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- W2950447491 abstract "2-Amino-2-methylmalonic acid has been shown to be a slow decarboxylation substrate for the enzyme serine hydroxymethyltransferase from both rabbit liver cytosol and E. coli. For both enzymes the amino acid product was (2R)-alanine. The enantiomers of 2-amino-2-methyl[1-13C]malonic acid have been synthesized and used to probe the stereochemical course and mechanism of the reaction. The pro-R carboxy group of 2-amino-2-methylmalonic acid was removed during the decarboxylation reaction catalysed by each enzyme and was replaced by a proton with retention of configuration at C-2. Similar results were also obtained with the H228N mutant of the E. coli enzyme. These results contrast earlier findings where it was suggested that 2-aminomalonic acid, a fast substrate for serine hydroxymethyltransferase, was decarboxylated non-stereospecifically." @default.
- W2950447491 created "2019-06-27" @default.
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- W2950447491 date "2010-08-19" @default.
- W2950447491 modified "2023-09-25" @default.
- W2950447491 title "ChemInform Abstract: Stereochemical Course of the Decarboxylation of 2-Amino-2- methylmalonic Acid by Serine Hydroxymethyltransferase." @default.
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- W2950447491 doi "https://doi.org/10.1002/chin.199412063" @default.
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