Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.98 3'-NADP+ noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 3-acetylpyridine adenine dinucleotide phosphate oxidized form, competitive with respect to NADPH Escherichia coli
1.3.1.98 ADP at high concentration, competitive with respect to NADPH Escherichia coli
1.3.1.98 ADP-ribose at high concentration, competitive with respect to NADPH Escherichia coli
1.3.1.98 NADP+ noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 NADPH substrate inhibition at pH 7.0, Ki: 1.6 mM Escherichia coli
1.3.1.98 nicotinamide 1,N6-ethenoadenine dinucleotide phosphate oxidized form, noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 nicotinamide hypoxanthine dinucleotide phosphate oxidized form, noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 thio-NADP+ noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 UDP at high concentration, noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 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
1.3.1.98 uridine diphospho-N-acetylglucosamine at very high concentration, noncompetitive with respect to NADPH Escherichia coli
1.3.1.98 uridine diphospho-N-acetylmuramic acid uncompetitive with respect to NADPH Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.98 0.02
-
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine in the presence of 50 mM K+ Escherichia coli
1.3.1.98 0.022
-
NADPH in the presence of 50 mM K+ Escherichia coli

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.98 38340
-
electrospray mass spectrometry of recombinant protein Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.98 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.98
-
Escherichia coli

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.98 8
-
-
Escherichia coli

Cofactor

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