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Literature summary for 1.1.1.37 extracted from

  • Tylicki, A.; Ziolkowska, G.; Bolkun, A.; Siemieniuk, M.; Czerniecki, J.; Nowakiewicz, A.
    Comparative study of the activity and kinetic properties of malate dehydrogenase and pyruvate decarboxylase from Candida albicans, Malassezia pachydermatis, and Saccharomyces cerevisiae (2008), Can. J. Microbiol., 54, 734-741.
    View publication on PubMed
Search for more literature for 1.1.1.37

Activating Compound

Activating Compound Comment Organism Structure
additional information highest MDH activity under aerobic conditions Malassezia pachydermatis

Inhibitors

Inhibitors Comment Organism Structure
additional information strong decrease in MDH activity under aerobic conditions Candida albicans
additional information strong decrease in MDH activity under aerobic conditions Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.036
-
 oxaloacetate in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2 Malassezia pachydermatis
0.041
-
 oxaloacetate in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2 Candida albicans
0.081
-
 oxaloacetate in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Candida albicans
-
-
-
Malassezia pachydermatis
-
-
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
 Saccharomyces cerevisiae oxaloacetate + NADH + H+
-
 ?
(S)-malate + NAD+
-
 Candida albicans oxaloacetate + NADH + H+
-
 r
(S)-malate + NAD+
-
 Malassezia pachydermatis oxaloacetate + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
MDH
-
 Saccharomyces cerevisiae
MDH
-
 Candida albicans
MDH
-
 Malassezia pachydermatis

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Saccharomyces cerevisiae
NADH
-
 Candida albicans
NADH
-
 Malassezia pachydermatis