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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.178 - beta-porphyranase and Organism(s) Zobellia galactanivorans and UniProt Accession D7GXF9

for references in articles please use BRENDA:EC3.2.1.178
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate [the other 30% are mostly agarobiose repeating units of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked 3,6-anhydro-alpha-L-galactopyranose] . This enzyme cleaves the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose, although some longer oligosaccharides of even number of residues are also observed. Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products . Methylation of the D-galactose prevents the enzyme from Zobellia galactanivorans, but not that from Wenyingzhuangia fucanilytica, from binding at subsite -1 [2,3].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Zobellia galactanivorans
UNIPROT: D7GXF9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Zobellia galactanivorans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran
Synonyms
porphyranase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-porphyranase A
-
endo-beta-porphyranase
-
-
-
-
PORB
-
-
-
-
porphyranase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
porphyran beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate 4-glycanohydrolase
The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate [the other 30% are mostly agarobiose repeating units of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked 3,6-anhydro-alpha-L-galactopyranose] [2]. This enzyme cleaves the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose, although some longer oligosaccharides of even number of residues are also observed. Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products [1]. Methylation of the D-galactose prevents the enzyme from Zobellia galactanivorans, but not that from Wenyingzhuangia fucanilytica, from binding at subsite -1 [2,3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agarose + H2O
?
show the reaction diagram
-
-
-
?
natural agar + H2O
?
show the reaction diagram
extracted from Porphyra umbilicalis or from Gracilaria sp.
-
-
?
porphyran + H2O
alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + ?
show the reaction diagram
the enzyme cleaves the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside, although some longer oligosaccharides of even number of residues are also observed. Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products
-
-
?
agarose + H2O
?
show the reaction diagram
-
-
-
?
natural agar + H2O
?
show the reaction diagram
extracted from Porphyra umbilicalis or from Gracilaria sp.
-
-
?
porphyran + H2O
alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + ?
show the reaction diagram
the enzyme cleaves the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose, although some longer oligosaccharides of even number of residues are also observed. Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products
-
-
?
porphyran + H2O
alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + oligosaccharides derived from porphyran
show the reaction diagram
the backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate. The other 30% are mostly agarobiose repeating units of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked 3,6-anhydro-alpha-L-galactopyranose. Methylation of the D-galactose prevents its binding at position -1. The disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose and oligosaccharides of the alpha-L-Galp-6-sulfate-(1->3)-beta-D-Galp series are the major final product
-
-
?
additional information
?
-
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
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the marine Bacteroidetes possesses a complex agarolytic system comprising four betaa-agarases and five beta-porphyranases, all belonging to the glycoside hydrolase family 16, GH16, degradation patterns and structure comparisons, overview
evolution
the marine Bacteroidetes possesses a complex agarolytic system comprising four beta-agarases and five beta-porphyranases, all belonging to the glycoside hydrolase family 16, GH16, degradation patterns and structure comparisons, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of PorB in complex with a porphyran tetrasaccharide
crystal structures of an inactivated mutant (E139S) of PorA in complex with a porphyran tetrasaccharide
purified recombinant catalytic domain of PorA, hanging drop vapour diffusion method, mixing of 0.002 ml of 2.6 mg/ml protein solution with 0.001 ml of crytallization solution and equilibration against a 0.5 ml reservoir, X-ray diffraction structure determination and analysis at 1.1 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E139S
inactive mutant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant N-terminal His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene porB, phylogenetic analysis, expression N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
gene porA, phylogenetic analysis, expression of N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3)
His-tagged expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Correc, G.; Hehemann, J.H.; Czjzek, M.; Helbert, W.
Structural analysis of the degradation products of porphyran digested by Zobellia galactanivorans ?-porphyranase A
Carbohydr. Polym.
83
277-283
2011
Zobellia galactanivorans (D7GXG0)
Manually annotated by BRENDA team
Hehemann, J.H.; Correc, G.; Barbeyron, T.; Helbert, W.; Czjzek, M.; Michel, G.
Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota
Nature
464
908-912
2010
Zobellia galactanivorans (D7GXF9), Zobellia galactanivorans (D7GXG0)
Manually annotated by BRENDA team
Hehemann, J.H.; Correc, G.; Thomas, F.; Bernard, T.; Barbeyron, T.; Jam, M.; Helbert, W.; Michel, G.; Czjzek, M.
Biochemical and structural characterization of the complex agarolytic enzyme system from the marine bacterium Zobellia galactanivorans
J. Biol. Chem.
287
30571-30584
2012
Zobellia galactanivorans (D7GXF9), Zobellia galactanivorans (D7GXG0), Zobellia galactanivorans DSM 12802 (D7GXF9), Zobellia galactanivorans DSM 12802 (D7GXG0)
Manually annotated by BRENDA team