[Catalytic properties of enzymes from Erwinia carotovora involved in transamination of phenylpyruvate].
Prikl Biokhim Mikrobiol
; 49(2): 129-35, 2013.
Article
em Ru
| MEDLINE
| ID: mdl-23795470
ABSTRACT
Km for L-phenylalanine, L-glutamic acid, L-aspartic acid, and the corresponding keto acids were calculated, as well as Vmax, was measured for the following pairs of substrates L-phenylalanine-2-ketoglutarate, L-phenylalanine-oxaloacetate, L-glutamic acid-phenylpyruvate, and L-aspartic acid-phenylpyruvate for aminotransferases PATI, PAT2, and PAT3 from Erwinia carotovora catalyzing transamination of phenylpyruvate. The ping-pong bi-bi mechanism was shown for the studied aminotransferases. The substrate inhibition (Ks) of PAT3 with 2-ketoglutarate and oxaloacetate was 10.23 +/- 3.20 and 3.73 +/- 1.99 mM, respectively.
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Base de dados:
MEDLINE
Assunto principal:
Ácidos Fenilpirúvicos
/
Proteínas de Bactérias
/
Pectobacterium carotovorum
/
Transaminases
Idioma:
Ru
Ano de publicação:
2013
Tipo de documento:
Article