ENZYME entry: EC 3.2.1.178
Accepted Name |
Beta-porphyranase.
|
Alternative Name(s) |
Endo-beta-porphyranase. |
Porphyranase. |
Reaction catalysed |
Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran |
Comment(s) |
- The backbone of porphyran consists largely (approximately 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 position -1.
|
Cross-references |
BRENDA | 3.2.1.178 |
EC2PDB | 3.2.1.178 |
ExplorEnz | 3.2.1.178 |
PRIAM enzyme-specific profiles | 3.2.1.178 |
KEGG Ligand Database for Enzyme Nomenclature | 3.2.1.178 |
IUBMB Enzyme Nomenclature | 3.2.1.178 |
IntEnz | 3.2.1.178 |
MEDLINE | Find literature relating to 3.2.1.178 |
MetaCyc | 3.2.1.178 |
UniProtKB/Swiss-Prot |
|
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