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Literature summary for 5.1.3.29 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
Search for more literature for 5.1.3.29

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-L-fucopyranose Escherichia coli
-
 beta-L-fucopyranose
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEN8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-L-fucopyranose
-
 Escherichia coli beta-L-fucopyranose
-
 r
alpha-L-fucopyranose FucU binds to both alpha- and beta-fucopyranose and accelerates the conversion between them Escherichia coli beta-L-fucopyranose
-
 r
additional information FucU exhibits a pyranase activity for D-ribose. No activity with D-glucose, L-rhamnose and D-fucose Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More FucU seems to require multimeric or dimeric structures for its enzymatic activity, because the N-terminally His-tagged FucU is an inactive monomer Escherichia coli

Synonyms

Synonyms Comment Organism
FucU
-
 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
27.9
-
 alpha-L-fucopyranose pH 7.5, temperature not specified in the publication Escherichia coli
65.1
-
 beta-L-fucopyranose pH 7.5, temperature not specified in the publication Escherichia coli