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Literature summary for 5.4.99.62 extracted from

  • Ryu, K.S.; Kim, C.; Kim, I.; Yoo, S.; Choi, B.S.; Park, C.
    NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration (2004), J. Biol. Chem., 279, 25544-25548.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H106A the mutant enzyme retains one-third of the original pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does, Escherichia coli
H20A mutation completely abolishes the pyranase activity, the mutant proteins are able to form an oligomer as is the case for the wild type, mutant binds to ribose as much as the wild type does, Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-ribopyranose Escherichia coli
-
 beta-D-ribofuranose
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P04982
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-allopyranose
-
 Escherichia coli beta-allofuranose
-
 ?
beta-D-ribopyranose
-
 Escherichia coli beta-D-ribofuranose
-
 ?

Subunits

Subunits Comment Organism
More the enzyme seems to require multimeric or dimeric structure for their enzymatic activity Escherichia coli

Synonyms

Synonyms Comment Organism
RbsD
-
 Escherichia coli