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Literature summary for 1.1.1.49 extracted from

  • Olavarria, K.; Valdes, D.; Cabrera, R.
    The cofactor preference of glucose-6-phosphate dehydrogenase from Escherichia coli - modeling the physiological production of reduced cofactors (2012), FEBS J., 279, 2296-2309.
    View publication on PubMed
Search for more literature for 1.1.1.49

Inhibitors

Inhibitors Comment Organism Structure
NADPH product inhibition with NADP+ or D-glucose 6-phosphate as the varying substrate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0075
-
 NADP+ 25°C, pH 8.0 Escherichia coli
0.174
-
 D-glucose 6-phosphate 25°C, pH 8.0, cofactor: NADP+ Escherichia coli
1.25
-
 D-glucose 6-phosphate 25°C, pH 8.0, cofactor: NAD+ Escherichia coli
5.09
-
 NAD+ 25°C, pH 8.0 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose 6-phosphate + NADP+ Escherichia coli first enzyme of the pentose phosphate pathway, one of the main sources of NADPH 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
 ?

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.
D-glucose 6-phosphate + NAD+ NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADH + H+
-
 ?
D-glucose 6-phosphate + NADP+ first enzyme of the pentose phosphate pathway, one of the main sources of NADPH Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
 ?
D-glucose 6-phosphate + NADP+ NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme. Modeling of the sensitivity of reduced cofactor production by G6PDH as a function of the redox ratios of NAD/NADH (rRNAD) and NADP/NADPH (rRNADP). NADPH production sharply increases within the range of thermodynamically feasible values of rRNADP, but NADH production remains low within the range feasible for rRNAD Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
 ?

Synonyms

Synonyms Comment Organism
G6PDH
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
174
-
 NADP+ 25°C, pH 8.0 Escherichia coli
288
-
 NAD+ 25°C, pH 8.0 Escherichia coli

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+ NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme Escherichia coli
NADP+ NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme. Modeling of the sensitivity of reduced cofactor production by G6PDH as a function of the redox ratios of NAD/NADH (rRNAD) and NADP/NADPH (rRNADP). NADPH production sharply increases within the range of thermodynamically feasible values of rRNADP, but NADH production remains low within the range feasible for rRNAD Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.038
-
 NADPH 25°C, pH 8.0, competitive inhibition constant Escherichia coli
2.09
-
 NADPH 25°C, pH 8.0, non-competitive inhibition constant Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
56
-
 NAD+ 25°C, pH 8.0 Escherichia coli
23200
-
 NADP+ 25°C, pH 8.0 Escherichia coli