Gene identification and characterization of the pyridoxine degradative enzyme alpha-(N-acetylaminomethylene)succinic acid amidohydrolase from Mesorhizobium loti MAFF303099.
J Nutr Sci Vitaminol (Tokyo)
; 54(3): 185-90, 2008 Jun.
Article
em En
| MEDLINE
| ID: mdl-18635903
ABSTRACT
We have found for the first time that a chromosomal gene, mlr6787, in Mesorhizobium loti encodes the pyridoxine degradative enzyme alpha-(N-acetylaminomethylene)succinic acid (AAMS) amidohydrolase. The recombinant enzyme expressed in Escherichia coli cells was homogeneously purified and characterized. The enzyme consisted of two subunits each with a molecular mass of 34,000+/-1,000 Da, and exhibited Km and kcat values of 53.7+/-6 microM and 307.3+/-12 min(-1), respectively. The enzyme required no cofactor or metal ion. The primary structure of AAMS amidohydrolase was elucidated for the first time here. The primary structure of the enzyme protein showed no significant identity to those of known hydrolase proteins and low homology to those of fluoroacetate dehalogenase (PDB code, 1Y37), haloalkane dehalogenase (1K5P), and aryl esterase (1VA4).
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Piridoxina
/
Expressão Gênica
/
Alphaproteobacteria
/
Succinato-Semialdeído Desidrogenase
/
Amidoidrolases
/
Hidrolases
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
J Nutr Sci Vitaminol (Tokyo)
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Japão