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Literature summary for 1.3.1.98 extracted from

  • Benson, T.E.; Marquardt, J.L.; Marquardt, A.C.; Etzkorn, F.A.; Walsh, C.T.
    Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase (1993), Biochemistry, 32, 2024-2030.
    View publication on PubMed
Search for more literature for 1.3.1.98

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli XA90F'lacIQ1 Escherichia coli

Protein Variants

Protein Variants Comment Organism
S229A by site-directed mutagenesis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0125
-
 UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine
-
 Escherichia coli
0.0199
-
 NADPH
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37850
-
 determined by cDNA sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH Escherichia coli
-
 UDP-N-acetyl-3-D-muramate + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
31.4
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH
-
 Escherichia coli UDP-N-acetyl-3-D-muramate + NADP+
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD tightly bound flavin cofactor FAD Escherichia coli
NADPH
-
 Escherichia coli