Initial characterisation of 4-chlorobenzoate dehalogenase fromPseudomonassp. CBS3

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Resolution of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS3 into three components.

Extracts of Pseudomonas sp. strain CBS3 grown with 4-chlorobenzoate as sole carbon source contained an enzyme that converted 4-chlorobenzoate to 4-hydroxybenzoate. This enzyme was shown to consist of three components, all necessary for the reaction. Component I, which had a molecular weight of about 3,000, was highly unstable. Components II and III were stable proteins with molecular weights of...

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Raman study of the polarizing forces promoting catalysis in 4-chlorobenzoate-CoA dehalogenase.

The enzyme 4-chlorobenzoate-CoA dehalogenase catalyzes the hydrolysis of 4-chlorobenzoate-CoA (4-CBA-CoA) to 4-hydroxybenzoyl-CoA (4-HBA-CoA). In order to facilitate electrophilic catalysis, the dehalogenase utilizes a strong polarizing interaction between the active site residues and the benzoyl portion of the substrate [Taylor, K. L., et al. (1995) Biochemistry 34, 13881]. As a result of this...

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Purification and characterization of a novel 3-chlorobenzoate-reductive dehalogenase from the cytoplasmic membrane of Desulfomonile tiedjei DCB-1.

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ژورنال

عنوان ژورنال: FEMS Microbiology Letters

سال: 1987

ISSN: 0378-1097,1574-6968

DOI: 10.1111/j.1574-6968.1987.tb02180.x