Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.2.11 - guluronate-specific alginate lyase and Organism(s) Corynebacterium sp. ALY-1 and UniProt Accession Q9RB42

for references in articles please use BRENDA:EC4.2.2.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.11 guluronate-specific alginate lyase
IUBMB Comments
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Corynebacterium sp. ALY-1
UNIPROT: Q9RB42
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Corynebacterium sp. ALY-1
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
algmytc, guluronate-specific alginate lyase, guluronate lyase, alya1pl7, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alginase II
-
-
-
-
guluronate lyase
-
-
-
-
L-guluronan lyase
-
-
-
-
L-guluronate lyase
-
-
-
-
lyase, polyguluronate
-
-
-
-
poly(1,4-alpha-L-guluronide)lyase
-
-
-
-
poly(alpha-L-guluronate) lyase
-
-
-
-
poly-alpha-L-guluronate lyase
-
-
-
-
polyguluronate-specific alginate lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination of an alcohol from a polysaccharide
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
alginate alpha-L-guluronate-uronate lyase
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
CAS REGISTRY NUMBER
COMMENTARY hide
64177-88-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-L-guluronosyl linkage in alginate
?
show the reaction diagram
-
endolyase
-
-
?
poly-alpha-L-guluronic acid
?
show the reaction diagram
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
show the reaction diagram
-
-
-
?
saturated deca((1-4)-alpha-L-guluronan)
?
show the reaction diagram
-
-
-
-
?
saturated hepta((1-4)-alpha-L-guluronan)
?
show the reaction diagram
-
-
-
-
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
show the reaction diagram
-
rapidly degraded in the endolytic mode, enzyme has a subsite corresponding to hexa((1-4)-alpha-L-guluronan) units, cleaving the substrate between subsites two and three from the non-reducing end
main products, the catalytic site is matched to the linkage between the second and the third uronic residue from the non-reducing end, the degradation of tri((1-4)-alpha-L-guluronan) does not apparently occur
?
saturated tetra((1-4)-alpha-L-guluronan)
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
show the reaction diagram
-
-
-
?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9RB42_9CORY
256
0
27344
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 27000, SDS-PAGE
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsubara, Y.; Kawada, R.; Iwasaki, K.; Oda, T.; Muramatsu, T.
Extracellular poly(alpha-L-guluronate)lyase from Corynebacterium sp.: purification, characteristics, and conformational properties
J. Protein Chem.
17
29-36
1998
Corynebacterium sp., Corynebacterium sp. ALY-1
Manually annotated by BRENDA team
Matsubara, Y.; Iwasaki, K.I.; Muramatsu, T.
Action of poly(alpha-L-guluronate) lyase from Corynebacterium sp. ALY-1 strain on saturated oligoguluronates
Biosci. Biotechnol. Biochem.
62
1055-1060
1998
Corynebacterium sp., Corynebacterium sp. ALY-1
Manually annotated by BRENDA team