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Literature summary extracted from

  • Kwak, M.K.; Ku, M.; Kang, S.O.
    NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans (2014), FEBS Lett., 588, 1144-1153 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.1 gene ADH1, sequence comparisons Candida albicans
1.2.1.23 gene ADH1, sequence comparisons Candida albicans

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.1 additional information generation of ADH1 gene disruption mutants Candida albicans
1.2.1.23 additional information generation of ADH1 gene disruption mutants Candida albicans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.23 0.0385
-
 pyruvate pH and temperature not specified in the publication Candida albicans
1.2.1.23 0.97
-
 methylglyoxal pH and temperature not specified in the publication Candida albicans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.1 methylglyoxal + NADH + H+ Candida albicans
-
 acetol + NAD+
-
 r
1.2.1.23 methylglyoxal + NAD+ + H2O Candida albicans
-
 pyruvate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Candida albicans A0A1D8PP43
-
-
1.2.1.23 Candida albicans A0A1D8PP43
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.23 8.27
-
 purified native enzyme, pH and temperature not specified in the publication Candida albicans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 methylglyoxal + NADH + H+
-
 Candida albicans acetol + NAD+
-
 r
1.1.1.1 additional information Candida albicans ADH1 is a bifunctional enzyme that catalyzes methylglyoxal oxidation and reduction, cf. EC 1.2.1.23 Candida albicans ?
-
 ?
1.2.1.23 methylglyoxal + NAD+ + H2O
-
 Candida albicans pyruvate + NADH + H+
-
 r
1.2.1.23 methylglyoxal + NAD+ + H2O the reduction reaction is highly preferred Candida albicans pyruvate + NADH + H+
-
 r
1.2.1.23 additional information Candida albicans ADH1 is a bifunctional enzyme that catalyzes methylglyoxal oxidation and reduction, cf. EC 1.1.1.1 Candida albicans ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 ADH1
-
 Candida albicans
1.1.1.1 alpha-ketoaldehyde dehydrogenase
-
 Candida albicans
1.1.1.1 MGD
-
 Candida albicans
1.1.1.1 NAD+-linked alcohol dehydrogenase 1
-
 Candida albicans
1.1.1.1 NAD+-linked methylglyoxal dehydrogenase
-
 Candida albicans
1.2.1.23 ADH1
-
 Candida albicans
1.2.1.23 alpha-ketoaldehyde dehydrogenase
-
 Candida albicans
1.2.1.23 MGD
-
 Candida albicans
1.2.1.23 NAD+-linked alcohol dehydrogenase 1
-
 Candida albicans
1.2.1.23 NAD+-linked methylglyoxal dehydrogenase
-
 Candida albicans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.23 18.17
-
 methylglyoxal pH and temperature not specified in the publication Candida albicans
1.2.1.23 170
-
 pyruvate pH and temperature not specified in the publication Candida albicans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+ specific for Candida albicans
1.1.1.1 NADH
-
 Candida albicans
1.2.1.23 NAD+ specific for Candida albicans
1.2.1.23 NADH
-
 Candida albicans

Expression

EC Number Organism Comment Expression
1.1.1.1 Candida albicans the enzyme activity is highly induced in glutathione GSH-deficient cells up
1.2.1.23 Candida albicans the enzyme activity is highly induced in glutathione GSH-deficient cells up

General Information

EC Number General Information Comment Organism
1.1.1.1 malfunction methylglyoxal accumulation leads to G2-phase arrest by affecting cell growth, ROS production, viability, differentiation, and virulence. Phenotypes of enzyme-deficient cells, overview Candida albicans
1.1.1.1 physiological function the enzyme catalyzes both methylglyoxal oxidation to pyruvate as well as its reduction to acetol. ADH1 activity likely shifts between methylglyoxal oxidation and reduction with a marked change in the intracellular redox state during the growth, such as GSH starvation. The enzyme is required for regulation of methylglyoxal content in the cell. Mgd activity is highly induced in GSH-deficient cells Candida albicans
1.2.1.23 malfunction methylglyoxal accumulation leads to G2-phase arrest by affecting cell growth, ROS production, viability, differentiation, and virulence. Phenotypes of enzyme-deficient cells, overview Candida albicans
1.2.1.23 physiological function the enzyme catalyzes both methylglyoxal oxidation to pyruvate as well as its reduction to acetol. ADH1 activity likely shifts between methylglyoxal oxidation and reduction with a marked change in the intracellular redox state during the growth, such as GSH starvation. The enzyme is required for regulation of methylglyoxal content in the cell. Mgd activity is highly induced in GSH-deficient cells Candida albicans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.23 18.73
-
 methylglyoxal pH and temperature not specified in the publication Candida albicans
1.2.1.23 4415.6
-
 pyruvate pH and temperature not specified in the publication Candida albicans