Cysteine188 Revealed as Being Critical for the Enzyme Activity of Arylmalonate Decarboxylase by Site-Directed Mutagenesis

Autor:	Hiromichi Ohta, Hitoshi Kakidani, Mamoru Miyazaki, Satoshi Hanzawa
Rok vydání:	1997
Předmět:	chemistry.chemical_classification biology Stereochemistry Decarboxylation General Chemistry Arylmalonate decarboxylase Enzyme assay Residue (chemistry) Enzyme chemistry Biochemistry biology.protein Site-directed mutagenesis Cysteine
Zdroj:	Bulletin of the Chemical Society of Japan. 70:2765-2769
ISSN:	1348-0634 0009-2673
DOI:	10.1246/bcsj.70.2765
Popis:	Arylmalonate decarboxylase (AMDase) catalyzes the asymmetric decarboxylation of α-aryl-α-methylmalonic acid. Since this enzyme is inhibited by SH-reagents, a cysteine residue is supposed to be invo...
Databáze:	OpenAIRE
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