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Literature summary for 1.3.1.98 extracted from

  • Dhalla, A.M.; Yanchunas, J.Jr.; Ho, H.T.; Falk, P.J.; Villafranca, J.J.; Robertson, J.G.
    Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase (1995), Biochemistry, 34, 5390-5402.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of protein in Escherichia coli strain JM109 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3'-NADP+ noncompetitive with respect to NADPH Escherichia coli
3-acetylpyridine adenine dinucleotide phosphate oxidized form, competitive with respect to NADPH Escherichia coli
ADP at high concentration, competitive with respect to NADPH Escherichia coli
ADP-ribose at high concentration, competitive with respect to NADPH Escherichia coli
NADP+ noncompetitive with respect to NADPH Escherichia coli
NADPH substrate inhibition at pH 7.0, Ki: 1.6 mM Escherichia coli
nicotinamide 1,N6-ethenoadenine dinucleotide phosphate oxidized form, noncompetitive with respect to NADPH Escherichia coli
nicotinamide hypoxanthine dinucleotide phosphate oxidized form, noncompetitive with respect to NADPH Escherichia coli
thio-NADP+ noncompetitive with respect to NADPH Escherichia coli
UDP at high concentration, noncompetitive with respect to NADPH Escherichia coli
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine substrate inhibition at pH 6, Ki 0.01 mM with 0.15 mM NADPH, weaker at more basic pH Escherichia coli
uridine diphospho-N-acetylglucosamine at very high concentration, noncompetitive with respect to NADPH Escherichia coli
uridine diphospho-N-acetylmuramic acid uncompetitive with respect to NADPH Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine in the presence of 50 mM K+ Escherichia coli
0.022
-
NADPH in the presence of 50 mM K+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Cs+ at saturating cation concentration maximal enzyme activity: 2 units/mg Escherichia coli
K+ at saturating cation concentration maximal enzyme activity: 50 units/mg Escherichia coli
K+ without monovalent cations, only minimium enzyme activity Escherichia coli
additional information divalent cations have no activating effect Escherichia coli
Na+ at saturating cation concentration maximal enzyme activity: 5 units/mg Escherichia coli
NH4+ at saturating cation concentration maximal enzyme activity: 35 units/mg Escherichia coli
Rb+ at saturating cation concentration maximal enzyme activity: 33 units/mg Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38340
-
electrospray mass spectrometry of recombinant protein 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

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+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol FAD per mol enzyme bound Escherichia coli
additional information NADH not substrate Escherichia coli
additional information thio-NADPH not substrate Escherichia coli
NADPH
-
Escherichia coli