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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General Information
General Information on EC 3.2.1.178 - beta-porphyranase
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evolution
additional information
the enzyme belongs to the glycoside hydrolase family 16, GH16, encoded in a polysaccharide utilization locus (PUL) obtained by horizontal gene transfer by the gut bacterium Bacteroides plebeius, genetic analysis, overview
evolution
the enzyme belongs to the glycoside hydrolase family 86, GH86, encoded in a polysaccharide utilization locus (PUL) obtained by horizontal gene transfer by the gut bacterium Bacteroides plebeius, genetic analysis, 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
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 enzyme belongs to the glycoside hydrolase family 16, GH16, encoded in a polysaccharide utilization locus (PUL) obtained by horizontal gene transfer by the gut bacterium Bacteroides plebeius, genetic analysis, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 86, GH86, encoded in a polysaccharide utilization locus (PUL) obtained by horizontal gene transfer by the gut bacterium Bacteroides plebeius, genetic analysis, overview
-
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
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most intriguing feature in native PorAcat is the presence of a short loop insertion (residues 238-245), that protrudes into the active site cleft and binds at place of the -1-binding site
additional information
most intriguing feature in native PorAcat is the presence of a short loop insertion (residues 238-245), that protrudes into the active site cleft and binds at place of the -1-binding site
additional information
the enzyme shows a multidomain architecture consisting of an N-terminal (beta/alpha)8 barrel and two C-terminal beta-sandwich domains, which align via their convex faces to the exterior of the (beta/alpha)8 barrel and connect with two N-terminal beta-strands that become part of these C-terminal beta-sandwich domains. The distal part of the barrel lacks the helix alpha2 in the outer ring and parts of the surface loops, which form the rim in the canonical (beta/alpha)8 barrel fold
additional information
the enzyme shows a multidomain architecture consisting of an N-terminal (beta/alpha)8 barrel and two C-terminal beta-sandwich domains, which align via their convex faces to the exterior of the (beta/alpha)8 barrel and connect with two N-terminal beta-strands that become part of these C-terminal beta-sandwich domains. The distal part of the barrel lacks the helix alpha2 in the outer ring and parts of the surface loops, which form the rim in the canonical (beta/alpha)8 barrel fold
additional information
-
the enzyme shows a multidomain architecture consisting of an N-terminal (beta/alpha)8 barrel and two C-terminal beta-sandwich domains, which align via their convex faces to the exterior of the (beta/alpha)8 barrel and connect with two N-terminal beta-strands that become part of these C-terminal beta-sandwich domains. The distal part of the barrel lacks the helix alpha2 in the outer ring and parts of the surface loops, which form the rim in the canonical (beta/alpha)8 barrel fold
additional information
-
the enzyme shows a multidomain architecture consisting of an N-terminal (beta/alpha)8 barrel and two C-terminal beta-sandwich domains, which align via their convex faces to the exterior of the (beta/alpha)8 barrel and connect with two N-terminal beta-strands that become part of these C-terminal beta-sandwich domains. The distal part of the barrel lacks the helix alpha2 in the outer ring and parts of the surface loops, which form the rim in the canonical (beta/alpha)8 barrel fold
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additional information
-
most intriguing feature in native PorAcat is the presence of a short loop insertion (residues 238-245), that protrudes into the active site cleft and binds at place of the -1-binding site
-