3.2.1.178: beta-porphyranase
This is an abbreviated version!
For detailed information about beta-porphyranase, go to the full flat file.
Reaction
hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6-sulfate linkages in porphyran =
Synonyms
beta-porphyranase A, BpGH16B, BpGH86A, endo-beta-porphyranase, PORA, PORB, porphyranase
ECTree
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Substrates Products
Substrates Products on EC 3.2.1.178 - beta-porphyranase
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REACTION DIAGRAM
porphyran + H2O
alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + oligosaccharides derived from porphyran
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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extracted from Porphyra umbilicalis or from Gracilaria sp.
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natural agar + H2O
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extracted from Porphyra umbilicalis or from Gracilaria sp.
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alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + ?
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
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porphyran + H2O
alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactopyranoside + ?
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
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additional information
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the enzyme degrades porphyran
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additional information
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the enzyme degrades porphyran
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additional information
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beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite
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additional information
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beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite
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additional information
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beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite
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additional information
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beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite
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?
additional information
?
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beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite
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?
additional information
?
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beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorB tolerates the presence of 3-6-anhydro-L-galactose in subsite -2 it does not accept methylation of the galactose unit in the -1 subsite
-
-
?
additional information
?
-
beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite
-
-
?
additional information
?
-
beta-porphyranases degrade the sulfated polymers found in various quantities in natural agars. PorA displays a strict requirement for C6-sulfate in the -2- and +1-binding subsites, it does not accept methylation of the galactose unit in the -1 subsite
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?