Abstract
Methylglyoxal synthase in Saccharomyces cerevisiae was purified approximately 300 folds from cell extracts with 20% of activity yield. During purification procedures, polymorphic behaviours of the enzyme were observed. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis and consisted of a single polypeptide chain of Mr = 26,000. The enzyme was most active at pH 9.5-10.5 and strictly specific to dihydroxyacetone phosphate with Km = 3 mM. Phosphoenolpyruvate, glyceraldehyde-3-phosphate, orthophosphate and thiol compounds were potent inhibitors of the enzyme.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Carbon-Oxygen Lyases*
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Chromatography
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Dihydroxyacetone Phosphate
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / enzymology
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Hydrogen-Ion Concentration
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Lyases / antagonists & inhibitors
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Lyases / isolation & purification
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Lyases / metabolism*
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Molecular Weight
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Phosphates / pharmacology
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Phosphoenolpyruvate / pharmacology
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Saccharomyces cerevisiae / enzymology*
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Substrate Specificity
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Sulfhydryl Compounds / pharmacology
Substances
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Phosphates
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Sulfhydryl Compounds
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Dihydroxyacetone Phosphate
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Phosphoenolpyruvate
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Lyases
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Carbon-Oxygen Lyases
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methylglyoxal synthase