In contrast to previously studied non-fermentative arginine-hydrolysing (F-/A+) Mycoplasma species, M. gallinarum cells suspended in a salts solution oxidised ethanol and L-lactic, pyruvic and 2-oxobutyric acids. The organic acids were additionally shown effectively to replace arginine as energy sources in
1-Deoxy-d-xylulose 5-phosphate synthase (DXP synthase) catalyzes the thiamine diphosphate (TPP)-dependent condensation of pyruvate and d-glyceraldehyde 3-phosphate (GAP) to yield DXP in the first step of the methylerythritol phosphate pathway for isoprenoid biosynthesis. Steady-state kinetic constants for DXP synthase calculated from
Fluoropyruvate: a potent inhibitor of the bacterial and the mammalian pyruvate dehydrogenase complex.
H Bisswanger
Biochemical and biophysical research communications, 95(2), 513-519 (1980-07-31)
Archives of biochemistry and biophysics, 369(2), 277-287 (1999-09-16)
Pyruvate dehydrogenase (E1), a heterotetramer (alpha(2)beta(2)), is the first catalytic component of the mammalian pyruvate dehydrogenase complex (PDC). To investigate the roles of cysteine-62 of E1alpha (alphaC62) and tryptophan-135 of E1beta (betaW135) (identified previously as active site residues using chemical
Protein science : a publication of the Protein Society, 3(1), 109-117 (1994-01-01)
The family of FMN-dependent, alpha-hydroxy acid-oxidizing enzymes catalyzes substrate dehydrogenation by a mechanism the first step of which is abstraction of the substrate alpha-proton (so-called carbanion mechanism). For flavocytochrome b2 and lactate oxidase, it was shown that once on the
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