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Literature summary for 1.2.1.23 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
Search for more literature for 1.2.1.23

Cloned(Commentary)

Cloned (Comment) Organism
gene ADH1, sequence comparisons Candida albicans

Protein Variants

Protein Variants Comment Organism
additional information generation of ADH1 gene disruption mutants Candida albicans

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Candida albicans A0A1D8PP43
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NAD+ specific for Candida albicans
NADH
-
 Candida albicans

Expression

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

General Information

General Information Comment Organism
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
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]

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