Information on EC 3.2.1.178 - beta-porphyranase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.178
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RECOMMENDED NAME
GeneOntology No.
beta-porphyranase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
porphyran degradation
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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 its binding at position -1 [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
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
porphyran + H2O
alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + ?
show the reaction diagram
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
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2)
Bacteroides plebeius (strain DSM 17135 / JCM 12973 / M2)
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme comprising the catalytic domain (residues 25-599) in complex with product, X-ray diffraction structure determiation and analysis at 1.3 A resolution
crystal structures of an inactivated mutant (E139S) of PorA in complex with a porphyran tetrasaccharide; crystal structures of PorB 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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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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; expression in Escherichia coli
gene BACPLE_01689, encoded in a polysaccharide utilization locus (PUL) obtained by horizontal gene transfer by the gut bacterium Bacteroides plebeius, DNA and amino acid sequence determination and analysis; gene BACPLE_01693, encoded in a polysaccharide utilization locus (PUL) obtained by horizontal gene transfer by the gut bacterium Bacteroides plebeius, DNA and amino acid sequence determination and analysis
gene porA, phylogenetic analysis, expression of N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3); gene porB, phylogenetic analysis, expression N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3)
His-tagged expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
porphyran induces the gene locus encoding gene BACPLE_01689; porphyran induces the gene locus encoding gene BACPLE_01693
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E139S
inactive mutant enzyme