Purification and characterization of salicylate hydroxylase from Pseudomonas putida PpG7.

You, I S; Murray, R I; Jollie, D; Gunsalus, I C

You, I S; Murray, R I; Jollie, D; Gunsalus, I C.

Afiliación

You IS; Department of Biochemistry, University of Illinois, Urbana 61801.

Biochem Biophys Res Commun ; 169(3): 1049-54, 1990 Jun 29.

Article en En | MEDLINE | ID: mdl-2363715

RESUMEN

The salicylate hydroxylase from P. putida PpG7 was purified and characterized. The enzyme appears to be monomeric, and it showed one major band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent Mr of 45 kDa. The sequence of the first 25 amino acids of salicylate hydroxylase (PpG7) was determined. Also, the total amino acid composition of salicylate hydroxylase (PpG7) was obtained and compared with that of the known salicylate hydroxylase from P. putida.

Asunto(s)

Oxigenasas de Función Mixta/aislamiento & purificación; Pseudomonas/enzimología; Secuencia de Aminoácidos; Aminoácidos/análisis; Oxigenasas de Función Mixta/metabolismo; Datos de Secuencia Molecular; Peso Molecular; Salicilatos/metabolismo

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pseudomonas / Oxigenasas de Función Mixta Idioma: En Revista: Biochem Biophys Res Commun Año: 1990 Tipo del documento: Article Pais de publicación: Estados Unidos

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