From Wikipedia, the free encyclopedia
3-O-alpha-D-glucosyl-L-rhamnose phosphorylase
Identifiers
EC no. 2.4.1.282
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

3-O-alpha-D-glucosyl-L-rhamnose phosphorylase ( EC 2.4.1.282, cphy1019 (gene)) is an enzyme with systematic name 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose:phosphate beta-D-glucosyltransferase. [1] This enzyme catalyses the following chemical reaction

3-O-alpha-D-glucopyranosyl-L-rhamnopyranose + phosphate L- rhamnopyranose + beta-D-glucose 1-phosphate

In the reverse phosphorolysis reaction the enzyme is specific for L- rhamnose as acceptor and beta-D-glucose 1-phosphate as donor.

References

  1. ^ Nihira T, Nakai H, Kitaoka M (March 2012). "3-O-α-D-glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans". Carbohydrate Research. 350: 94–7. doi: 10.1016/j.carres.2011.12.019. PMID  22277537.

External links

From Wikipedia, the free encyclopedia
3-O-alpha-D-glucosyl-L-rhamnose phosphorylase
Identifiers
EC no. 2.4.1.282
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

3-O-alpha-D-glucosyl-L-rhamnose phosphorylase ( EC 2.4.1.282, cphy1019 (gene)) is an enzyme with systematic name 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose:phosphate beta-D-glucosyltransferase. [1] This enzyme catalyses the following chemical reaction

3-O-alpha-D-glucopyranosyl-L-rhamnopyranose + phosphate L- rhamnopyranose + beta-D-glucose 1-phosphate

In the reverse phosphorolysis reaction the enzyme is specific for L- rhamnose as acceptor and beta-D-glucose 1-phosphate as donor.

References

  1. ^ Nihira T, Nakai H, Kitaoka M (March 2012). "3-O-α-D-glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans". Carbohydrate Research. 350: 94–7. doi: 10.1016/j.carres.2011.12.019. PMID  22277537.

External links


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