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NAD + ‐linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans
Author(s) -
Kwak Min-Kyu,
Ku MyungHee,
Kang Sa-Ouk
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.02.042
Subject(s) - methylglyoxal , nad+ kinase , biochemistry , candida albicans , glutathione , lactoylglutathione lyase , chemistry , alcohol dehydrogenase , dehydrogenase , aldehyde dehydrogenase , corpus albicans , intracellular , enzyme , microbiology and biotechnology , yeast , biology
We purified a fraction that showed NAD + ‐linked methylglyoxal dehydrogenase activity, directly catalyzing methylglyoxal oxidation to pyruvate, which was significantly increased in glutathione‐depleted Candida albicans . It also showed NADH‐linked methylglyoxal‐reducing activity. The fraction was identified as a NAD + ‐linked alcohol dehydrogenase (ADH1) through mass spectrometric analyses. In ADH1 ‐disruptants of both the wild type and glutathione‐depleted cells, the intracellular methylglyoxal concentration increased significantly; defects in growth, differentiation, and virulence were observed; and G2‐phase arrest was induced.