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Journal ArticleDOI

A reinvestigation of inhibitors of glyoxalase I

Subhankar Ray, +1 more
- 01 Dec 1987 - 
- Vol. 12, Iss: 4, pp 405-414
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TLDR
It is found that nucleotides such as ATP, GTP and different classes of other reagents based on transition state analogy (D-isoascorbate, dihydroxyfumaric acid, rhodizonic acid) do not inhibit yeast or goat liver glyoxalase I.
Abstract
It has been reported earlier that nucleotides, nucleosides and a series of structurally related compounds as well as compounds based on transition state analogy inhibit yeast glyoxalase I. In our study on the metabolic regulation of glyoxalase I, we have found that nucleotides such as ATP, GTP and different classes of other reagents based on transition state analogy (D-isoascorbate, dihydroxyfumaric acid, rhodizonic acid) do not inhibit yeast or goat liver glyoxalase I. The reported inhibition of glyoxalase I by these compounds has been found to be due to the interference of these compounds with the absorbancy at 240 nm of S-D-lactoylglutathione formed by the glyoxalase I reaction.

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Citations
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Journal ArticleDOI

Investigation on glyoxalase I inhibitors.

TL;DR: Examination of some of the aforementioned compounds has revealed that squaric acid does not function as an inhibitor of glyoxalase I and several other compounds are much less effective in this regard than previously reported.
Journal ArticleDOI

Interaction of aldehydes with glyoxalase I and the status of several aldehyde metabolizing enzymes of Ehrlich ascites carcinoma cells.

TL;DR: The results indicate that D, and L-lactaldehyde are strong non-competitive inhibitors of glyoxalase I and the effect with the D-isomer is more pronounced, whereas both D,L-glyceraldehyde and acetaldehyde are moderately inhibitory and the nature of inhibition is strictly competitive.
References
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Journal ArticleDOI

Isolation of methylglyoxal synthase from goat liver.

TL;DR: An enzyme fraction which specifically catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate has been isolated and partially purified from goat liver and appears to be substantially free from glyoxalase I, reduced glutathione, and triosephosphate isomerase.
Journal ArticleDOI

The enzymatic oxidation of 1,2-propanediol phosphate to acetol phosphate.

TL;DR: The product of the oxidation of propanediol-P by rabbit muscle oc-glycerol phosphate dehydrogenase has been established as acetol-P, CH3COCH20P03H2, and attempts to demonstrate this reaction in rat liver homogenates have been unsuccessful.
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Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone.

TL;DR: An enzyme which oxidizes aminoacetone to methylglyoxal has been purified from the particulate fraction of goat liver and is highly sensitive to carbonyl group reagents.
Journal ArticleDOI

Characterization of methylglyoxal synthase in Saccharomyces cerevisiae

TL;DR: Methylglyoxal synthase in Saccharomyces cerevisiae was purified approximately 300 folds from cell extracts with 20% of activity yield and during purification procedures, polymorphic behaviours of the enzyme were observed.
Journal ArticleDOI

The structure of a glyoxalase I inhibitor and its chemical reactivity with SH-compounds.

TL;DR: The structure of a glyoxalase I inhibitor (I), isolated from a cultured broth of Streptomyces griseosporeus, was found to be 2-crotonyloxymethyl-4,5,6-trihydroxy-cyclohex-2-enone by chemical studies.
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