PubMed Health⌕ Search

Biomedical subjects

R M Sarmiento

Publications and source records attributed to R M Sarmiento.

4 recordsLinked to original sources
PubMed1984

Further purification and characterization of diacetyl reducing enzymes from beef liver.

Two diacetyl reducing enzymes have been isolated from beef liver. One of them, a monomer of mol. wt 28-30,000 dalton and pI 6.2, corresponds to the low molecular weight diacetyl reductase formerly accounted for using preparations of this organ; it has been now identified as an L-glycol dehydrogenase. The other one, an oligomer of 78,000 dalton and pI 7.0, which matches the high molecular weight diacetyl reductase, is, in the authors' opinion, a new enzyme for which the systematic name L(+)-alpha-hydroxycarbonyl: NAD(P) oxidoreductase (EC 1.1.1...) and common name alpha-dicarbonyl reductase are proposed.

Acetoin Dehydrogenase↗
PubMed1982

Diacetyl reductase.

Explore the source record for details and available documents.

Acetoin Dehydrogenase↗
PubMedDate not supplied

Kinetics of alpha-dicarbonyls reduction by L-glycol dehydrogenase (NAD+) from Enterobacter aerogenes.

L-glycol dehydrogenase from Enterobacter aerogenes shows a high affinity by NADH (Ks = 2-4 microM; Km = 4.3-9.7 microM), which indicates that it must operate in vivo saturated with this coenzyme. Michaelis and dissociation constants for the reduction of the carbonyl substrates assayed (diacetyl, 2,3-pentanedione, methylglyoxal and ethyl pyruvate) are similar to those reported for other diacetyl reducing enzymes. The kinetic mechanism followed by these reactions has also been studied. Our results prove that the reduction of diacetyl and ethyl pyruvate takes place via an Ordered Bi-Bi system with the coenzyme as the leading substrate. Methylglyoxal and 2,3-pentanedione are reduced by the same mechanism or by a Theorell-Chance one.

Acetone↗