn2+ added, 0.1 mM Zn2+ reduces the activity to 61%
Zn2+
-
-
Zn2+
1 mM, more than 95% inhibition
Zn2+
-
1 mM, complete inhibition
Zn2+
1 mM, 21% inhibition
Zn2+
-
68% residual activity at 1 mM
Zn2+
isoform A9mT is inhibited by 19% at 1 mM
Zn2+
-
; 50 mM, isoform A 10%, isoform B 14%, isoform C 12% of initial activity
Zn2+
Stenotrophomas maltophilia
-
ZnCl2
-
58% inhibition at 1 mM
ZnSO4
-
relative activity: 78%
additional information
not affected by EDTA
-
additional information
-
oligoalginate lyase is not affected by addition of 1 mM EDTA, GSH, 2-mercaptoethanol, iodoacetic acid, N-ethylmaleimide, and sugars at 5 mM, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on oligoalginate lyase by Cu2+, Co2+, and Hg2+ at 1 mM
-
additional information
-
isozymes A1-I and A1-II are not affected by addition of 1 mM EDTA, DTT, GSH, 2-mercaptoethanol, iodoacetic acid, and sugars, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on isozymes A1-I and A1-II of Ca2+, Co2+, Mg2+, and Mn2+ at 1 mM
-
additional information
Agarivorans sp.
Ni2+, Co2+, and Mg2+ ions do not affect enzyme activity, dithiothreitol and 2-mercaptoethanol (5 mM each) do not affect the enzyme activity at all
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
Agarivorans sp.
409% relative activity at 200 mM
(NH4)2SO4
(NH4)2SO4 at 0.2 M increases the original activity of isoform A9mT 23.5times
AgNO3
activates 31% at 1 mM
alginate
stimulates the expression of extracellular isozyme, but not of the intracellular isozymes
Ca2+
required
Ca2+
-
1.4-2fold increase in activity of oligoalginate lyase at 1 mM
CH3COO- NH4+
Agarivorans sp.
298% relative activity at 200 mM
CH3COO- NH4+
CH3COONH4 at 0.2 M increases the original activity of isoform A9mT 20.9times
CH3COONa
Agarivorans sp.
233% relative activity at 200 mM
CH3COONa
CH3COONa at 0.2 M increases the original activity of isoform A9mT 21times
CoCl2
activates 8% at 1 mM
CsCl
CsCl at 0.2 M increases the original activity of isoform A9mT 25times
EDTA
-
enhances activity
EDTA
-
enhances activity
Fe2+
-
1.4-2fold increase in activity of oligoalginate lyase at 1 mM
K2HPO4
Agarivorans sp.
439% relative activity at 200 mM
KCl
Agarivorans sp.
521% relative activity at 200 mM
KCl
KCl at 0.2 M increases the original activity of isoform A9mT 24.9times
LiCl
LiCl at 0.2 M increases the original activity of isoform A9mT 18.8times
Mg2+
-
1.4-2fold increase in activity of oligoalginate lyase at 1 mM
Mn2+
-
1.4-2fold increase in activity of oligoalginate lyase at 1 mM
NaBr
Agarivorans sp.
712% relative activity at 200 mM
NaBr
NaBr at 0.2 M increases the original activity of isoform A9mT 21.8times
NaCl
Agarivorans sp.
best activator, 823% relative activity at 200 mM, the activity is increased to 1.8times by adding 0.2 M NaCl, the activity reaches maximum at 0.6-0.8 M NaCl, which is around 20 times without NaCl
NaCl
recombinant isoform A9mT is remarkably activated in the presence of NaCl, when 0.4 M NaCl is added to the reaction mixture, the activity is increased maximally to 24times the original activity, the activity gradually decreases at higher NaCl concentrations, but is still activated 20times at 0.8 M and 8 times at 1.6 M NaCl
NaCl
-
about 20% of maximal activity in the absence of NaCl, maximal activity at around 0.1 M NaCl; absolutely required, maximal activity above 0.2 M
NaF
Agarivorans sp.
419% relative activity at 200 mM
NaF
NaF at 0.2 M increases the original activity of isoform A9mT 21.7times
NH4Cl
Agarivorans sp.
549% relative activity at 200 mM
NH4Cl
NH4Cl at 0.2 M increases the original activity of isoform A9mT 22.7times
Nonidet P40
the enzyme is moderately activated by Nonidet P40 by 134%
RbCl
RbCl at 0.2 M increases the original activity of isoform A9mT 25times
Tween 20
the enzyme is moderately activated by Tween 20 by 139%
additional information
not affected by EDTA
-
additional information
-
oligoalginate lyase is not affected by addition of 1 mM EDTA, GSH, 2-mercaptoethanol, iodoacetic acid, N-ethylmaleimide, and sugars at 5 mM, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on oligoalginate lyase by Cu2+, Co2+, and Hg2+ at 1 mM
-
additional information
-
the lyase activity is probably stimulated by the epimerase activity forming more guluronate residues at the reducing end of the substrate polymers
-
additional information
-
isozymes A1-I and A1-II are not affected by addition of 1 mM EDTA, DTT, GSH, 2-mercaptoethanol, iodoacetic acid, and sugars, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on isozymes A1-I and A1-II of Ca2+, Co2+, Mg2+, and Mn2+ at 1 mM
-
additional information
5 mM EDTA and EGTA do not influence enzyme activity of isoform A9mT
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
alginate
-
-
0.46
alginate
; alginate rich in mannuronic acid
0.94
alginate
Azotobacter vinelandii phage
-
bacterial alginate containing 25.5% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate
1.05
alginate
Azotobacter vinelandii phage
-
algal alginate containing 31.5% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate
1.09
alginate
Azotobacter vinelandii phage
-
bacterial alginate containing 55% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate
1.09
alginate
-
1.28
alginate
Azotobacter vinelandii phage
-
algal alginate containing 48% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate
2.36
alginate
-
in 50 mM phosphate buffer, pH 7.0, at 40C
0.031
hepta-alpha1,4-L-guluronate
-
pH 8.5, 30C
0.192
hepta-beta1,4-D-mannuronate
-
pH 8.5, 30C
0.035
hexa-alpha1,4-L-guluronate
-
pH 8.5, 30C
0.025
nona-alpha1,4-L-guluronate
-
pH 8.5, 30C
0.172
nona-beta1,4-D-mannuronate
-
pH 8.5, 30C
0.028
octa-alpha1,4-L-guluronate
-
pH 8.5, 30C
0.186
octa-beta1,4-D-mannuronate
-
pH 8.5, 30C
-
0.039
penta-alpha1,4-L-guluronate
-
pH 8.5, 30C
0.232
penta-beta1,4-D-mannuronate
-
pH 8.5, 30C
0.0101
sodium alginate
pH 7.5, 30C, mutant Q149A
0.0121
sodium alginate
pH 7.5, 30C, mutant R260A
0.0216
sodium alginate
pH 7.5, 30C, H415A
0.0223
sodium alginate
pH 7.5, 30C, wild-type enzyme
0.0311
sodium alginate
pH 7.5, 30C, mutant R438A
0.0916
sodium alginate
pH 7.5, 30C, mutant H202L
3.86
tetra-alpha1,4-L-guluronate
-
pH 8.5, 30C
4.25
tetra-beta1,4-D-mannuronate
-
pH 8.5, 30C
0.226
hexa-beta1,4-D-mannuronate
-
pH 8.5, 30C
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km for sodium alginate is 0.13 mg/ml
-
additional information
additional information
-
KM value for sodium alginate is 21.5 mg/ml
-
additional information
additional information
-
KM-value for alpha-L-guluronosyl linkage in alginate, 1.086 mg/ml, for poly(alpha-L-guluronic acid), 2.751 mg/ml at pH 8.5, 50C
-
additional information
additional information
KM value of wild-type, substrate alginate, 0.08 mg/ml; Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
pseudo Michaelis-Menten kinetics of native and recombinant His-tagged enzymes, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
dimeric AlyA5 shows two-phase kinetics with alginate, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.42
alginate
Pseudomonas aeruginosa
-
protein PA1167, pH 7.5, 37C
748
alginate
Pseudomonas aeruginosa
-
AlgL
7.6
hepta-alpha1,4-L-guluronate
Alteromonas sp.
-
pH 8.5, 30C
13.2
hepta-beta1,4-D-mannuronate
Alteromonas sp.
-
pH 8.5, 30C
7.9
hexa-alpha1,4-L-guluronate
Alteromonas sp.
-
pH 8.5, 30C
11.9
hexa-beta1,4-D-mannuronate
Alteromonas sp.
-
pH 8.5, 30C
7.8
nona-alpha1,4-L-guluronate
Alteromonas sp.
-
pH 8.5, 30C
10.8
nona-beta1,4-D-mannuronate
Alteromonas sp.
-
pH 8.5, 30C
7.3
octa-alpha1,4-L-guluronate
Alteromonas sp.
-
pH 8.5, 30C
11.1
octa-beta1,4-D-mannuronate
Alteromonas sp.
-
pH 8.5, 30C
-
6.2
penta-alpha1,4-L-guluronate
Alteromonas sp.
-
pH 8.5, 30C
7.4
penta-beta1,4-D-mannuronate
Alteromonas sp.
-
pH 8.5, 30C
0.0149
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant R260A
0.0156
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant Q149A
0.018
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant R438A
0.057
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, H415A
10.9
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant H202L
56.9
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, wild-type enzyme
2.5
tetra-alpha1,4-L-guluronate
Alteromonas sp.
-
pH 8.5, 30C
3.2
tetra-beta1,4-D-mannuronate
Alteromonas sp.
-
pH 8.5, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.58
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant R438A
120502
1.3
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant R260A
120502
1.6
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant Q149A
120502
2.6
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, H415A
120502
120
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, mutant H202L
120502
2570
sodium alginate
Saccharophagus degradans
Q21FJ0
pH 7.5, 30C, wild-type enzyme
120502
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
(NH4)2SO4
-
pH 7.5, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.021
purified recombinant enzyme
0.0274
-
protein PA1167
0.142
Agarivorans sp.
crude extract, at pH 10.0
1.14
wild-type, pH 7.5, 30C
1.98
-
wild-type enzyme, pH 7.0, 50C, substrate alginate
21.77
-
alginate lyase C, substrate with M blocks, pH 7.0, 30C
34.4
-
purified enzyme
41.4
-
purified recombinant His-tagged enzyme, pH 7.0, 50C, substrate alginate
45
-
purified isozyme A1-III
67
-
pH 6.5, 35C
67
-
purified recombinant His-tagged enzyme, substrate poly(beta-D-mannuronate), pH 7.0, 50C
67.24
-
purified enzyme, pH 6.5, 35C
73.1
-
purified isozyme A1-I
93.88
purified enzyme
108.5
Agarivorans sp.
after 764.1fold purification, at pH 10.0
109
-
purified isozyme A1-II
129
-
alginate lyase C, substrate with G blocks, pH 7.0, 30C
330
-
alginate lyase B, substrate with G blocks, pH 7.0, 30C
382
-
alginate lyase B, substrate with M blocks, pH 7.0, 30C; isoform B, substrate poly(beta-D-mannuronate), pH 7.0, 30C
390
-
alginate lyase A, substrate with G blocks, pH 7.0, 30C
467
-
isoform B, substrate sodium alginate, pH 7.0, 30C
651
-
alginate lyase A, substrate with M blocks, pH 7.0, 30C; isoform A, substrate poly(beta-D-mannuronate), pH 7.0, 30C
653
-
isoform A, substrate sodium alginate, pH 7.0, 30C
937
-
substrate poly(beta-D-mannuronic acid/alpha-L-guluronic acid), 22C, pH 7.5
1123
-
extracellular enzyme, pH 7.0, 30C
1401
pH 7.5, 30C
2057
-
pH 7.0, 30C; purified isozyme AkAly33, pH 8.0, 37C
2100
purified recombinant His-tagged AkAly30, pH 8.0, 30C
2152
-
purified enzyme, pH 7.0, 38C
2490
-
30C, pH 8.0
4803
-
pH 8.5, 50C; purified enzyme, pH 8.5, 50C
5740
-
pH 7.0, 30C
5741
-
purified isozyme AkAly28, pH 8.0, 37C
5796
purified native AkAly30, pH 8.0, 30C
8409
AB489222
purified native enzyme, pH 7.0, 50C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
assay methods, overview
additional information
assay methods, overview
additional information
Azotobacter phage A22, Azotobacter phage A31
-
assay methods, overview
additional information
assay methods, overview
additional information
Azotobacter vinelandii phage
-
assay methods, overview, endolytic activity
additional information
-
assay methods, overview
additional information
assay methods, overview
additional information
assay methods, overview
additional information
assay methods, overview
additional information
-
-
additional information
activity of different enzyme expressing plasmid constructs in Escherichia coli
additional information
-
the specific activity of the recombinant enzyme at 30C in buffer containing 10 mM NaPi (pH 8.0) is 2490 units/mg, one unit of lyase activity is defined as the amount of enzyme that increases the absorbance at 235 nm by 0.01 unit after 1 min
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
-
in 0.05 M salt
5.6
-
in presence of 0.05 M NaCl
5.8
-
strain JBH2
6.8
-
isoform AlyA2
7
-
optimal activity near neutral pH
7
-
about, groups 3,4,5,8
7
-
in the presence of 0.1 M NaCl
7
-
recombinant enzyme
7 - 7.5
intracellular isozyme
7 - 8
-
-
7 - 8
Dollabella auricola
-
-
7.2
-
assay at
7.2
-
assay at
7.3
-
maximal activity
7.4 - 7.6
-
-
7.5
extracellular isozyme
7.5
Azotobacter phage A22, Bacillus sp., Pelvetia canaliculata
-
-
7.5
-
assay at
7.5
-
assay at
7.5
-
isoform AlyA3
7.5
-
assay at
7.5
-
assay at
7.5 - 8
-
-
7.5 - 8
-
-
7.5 - 9.2
-
isozyme SP1
7.6 - 9
; recombinant isoform A9mT, in 100 mM Tris-HCl buffer, MOPS buffer, and glycine-NaOH buffer in the presence of 0.2 M NaCl
7.7
Azotobacter vinelandii phage
-
-
7.7 - 9.4
-
isozyme SP2
7.8
-
isoform AlyA1
8
Alginovibrio aquatilis, Haliotis tuberculata
-
-
8
-
isozymes A1-I and A1-II
8
Stenotrophomas maltophilia
-
8 - 8.5
-
activity stimulated by addition of 7.5 mM CaCl2 and 0.2 M NaCl
8 - 8.5
-
in presence of 0.2 M NaCl
8 - 9
crude recombinant A9mL isozyme
8.5
-
protein PA1167
10
Agarivorans sp.
the optimal pH is around 10 in glycine-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 10.5
-
assay range
3 - 11
-
activity range, profile, overview
3.6 - 11
-
-
4 - 11
-
activity range
4 - 6
-
pH 4.0: about 25% of maximal activity, pH 6.0: about 55% of maximal activity
4 - 9
-
pH 4.0: about 40% of maximal activity, pH 9.0: about 70% of maximal activity
5 - 10
-
assay range
5 - 11
-
activity range, profile overview
5 - 7
-
pH 5.0: about 40% of maximal activity, pH 7.0: about 25% of maximal activity
5 - 8.5
pH 5.0: about 40% of maximal activity, pH 8.5: about 35% of maximal activity
5 - 9
activity range
5.5 - 8
-
pH 5.5: about 30% of maximal activity, pH 8.0: about 60% of maximal activity
5.5 - 9.5
AB489222
activity range, profile overview
5.8 - 9.1
-
less than 10% of maximal activity below pH 5.8 and above pH 9.1
6
highest activity at pH 6.0, which sharply decreases when the pH is higher or lower than pH 6.0
6 - 10
pH 6.0: about 55% of maximal activity, pH 10.0: about 60% of maximal activity
6 - 8.8
pH 6.0: about 45% of maximal activity, pH 8.8: about 50% of maximal activity
6.5 - 8
pH 6.5: about 45% of maximal activity, pH 8.0: about 50% of maximal activity
6.7 - 8.4
pH 6.7: about 50% of maximal activity, pH 8.1-8.4: optimum; pH 6.7: about 50% of maximal activity, pH 8.1-8.4: optimum
7 - 8.5
Azotobacter vinelandii phage
-
pH 7.0: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
additional information
-
-
additional information
residue N120 is not directly related to the pH-dependence of AkAly30, overview
additional information
pH profile, narrow activity range, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
30
extracellular isozyme
30
-
assay at
30
-
assay at
30
Agarivorans sp.
around 30C
30
recombinant isoform A9mT, around 30C in the presence of 0.2 M NaCl at pH 7.5
35
intracellular isozyme
35 - 40
-
-
37
-
assay at
37
-
assay at
37
-
assay at
40
-
protein PA1167
40
-
in the presence of 0.1 M NaCl
40
Stenotrophomas maltophilia
-
45
-
isozyme A1-I
50
-
strain JBH2
50
-
recombinant enzyme
70
-
isozyme A1-I
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 65
-
assay range
4 - 50
-
assay range, 80% of maximal activity at 20C and 45C, activity is completely lost at 50C
10 - 45
temperature profile, overview
10 - 60
-
activity range
15 - 35
-
15C: about 70% of maximal activity, 35C: about 40% of maximal activity
20 - 50
-
20C: about 60% of maximal activity, 50C: about 40% of maximal activity
20 - 60
-
20C: about 55% of maximal activity, 60C: about 50% of maximal activity
20 - 70
activity ramge, recombinant enzyme
20 - 70
-
activity range, profile overview
20 - 80
-
-
20 - 80
activity range
23 - 37
-
-
25
-
isoform C, 54% of maximum activity
25 - 40
-
isoforms A, B, more than 60% of maximum activity
25 - 40
-
more than 80% of maximum activity
25 - 45
25C: about 55% of maximal activity, 45C: about 65% of maximal activity
25 - 60
-
activity range, the lyases possess more than 60% activity in the range of 25C to 40C except alginate lyase C at 25C which is 53.89% activity, but the activities decrease above 40C
25 - 60
AB489222
activity range, profile overview
30 - 45
30C: about 60% of maximal activity, 45C: about 70% of maximal activity
30 - 50
30C: about 55% of maximal activity, 50C: about 70% of maximal activity
30 - 50
-
30C: about 50% of maximal activity, 50C: about 10% of maximal activity
30 - 65
30C: about 50% of maximal activity, 65C: about 55% of maximal activity
40 - 50
-
maximal activity, however it is shown that alginase quickly loses its catalytic capability when the temperature is above 45C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
-
isoelectric focusing
4
-
alginate lyase A, isoelectri focusing; isoform A, isoelectric focusing
4.2
-
isoform AlyA3, calculated from amino acid sequence
4.36
-
alginate lyase B, isoelectri focusing
4.4
-
isoform B, isoelectric focusing
4.59
-
alginate lyase C, isoelectri focusing
4.6
-
isoform C, isoelectric focusing
4.7
isoform A9mC, calculated from amino acid sequence
4.7 - 4.8
extracellular isozyme
4.9
isoform A9mL, calculated from amino acid sequence
5.1
isoelectric focusing
5.4
intracellular isozyme
5.6
-
isoform AlyA2, calculated from amino acid sequence
6.4
Agarivorans sp.
calculated; isoform A1mU, calculated from amino acid sequence
6.7
intracellular isozyme
6.8
-
ALY-II
7.2
calculated; isoform A9mT, calculated from amino acid sequence
9.7
-
isoform AlyA1, calculated from amino acid sequence
10.2
-
ALY-III
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Dollabella auricola
-
-
Manually annotated by BRENDA team
additional information
strain H-4, can grow on alginate as sole carbon source
Manually annotated by BRENDA team
additional information
the organism is able to grow on alginate as the sole carbon source
Manually annotated by BRENDA team
additional information
Alteromonas sp. H-4
-
strain H-4, can grow on alginate as sole carbon source
-
Manually annotated by BRENDA team
additional information
-
the organism is able to grow on alginate as the sole carbon source
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Fucus spp.
-
bound
Manually annotated by BRENDA team
Alginovibrio aquatilis
-
-
-
Manually annotated by BRENDA team
constitutive expression
-
Manually annotated by BRENDA team
Azotobacter phage A22, Azotobacter phage A31, Azotobacter vinelandii phage
-
-
-
Manually annotated by BRENDA team
-
secretion to the culture medium
-
Manually annotated by BRENDA team
-
lyase AlyA is secreted by strain SM0524
-
Manually annotated by BRENDA team
-
; aly-SJ02 is secreted
-
Manually annotated by BRENDA team
-
secretion to the culture medium
-
-
Manually annotated by BRENDA team
Alteromonas sp. H-4
-
constitutive expression
-
-
Manually annotated by BRENDA team
Azotobacter chroococcum 4A1M
-
strain 4A1M
-
-
Manually annotated by BRENDA team
Bacillus sp. ATB-1015
-
-
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae SM0524
-
lyase AlyA is secreted by strain SM0524
-
-
Manually annotated by BRENDA team
Photobacterium sp. ATCC 43367 Alg-A
-
-
-
-
Manually annotated by BRENDA team
-
; aly-SJ02 is secreted
-
-
Manually annotated by BRENDA team
constitutive expression, intracellular isozymes also show hydrolase activity on alginate
Manually annotated by BRENDA team
Alteromonas sp. H-4
-
constitutive expression, intracellular isozymes also show hydrolase activity on alginate
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa FRDI
-
recombinant enzyme
-
Manually annotated by BRENDA team
Pseudomonas alginovora XO17
-
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa FRDI
-
-
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa CF1/M1
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
about, strain 4A1M
648532
23000
-
gel filtration
648533
25000
-
gel filtration
34062
25000
-
ALY-II
648532
25000
-
isozyme A1-II, gel filtration
653728
25000
gel filtration
665371
25000
-
protein PA1167, gel filtration
665543
25010
isoform A9mC, calculated from amino acid sequence
705481
25550
-
amino acid sequence determination
653039
25900
-
isoform AlyA1, calculated from amino acid sequence
704300
26600
-
isoform AlyA2, calculated from amino acid sequence
704300
27500
SDS-PAGE
693967
28000
-
SDS-PAGE
692125, 703781
28000
-
three alginate lyases with molecular masses of 35000, 32000, and 28000 Da are isolated, SDS-PAGE
703781
28000
isoform A9mT, SDS-PAGE
705481
28000
AB489222
-
729531
29000
-
gel filtration
34068
29640
isoform A9mT, calculated from amino acid sequence
705481
30000
-
648532
30000 - 35000
Azotobacter vinelandii phage
-
-
34060, 648532
30220
Agarivorans sp.
isoform A1mU, calculated from amino acid sequence
705481
31000
Agarivorans sp.
SDS-PAGE
703603
31000
gel filtration; isoform A9mT, Bio-Gel-A0.5 m gel filtration
705481
32000
extracellular isozyme
648532
32000
-
both isozymes
648532
32000
-
SDS-PAGE
695268
32000
-
three alginate lyases with molecular masses of 35000, 32000, and 28000 Da are isolated, SDS-PAGE
703781
32300
Agarivorans sp.
calculated from amino acid sequence
703603
34000
-
-
648532
34000
-
SDS-PAGE
703781
35000
-
three alginate lyases with molecular masses of 35000, 32000, and 28000 Da are isolated, SDS-PAGE
703781
35000 - 42000
Azotobacter phage A31
-
-
648532
36000
-
gel filtration
34063
38000
-
ALY-III
648532
38300
monomeric recombinant His-tagged enzyme, gel filtration
730018
39000
-
gel filtration
34064
39000
-
648532
39000
-
648532
39000
from strain FRDI
648532
39000 - 41000
-
-
648532
40000
-
gel filtration
34074
40000
-
-
648532
40000
-
isozyme A1-III, gel filtration
653728
43500
recombinant enzyme
648532
46000
gel filtration
651639
47000
-
-
648532
49400
-
isoform AlyA3, calculated from amino acid sequence
704300
50000
-
gel filtration
34060
54430
isoform A9mL, calculated from amino acid sequence
705481
57400
-
calculated from amino acid sequence
702993
58000
-
SDS-PAGE
702993
60000
-
ALY-I
648532
62500
-
gel filtration
677288
66000
-
isozyme A1-I, gel filtration
653728
69500
dimeric recombinant His-tagged enzyme, gel filtration
730018
74000
-
-
648532
83000
-
oligoalginate lyase, native PAGE
651661
85000
gel filtration
665769
87870
calculated from amino acid sequence
704682
94000
-
gel filtration
34078
100000
-
gel filtration
34061
110000
Alginovibrio aquatilis
-
-
648532
350000
-
gel filtration
682820
additional information
Azotobacter vinelandii phage
-
-
34060
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 35000, SDS-PAGE
?
x * 39000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
x * 39000, recombinant enzyme, SDS-PAGE
?
x * 40000, SDS-PAGE
?
-
x * 25000, protein PA1167, SDS-PAGE
?
-
x * 32000, SDS-PAGE
?
-
x * 34600, SDS-PAGE
?
-
x * 32000, SDS-PAGE
?
x * 42200, calculated from sequence; x * 42800, SDS-PAGE
?
Agarivorans sp.
x * 30218, calculated
?
-
x * 60250, alginate lyase A, SDS-PAGE, x * 36000, alginate lyase B, SDS-PAGE, x * 23000, alginate lyase C, SDS-PAGE; x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
?
x * 29722, sequence calculation, x * 30000, SDS-PAGE
?
-
x * 27500, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 28000, SDS-PAGE; x * 33000, isozyme AkAly33, SDS-PAGE, x * 28000, isozyme AkAly28, SDS-PAGE; x * 33000, SDS-PAGE
?
-
x * 45000 plus x * 50000, SDS-PAGE; x * 45000 + x * 50000
?
x * 79600, recombinant His6-tagged enzyme, SDS-PAGE; x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
?
-
x * 32000, SDS-PAGE
?
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
?
Stenotrophomas maltophilia
x * 47800, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 32700, recombinant His-tagged enzyme without, SDS-PAGE
?
-
x * 37000, SDS-PAGE
?
x * 28000, recombinant His-tagged wild-type enzyme, SDS-PAGE, x * 28999, sequence calculation
?
-
x * 30218, calculated
-
?
-
x * 32000, SDS-PAGE
-
?
Pseudomonas aeruginosa AlgL
-
x * 25000, protein PA1167, SDS-PAGE
-
?
Pseudomonas fluorescens HZJ216
-
x * 60250, alginate lyase A, SDS-PAGE, x * 36000, alginate lyase B, SDS-PAGE, x * 23000, alginate lyase C, SDS-PAGE; x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
-
?
-
x * 46000, SDS-PAGE
-
?
-
x * 79600, recombinant His6-tagged enzyme, SDS-PAGE; x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
-
?
Stenotrophomas maltophilia KJ-2
-
x * 47800, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 32000, SDS-PAGE
-
?
Streptomyces sp. ALG-5
-
x * 27500, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 37000, SDS-PAGE
-
homodimer
structure analysis, SDS-PAGE and analytical gel filtration, overview
homodimer
Saccharophagus degradans DSM 17024
-
structure analysis, SDS-PAGE and analytical gel filtration, overview
-
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE
monomer
-
1 * 41000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 33900, SDS-PAGE
monomer
1 * 43000, SDS-PAGE
monomer
-
1 * 85000, oligoalginate lyase, SDS-PAGE
monomer
-
1 * 63000, A1-I, SDS-PAGE, 1 * 25000, A1-II, SDS-PAGE, 1 * 40000, A1-III, SDS-PAGE
monomer
1 * 25000, SDS-PAGE
monomer
1 * 29643, calculated, 1 * 28000, SDS-PAGE; 1 * 31000, isoform A9mT, Bio-Gel-A0.5 m gel filtration
monomer
AB489222
1 * 28000
monomer
-
1 * 33900, SDS-PAGE
-
monomer
Bacillus sp. ATB-1015
-
1 * 41000, SDS-PAGE
-
monomer
Isoptericola halotolerans CGMCC5336
-
1 * 28000
-
monomer
Vibrio sp. A9m, Vibrio sp. JAM-A9m
-
1 * 29643, calculated, 1 * 28000, SDS-PAGE; 1 * 31000, isoform A9mT, Bio-Gel-A0.5 m gel filtration
-
monomer or dimer
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
tetramer
-
4 * 87871, calculated from sequence; 4 * 88000, SDS-PAGE
tetramer
Agrobacterium tumefaciens C58
-
4 * 87871, calculated from sequence; 4 * 88000, SDS-PAGE
-
monomer or dimer
Zobellia galactanivorans DSM 12802
-
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
-
additional information
-
structural analysis
additional information
-
the enzyme shows an (alpha6/alpha5)-barrel structure with a tunnel-like active site cleft
additional information
-
purification leads to a mixture of three monomeric alginate lyases with molecular masses of 60.25, 36, and 23 kDa
additional information
-
tryptic peptide mapping, mass spectrometric analysis, overview
additional information
AlgL has an alpha6/alpha5-barrel fold
additional information
Pseudomonas sp. HZJ 216
-
purification leads to a mixture of three monomeric alginate lyases with molecular masses of 60.25, 36, and 23 kDa
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
signal peptide is cleaved off, leaving a mature protein of 39000 Da
proteolytic modification
-
A1-I is autolytically cleaved into A1-II and A1-III, which shows different substrate specificities, therfore A1-I possesses 3 active sites, 1 protease and 2 alginate lyase sites
proteolytic modification
signal peptide is cleaved off leaving a mature protein of 34000 Da
proteolytic modification
sequence contains a putative signal sequence of 23 amino acids
proteolytic modification
Vibrio sp. A9m, Vibrio sp. JAM-A9m
-
sequence contains a putative signal sequence of 23 amino acids
-
proteolytic modification
-
signal peptide is cleaved off leaving a mature protein of 34000 Da
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of native protein and its inactive mutant H531A in complex with alginate trisaccharide, at 2.10 and 2.99 A resolutions with final R-factors of 18.3 and 19.9%, respectively. The enzyme is comprised of an alpha/alpha-barrel plus anti-parallel beta-sheet as a basic scaffold. His311 and Tyr365 are the catalytic base and acid, respectively. A short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains are essential for the exolytic mode of action; wild type and mutant enzyme H531A in complex with alginate trisaccharide, sitting drop vapor diffusion method, using 80 mM Tris-HCl (pH 8.5), 24% (w/v) polyethylene glycol 4,000, 0.16 M magnesium chloride, and 20% (v/v) glycerol
crystallization at 20C by sitting-drop vapour diffusion with polyethylene glycol 4000 as a precipitant. X-ray analysis shows that the Atu3025 crystal belong to space group P2(1) and diffracted to 2.8 A resolution, with unit cell parameters a = 107.7, b = 108.3, c = 149.5 A, beta = 91.5
-
hanging-drop vapour-diffusion method, 1.2 A resolution
-
hanging-drop vapour diffusion method, crystal structure determined at 2.0 A resolution. PA1167 forms a glove-like beta-sandwich composed of 15 beta-strands and 3 alpha-helices
-
purified recombinant His-tagged AlgL28-362 protein, hanging drop vapour diffusion method, mixing of 0.002 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate, pH 4.6, 28% w/v PEG 4000, 0.3 M PIPES, method optimization, 4 days, 20C, X-ray diffraction structure determination and analysis at 1.64 A resolution
purified recombinant soluble His-tagged wild-type and selenomethionine-labeled enzyme, and two mutant enzymes H202L and Y258A, and Y258A DELTAMMG variant, free or in complex with an alginate trisaccharide, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in in 20 mM HEPES, pH 7.5, 100 mM KCl, with 0.1 M Tris, pH 8.0, 5% 2-methyl-2,4-pentanediol, 10% PEG 6000, 3 days, 16C, X-ray diffraction structure determination and analysis at 1.85 A, 1.7 A, 2.45 A, and 1.9 A resolution, respectively
8 mg/ml purified isozyme A1-III complexed with trisaccharide product 4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid, hanging drop vapour diffusion method, 0.1 M HEPES, pH 7.5, containg 48% PEG w/v saturated ammonium sulfate, 290 mM trisaccharide, 20C, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
hanging drop vapour diffusion method, 0.003 ml protein solution: 17.2 mg/ml protein, 0.1 M HEPES, pH 7.5, + 0.003 ml bottom solution: 47-49% saturated ammonium sulfate, 0.1 M HEPES, pH 7.5, 20C, 1 month, for large crystals micro- and macroseeding is used, crystal are soaked in heavy-atom derivatives for 1-4 h for X-ray diffraction structure determination and analysis at 1.78-10.0 A resolution
-
purified isozyme A1-II, hanging drop vapour diffusion method, 0.003 ml protein solution: 38 mg/ml protein, 50 mM Tris-HCl, pH 7.5, + 0.003 ml bottom solution: 0.1 M Tris-HCl, pH 8.5, 43% saturated ammonium sulfate, 8% PEG 4000, 0.2 M Li2SO4, 20C, 1 month, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
purified recombinant mutants H192A and Y246F complexed with substrate 4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)2-mannuronic acid, hanging drop vapour diffusion method, 10 mg/ml protein in solution is mixed with reservoir solution containing 24% w/v PEG 4000, 0.3 M ammonium acetate, 0.1 M sodium citrate pH 5.5, 20C, 1 month, X-ray diffraction structure determination and analysis at 2.2 resolution, final models of the complex forms, which comprise two monomers (of 353 amino-acid residues each), 268-287 water molecules and two tetrasaccharide substrates
-
recombinant
-
recombinant, alginate lyase A1-II and alginate lyase A1-II'. Both proteins are crystallized at 20C using hanging-drop vapour-diffusion method. A crystal of A-1II belongs to space group P2(1) and diffracts to 2.2 A resolution, with unit-cell parameters a = 51.3 A, b = 30.1 A, c = 101.6 A, beta = 100.2. Crystals of A1-II' belong to space group P2(1)2(1)2(1) and diffract to 1.0 A resolution, with unit-cell parameters a = 34.6, b = 68.5, c = 80.3 A
-
purified recombinant full-length dimeric AlyA5, hanging drop vapor diffusion method, 0.002 ml of 7.7 mg/ml protein solution with 0.1 mg/ml oligoglucuronate, are mixed with 0.001 ml of reservoir solution containing PEG 3350 and 0.2 M sodium/potassium tartrate, and equilibration against 0.2 ml reservoir solution, 21C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 11
-
the pH range at which 90% or more activity of the enzymes remains s pH 3.0-11.0
703781
4 - 10
-
stable
34063
4 - 10
-
37C, 3 h, about 40% loss of activity at pH 4.0, about 30% loss of activity, completely stable at pH 5.0
34074
4 - 11
-
at 25 C for 20 min, the purified enzyme retains more than 50% activity at pH 7.0-10, aly-SJ02 is most stable at pH 8.0
716092
4 - 8
-
stable
34074
5
-
relatively stable at alkaline pH, unstable below pH 5.0
34064
5 - 10.5
30C, 30 min
664733
5 - 7
-
alginate lyase C, stable; isoform C
713799
5 - 9
-
alginate lyase A and B, stable; isoforms A and B
713799
5.5 - 8.5
AB489222
purified enzyme, 12 h, over 60% activity within this pH range remains pH 5.5 to 8.5, mostly stable at pH 7.5, half inactivation at pH 9.5
729531
6 - 10
Agarivorans sp.
A1m is quite stable in incubation at 30C for 1 h between pH 6.0 and 9.0. When the optimal pH in the presence of 0.2 M NaCl is shifted to pH 9.0, the activity is more than 10times compared with that at pH 9 in the absence of NaCl. Similar results are observed in 100 mM borate buffer with or without 0.2 M NaCl. The stability of A1m in various pH buffers is unaffected by adding NaCl
703603
6 - 7.5
-
stable
677288
6 - 9
-
the pH range at which 90% or more activity of the enzymes remained was pH 6.0-9.0
703781
6 - 9
-
the pH range at which 90% or more activity of the enzymes remains
703781
6 - 9
-
purified native enzyme, 40C, stable within this pH range
729470
6.5 - 8.5
-
30C, 5 min, stable
34078
7
-
optimal stability
34062
7 - 10
isoform A9mT is stable at pH 7.0-10.0 in various 20 mM buffers without NaCl after incubation at 30C for 15 min; isoform A9mT is stable at pH 7.0-10.0 in various 20 mM buffers without NaCl after incubation at 30C for 15 min
705481
7 - 9
-
stable
679376
8
-
most stable at pH 8.0
716092
8 - 9
Stenotrophomas maltophilia
the purified recombinant His-tagged enzyme exhibits stable and high activity at pH between 8.0 and 9.0
729058
9.5 - 10
the relative activities at pH 9.5 and 10 in glycine-NaOH buffer are approximately 50% and 20%, respectively, of the maximal activity of isoform A9mL; the relative activities at pH 9.5 and 10 in glycine-NaOH buffer are approximately 50% and 20%, respectively, of the maximal activity of isoform A9mL
705481
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
the relative activities of isoform A9mT at 10C and 2C are around 45% and 30% of the maximal activity at 30C, respectively, isoform A9mT shows the highest thermal stability in the presence of NaCl, recombinant isoform A9mT is rapidly inactivated above 30C when the enzyme is incubated at 5C to 50C for 15 min in 100 mM Tris-HCl buffer (pH 7.5) with or without 0.2 M NaCl and the enzyme is rapidly inactivated when incubated at above 40C in the absence of NaCl
705481
20
-
30 min, 40% loss of activity
34064
20 - 50
-
the enzyme activities at 20 and 50C decrease to 50% and 30%, respectively
701884
20 - 50
-
the residual activity decreases when the temperature goes above 20C and disappears at 50C
702993
20 - 50
Agarivorans sp.
A1m is rapidly inactivated upon incubation at 30-50C for 15 min in 20 mM glycine-NaOH buffer (pH 9) with or without 0.2 M NaCl. The residual activity after treatment at 30C with 0.2 M NaCl is 53% of the residual activity without NaCl. The residual activities after treatment at 50C are 10% of the initial activities after incubation at 30C with or without NaCl. Activation of the enzyme by NaCl is prominent between 25 and 35C
703603
30
pH 7.5, 5 min, stable
665371
30
1 h, about 10% loss of activity
682995
30 - 60
1 h, residual activity decreases when temperature goes above 30C and disappears at 60C
664733
35
pH 7.5, 5 min, about 10% loss of initial activity
665371
35
-
1 h, about 50% loss of activity
677288
35
-
stable below
679376
35
-
30 min, isoform B 59% residual activity, isoform C 55% residual activity
713799
38
-
temperature at which activity decreases to 50% of the original activity for 20 min incubation is 38C
703781
38
-
half inactivation after 20 min; half-life of isozymes AkAly28 and AkAly33 is 20 min
714770
40
-
pH 5.6, 1 h, stable
34074
40
-
stable below, 10 min, pH 7.2
651661
40
pH 7.5, 5 min, about 35% loss of initial activity
665371
40
-
1 h, about 70% loss of activity
677288
40
1 h, about 20% loss of activity
682995
40
-
isoform A, 30 min, 70% residual activity
713799
40
-
activity is stable up to 40C for 30 min reaction, and then sharply decreases with further increase in temperature
714484
40
-
half-life 41 min; half-life is 41 min
716092
40
Stenotrophomas maltophilia
purified recombinant His-tagged enzyme, 20 min, stable up to, significant loss of activity above
729058
40
AB489222
purified enzyme, loss of 40% activity after 180 min
729531
41
-
temperature at which activity decreases to 50% of the original activity for 20 min incubation is 43C
703781
43
-
temperature at which activity decreases to 50% of the original activity for 20 min incubation is 41C
703781
45
-
stable below
34063
45
-
pH 7.2, 10 min, loss f 50% activity, isozyme A1-I
653728
45
pH 7.5, 5 min, about 50% loss of initial activity
665371
45
-
10 min, 80% loss of activity, protein PA1167
665543
50
-
1 h, complete inactivation
34074
50
-
pH 7.2, 10 min, loss f 50% activity, isozyme A1-I
653728
50
pH 7.5, 5 min, about 65% loss of initial activity
665371
50
10 min, 85% loss of activity
665769
50
-
1 h, about 90% loss of activity
677288
50
1 h, about 40% loss of activity
682995
50
-
temperature at which activity decreases to 50% of the original activity for 20 min incubation is 50C
703781
50
-
30 min, 50% residual activity; the activity of recombinant Aly is decreased by 50% after incubation at 50C for 30 min
705483
50
-
half-life 20 min; half-life is 20 min
716092
50
AB489222
purified enzyme, inactivation after 120 min
729531
60
-
30 min, 50% loss of activity
34064
60
1 h, about 75% loss of activity
682995
60
AB489222
purified enzyme, inactivation after 90 min
729531
70
-
92% of the activity is lost after incubation at 70C and pH 7.5 for 20 min
680308
70
-
enzyme totally inactivated at 70C within 10 min
695268
80
1 h, complete loss of activity
682995
90
-
purified native enzyme, 10 min, pH 7.0, 40% activity remians
729470
130
-
1 h, stable
677288
additional information
-
-
648533
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by repeated freezing and thawing
-
AlyDW11 contains three highly conserved regions, RSEL, QIH, and YFKAGVYNQ, which may act to stabilize the three-dimensional conformation and function of the alginate lyase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, rapid loss of activity
-
-20C, 3 months, stable
Azotobacter vinelandii phage
-
-15C, 4 months, stable
-
-20C, 3 months, stable
-
4C, in presence of sodium azide, 10 days, 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography
Agarivorans sp.
SuperQ Toyopearl column chromatography, butyl Toyopearl column chromatography, and ammonium sulfate fractionation
Agarivorans sp.
DEAE-Toyopearl 650M column chromatography, Q Sepharose column chromatography, and Superdex 200 gel filtration
from the culture medium, 135fold, to homogeneity
-
; native isozyme AkAly28 72.6fold and isozyme isozyme AkAly33 26fold by ammonium sulfate fractionation and cation exchange chromatography
-
recombinant His-tagged AkAly30 33fold from Escherihcia coli strain BL21(DE3) by nickel affinity chromatography, native AkAly30 97.58fold by ammonium sulfate fractionation and cation exchange chromatography
; native extracellular enzyme, 140fold
-
recombinant enzyme from Escherichia coli, 10.1fold
HiTrap SP column chromatography (isoform AlyA1), HiTrap Q column chromatography (isoform AlyA2 and AlyA3), and butyl Sepharose column chromatography (isoform AlyA2)
-
recombinant His-tagged enzyme from Escherichia coli, 4.8fold
purified by dual ammonium sulfate precipitation
-
ammonium sulfate fractionation, Toyopearl CM-650 M column chromatography, and hydroxyapatite column chromatography
-
ammonium sulfate precipitation and Ni-NTA column chromatography
-
using Ni-NTA chromatography
-
ammonium sulfate fractionation, Toyopearl CM-650 M column chromatography, and hydroxyapatite column chromatography
-
native enzyme 1.75fold by ammonium sulfate fractionation and anion exchange chromatography
AB489222
ammonium sulfate fractionation, Toyopearl CM-650 M column chromatography, and hydroxyapatite column chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
ammonium sulfate fractionation, Toyopearl CM-650 M column chromatography, and hydroxyapatite column chromatography
-
using gel filtraton and anion-exchange chromatography
-
; native, secreted aly-SJ02 73.4fold by ultrafiltration, anion exchange chromatography, and gel filtration
-
Ni-Sepharose column chromatography
-
recombinant AlgL; recombinant protein PA1167
-
recombinant C-terminally His6-tagged AlgL by nickel affinity chromatography and dialysis, native enzyme by hydroxyapatite chromatography, ultrafiltration, and gel filtration
-
recombinant His-tagged AlgL28-362 protein from Escherichia coli strain Origami 2 (DE3) by nickel affinity chrmatography, ultrafiltration, and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain C41(DE3) by nickel or cobalt affinity chromatography
-
native alginate lyases, by acetone precipitation, anion exchange chromatography, and gel filtration
-
partially purified by ultrafiltration
-
purification leads to a mixture of three monomeric alginate lyases with molecular masses of 60.25, 36, and 23 kDa
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli
recombinant Alg17C from Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
recombinant soluble His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta culture supernatant by nickel affinity chromatography and gel filtration
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli by metal affinity chromatography
recombinant C-terminally His6-tagged A1-III by nickel affinity chromatography and dialysis, native enzyme by hydroxyapatite chromatography, ultrafiltration, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography; recombinant protein
recombinant isozyme A1-II from Escherichia coli, 52.9fold
-
recombinant isozyme A1-III from Bacillus subtilis
-
recombinant isozymes A1-I 11.2fold, A1-II 25.5fold, and A1-III 4.9fold, from Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS
-
using Ni-NTA chromatography
-
recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain BL21(DE3)
Stenotrophomas maltophilia
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
using Ni-Sepharose affinity chromatography
addition of EDTA to the purification system improves the enzyme activity and the yield
-
enzyme form SP2
-
recombinant enzyme
-
combination of ammonium sulfate precipitation and diethylaminoethyl-Sephacel column chromatography
-
DEAE-Toyopearl column chromatography; DEAE-Toyopearl column chromatography; DEAE-Toyopearl column chromatography
native extracellular enzyme 23.6fold from cell culture supernatant
-
recombinant
recombinant GST-fusion wild-type and mutant enzymes from Escherichia coli strain BL-21 LysS by glutathione affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha cells
Agarivorans sp.
expressed in Escherichia coli B834(DE3) cells; expression in Escherichia coli
overexpressed in Escherichia coli
-
AkAly30 DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)
phylogenetic analysis
-
gene algL, DNA and amino acid sequence determination and analysis, cloning and overexpression in Escherichia coli
expressed in Escherichia coli DH5alpha cells
-
expression in Escherichia coli; expression in Escherichia coli
gene algL, construction of a mutant strain SML2, by introductionof a non-polar mutation, with no alginate lyase activity
-
gene cl2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli as His-tagged protein
baculoviral expression system; expressed as secreted proteins with baculoviral expression systems in Sf9 cells
-
expressed in yeast and Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
AB489222
DNA and amino acid sequence determination and analysis, lambda phage display, sequence comparisons
gene alyA, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression in Escherichia coli. Various calcium compounds that enhance the expression of the active enzyme. Maximum activity is observed in the clones cultured in broth containing 50-100% artificial seawater, respectively
-
overexpressed in Escherichia coli
-
when the alginate lysase gene (aly) is expressed in Escherichi coli, most of the gene product is organized as aggregated insoluble particles. At least 37% of the total alginate lyase is produced in the soluble fraction when aly is coexpressed with DnaK/DnaJ/GrpE chaperone
-
DNA and amino acid sequence determination and analysis
-
expressed in Escherichia coli BL21(DE3) cells
-
AlgL is co-expressed in the algD operon
expression of C-terminally His6-tagged AlgL
-
gene algL, algL is part of the alginate biosynthetic operon, expression of His-tagged enzyme in Escherichia coli strain C41(DE3)
-
gene algL, expression from pNMAlgL28362 expression vector as His-tagged enzyme in Escherichia coli strain Origami 2 (DE3)
mutant enzymes H202Q and Y256F
-
overexpression of AlgL in Escherichia coli; protein PA1167, overexpression in Escherichia coli
-
recombinant expression of N-terminally GST-tagged enzyme in Escherichia coli strains BL21(DE3), C41(DE3) and C43(DE3)
-
algL is expressed in pET24a (+)/E. coli BL21 (DE3) system
expression in Escherichia coli
-
gene algL, DNA sequence determination and analysis, overexpression in Escherichia coli BL21(DE3), periplasmic enzyme location
gene alg17C, expression in Escherichia coli strain BL21(DE3)
gene alg7D, overexpression of soluble His-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21(DE3)
-
subcloning of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5-alpha, expression in Escherichia coli strain BL21(DE3) Rosetta, the enzymes are secreted from periplasmic space
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3); expression in Escherichia coli
DNA sequence determination and analysis of the gene encoding isozyme A1-III, expression of wild-type and mutant H192A in Escherichia coli
-
expressed as a His-tagged fusion protein
-
expression in T7 driven pET vector system; expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
expression of C-terminally His6-tagged A1-III
-
expression of native A1-II' and a truncated A1-II' lacking the N-terminal 80 amino acid residues in Escherichia coli
gene encoding the oligoalginate lyase, DNA sequence determination and analysis, genetic mapping
-
overexpression in Escherichia coli
overexpression of isozyme A1-II in Escherichia coli
-
overexpression of isozyme A1-III in Bacillus subtilis
-
sequence comparison of PL-5 alginate lyase, recombinant wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
-
the 3 isozymes are natively expressed as 1 precursor molecule and are posttranslationally processed to monomeric forms, overexpression of all isozymes A1-I, A1-II, and A1-III in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Stenotrophomas maltophilia
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) at 37C and at 15C. The recombinant alginate lyase expressed with pColdI at 15C exhibits the highest alginate-degrading activity, method evaluation and optimization
-
expressed as a His-tagged fusion protein in Escherichia coli
expressed in Escherichia coli DH5alpha cells; expressed in Escherichia coli DH5alpha cells; expressed in Escherichia coli DH5alpha cells; expression in Escherichia coli
expression in Escherichia coli
gene alyVI, expression of GST-fusion wild-type and mutant enzymes in Escherichia coli strain BL-21 LysS
-
gene of alginate lyase (AlyVI) from marine bacterium Vibrio is cloned into the multiple cloning site of the surface display vector pINA1317-YlCWP110 and expressed in cells of Yarrowia lipolytica
-
phylogenetic analysis, recombinant expression of His-tagged AlyA5 in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H311A
0.3% of wild-type activity
R199A
4.3% of wild-type activity
W467A
0.45% of wild-type activity
Y365F
0.011% of wild-type activity
K99A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
N120H
site-directed mutagenesis, reverse replacement of N120 by His in recAkAly30 increases the activity at pH 10.0 from 8 U/mg to 93 U/mg. However, the activity level at pH 7.0, i.e., 774.8 U/mg, is still much higher than that at pH 10.0
R128A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
S126A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
Y140F
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
Y142F
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
D152G
-
nearly inactive mutant
K162A
-
mutant shows comparable activity to wild-type enzyme
K196A
-
mutant shows comparable activity to wild-type enzyme
K95A
-
mutant is completely inactive
R110A
-
mutation causes 65% or more inactivation
R119A
-
mutation causes 65% or more inactivation
R92A
-
mutation causes 65% or more inactivation
A78S
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 820 U/mg, against poly(alpha-L-guluronic acid) 938 U/mg. Ratio of activities 1.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
A78S/T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 228 U/mg, against poly(alpha-L-guluronic acid) 34.3 U/mg. Ratio of activities 0.2; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
A78S/T89I/A217E
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 187 U/mg, against poly(alpha-L-guluronic acid) 29.8 U/mg. Ratio of activities 0.2; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
G26E
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 692 U/mg, against poly(alpha-L-guluronic acid) 787 U/mg. Ratio of activities 1.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
G26E/P39H
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 246 U/mg, against poly(alpha-L-guluronic acid) 19.5 U/mg. Ratio of activities 0.1. In the absence of Ca2+, no detectable activity against G-M linkages; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
G304V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 828 U/mg, against poly(alpha-L-guluronic acid) 878 U/mg. Ratio of activities 1.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
I51M
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 731 U/mg, against poly(alpha-L-guluronic acid) 786 U/mg. Ratio of activities 1.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
I51M/T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 227 U/mg, against poly(alpha-L-guluronic acid) 18.8 U/mg. Ratio of activities 0.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
P39H
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 356 U/mg, against poly(alpha-L-guluronic acid) 37 U/mg. Ratio of activities 0.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
P39T
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 216 U/mg, against poly(alpha-L-guluronic acid) 71 U/mg. Ratio of activities 0.3; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
S35R
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 443 U/mg, against poly(alpha-L-guluronic acid) 448 U/mg. Ratio of activities 1.0; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
S35R/P39T
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 32.6 U/mg, against poly(alpha-L-guluronic acid) 6.9 U/mg. Ratio of activities 0.2; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
S35R/P39T/A224V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 43 U/mg, against poly(alpha-L-guluronic acid) 3.4 U/mg. Ratio of activities 0.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
S37I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 53.8 U/mg, against poly(alpha-L-guluronic acid) 4.3 U/mg. Ratio of activities 0.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
S86L
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 31 U/mg, against poly(alpha-L-guluronic acid) 9.1 U/mg. Ratio of activities 0.3; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
T85A
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) 24.8 is U/mg, against poly(alpha-L-guluronic acid) 4.4 U/mg. Ratio of activities 0.32; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 218 U/mg, against poly(alpha-L-guluronic acid) 31 U/mg. Ratio of activities 0.1; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
V6I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is858 U/mg, against poly(alpha-L-guluronic acid) 851 U/mg. Ratio of activities 1.0; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
T85A
Klebsiella pneumoniae SM0524
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) 24.8 is U/mg, against poly(alpha-L-guluronic acid) 4.4 U/mg. Ratio of activities 0.32; random mutagenesis, mutant activities with and ratio of polyG (alpha-L-guluronic acid) to polyM (beta-D-mannuronic acid) compared to the wild-type enzyme
-
T89I
Klebsiella pneumoniae SM0524
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 218 U/mg, against poly(alpha-L-guluronic acid) 31 U/mg. Ratio of activities 0.1
-
K94A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
K97A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
R123A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
T121A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme, the replacement of T121 by Ala changes the substrate preference of LbAly28
Y135A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
Y137A
site-directed mutagenesis, the enzyme shows reduced activity compared to the wild-type enzyme
H202Q
-
inactive mutant
Y256F
-
inactive mutant
H202L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H415A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N201A
site-directed mutagenesis, inactive mutant
Q149A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R260A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R438A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y258A
site-directed mutagenesis, inactive mutant
Y450A
site-directed mutagenesis, inactive mutant
H202L
Saccharophagus degradans DSM 17024
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H415A
Saccharophagus degradans DSM 17024
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
N201A
Saccharophagus degradans DSM 17024
-
site-directed mutagenesis, inactive mutant
-
Y258A
Saccharophagus degradans DSM 17024
-
site-directed mutagenesis, inactive mutant
-
Y450A
Saccharophagus degradans DSM 17024
-
site-directed mutagenesis, inactive mutant
-
A270C
decrease in both KM value and maximum reaction velocity; site-directed mutagenesis, codon optimization, the mutant shows reduced activity compared to the wild-type enzyme
A328C
decrease in both KM value and maximum reaction velocity; site-directed mutagenesis, codon optimization, the mutant shows reduced activity compared to the wild-type enzyme
A41C
low maximum reaction velocities; site-directed mutagenesis, codon optimization, the mutant shows reduced activity compared to the wild-type enzyme
A53C
maximum reaction velocities similar to wild-type, decrease in KM value. Application of mutant to produce lyase-PEG conjugates with enhanced catalytic function and reduced immunoreactivity; site-directed mutagenesis, codon optimization, the mutant maintains Vmax values similar to the wild-type enzyme. Subsequent PEGylation produces a 60% increase in Vmax restoring the variant's maximum reaction velocity to wild-type levels while not altering the reduced Km value. The result is an enzyme-PEG conjugate with a 2fold improved catalytic efficiency compared to wild-type
E148A
-
mutant protein is insoluble
G60A
-
site-directed active site mutagenesis, the mutant shows 41.4% reduced activity compared to the wild-type enzyme
H188A
-
site-directed mutagenesis, the mutation switches the histidine 188 GTG codon to a CGC codon
H191A
-
Vmax is 7230fold lower than wild-type value
H191N/Y284F
-
crystal structure of mutant H191N/Y284F complexed with a tetrasaccharide bound at subsites -1 to +3 suggests that Gln189 functions as a neutralizer for the substrate carboxyl group, His191 as a general base, and Tyr284 as a general acid
H192A
-
site-directed mutagenesis, mutation of active site His residue, mutant shows highly reduced activity, ut no conformational change, insensitive against metyl-4-nitrobenzenesulfonate treatment
H192A
-
site-directed active site mutagenesis, almost inactive mutant
K280A
-
Vmax is 243fold lower than wild-type value
N141C/N199C
-
almost all molecules of N141C/N199C form a disulfide bond between Cys141 and Cys199. Crystal structure of N141C/N199C is determined at 2.1 A resolution by X-ray crystallography. Mutant has a glove-like beta- sandwich structure composed of four short alpha-helices and two beta-sheets. Two sulfate ions derived from the crystallization solution are accommodated at subsites +1 and +3. The loops of the mutant adopt the closed form. A disulfide bond between Cys141 and Cys199 forms in the absence of reducing agents; Km (mg/ml) (alginate): 0.32 (N141C/N199C + 0.5 mM DTT), 0.14 (N141C/N199C), Vmax (U/mg) (alginate): 7.1 (N141C/N199C + 0.5 mM DTT), 0.63 (N141C/N199C)
Q