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Literature summary for 1.1.1.69 extracted from

  • Ameyama, M.; Adachi, O.
    5-keto-D-Gluconate reductase from Gluconobacter suboxydans (1982), Methods Enzymol., 89, 198-202.
No PubMed abstract available

General Stability

General Stability Organism
75% loss of activity within a few days unless either D-gluconate or 5-dehydro-D-gluconate is added during storage or purification Gluconobacter oxydans

Inhibitors

Inhibitors Comment Organism Structure
Hg2+
-
Gluconobacter oxydans
PCMB
-
Gluconobacter oxydans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
NADPH
-
Gluconobacter oxydans
0.02
-
NADP+
-
Gluconobacter oxydans
0.9
-
5-Dehydro-D-gluconate
-
Gluconobacter oxydans
20
-
D-gluconate
-
Gluconobacter oxydans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
4 * 25000, SDS-PAGE Gluconobacter oxydans
100000
-
gel filtration Gluconobacter oxydans
110000
-
gel filtration Gluconobacter oxydans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-dehydro-D-gluconate + NADPH Gluconobacter oxydans the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+ D-gluconate + NADP+
-
?
5-dehydro-D-gluconate + NADPH Gluconobacter oxydans maximum enzyme formation at the end of the exponential growth, in the decreasing growth phase, about 65% of the maximum enzyme activity remains D-gluconate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
IFO 12528
-

Purification (Commentary)

Purification (Comment) Organism
-
Gluconobacter oxydans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
69.69
-
-
Gluconobacter oxydans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-dehydro-D-gluconate + NADPH the rate of D-gluconate oxidation is about 60% of the rate of 5-keto-D-gluconate reduction Gluconobacter oxydans D-gluconate + NADP+
-
r
5-dehydro-D-gluconate + NADPH the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+ Gluconobacter oxydans D-gluconate + NADP+
-
?
5-dehydro-D-gluconate + NADPH maximum enzyme formation at the end of the exponential growth, in the decreasing growth phase, about 65% of the maximum enzyme activity remains Gluconobacter oxydans D-gluconate + NADP+
-
?
D-gluconate + NADP+ the rate of D-gluconate oxidation is about 60% of the rate of 5-keto-D-gluconate reduction Gluconobacter oxydans 5-dehydro-D-gluconate + NADPH
-
r

Subunits

Subunits Comment Organism
tetramer 4 * 25000, SDS-PAGE Gluconobacter oxydans

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
50
-
reduction of 5-dehydro-D-gluconate and oxidation of D-gluconate Gluconobacter oxydans

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
additional information
-
thermal stability is enhanced by addition of either D-gluconate or 5-keto-D-gluconate, or both Gluconobacter oxydans
40
-
loss of activity after a few min Gluconobacter oxydans
55
-
5 min, in presence of D-gluconate or 5-dehydro-D-gluconate, even at 0.0001 mg/ml protein Gluconobacter oxydans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
reduction of 5-dehydro-D-gluconate Gluconobacter oxydans
10
-
oxidation of D-gluconate in presence of NADP+ Gluconobacter oxydans

Cofactor

Cofactor Comment Organism Structure
NADP+ cofactor Gluconobacter oxydans
NADPH cofactor Gluconobacter oxydans