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Literature summary for 1.1.1.271 extracted from

  • Menon, S.; Stahl, M.; Kumar, R.; Xu, G.Y.; Sullivan, F.
    Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli (1999), J. Biol. Chem., 274, 26743-26750.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
GDP competitive with respect to GDP-4-keto-6-deoxymannose Escherichia coli
GDP-fucose competitive with respect to NADPH and GDP-4-keto-6-deoxymannose Escherichia coli
NADP competitive inhibitor Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
 NADPH
-
 Escherichia coli
0.109
-
 NADH
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADH + H+
-
 Escherichia coli GDP-beta-L-fucose + NAD+
-
 r
GDP-4-keto-6-deoxy-D-mannose + NADPH catalyzes the stereospecific hydride transfer of the ProS hydrogen from NADPH to carbon 4 of the mannose sugar Escherichia coli GDP-6-deoxy-L-galactose + NADP+
-
 ?
GDP-4-keto-6-deoxy-D-mannose + NADPH enzyme also utilizes NADH but with lower affinity Escherichia coli GDP-6-deoxy-L-galactose + NADP+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADH enzyme has lower affinity for NADH as compared with NADPH Escherichia coli
NADPH
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.055
-
 GDP-fucose
-
 Escherichia coli
0.061
-
 GDP
-
 Escherichia coli
0.069
-
 NADP+
-
 Escherichia coli