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Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases.
Babbitt, P C; Kenyon, G L; Martin, B M; Charest, H; Slyvestre, M; Scholten, J D; Chang, K H; Liang, P H; Dunaway-Mariano, D.
Afiliación
  • Babbitt PC; Department of Pharmaceutical Chemistry, University of California, San Francisco 94143.
Biochemistry ; 31(24): 5594-604, 1992 Jun 23.
Article en En | MEDLINE | ID: mdl-1351742
We have deduced the nucleotide sequence of the genes encoding the three components of 4-chlorobenzoate (4-CBA) dehalogenase from Pseudomonas sp. CBS-3 and examined the origin of these proteins by homology analysis. Open reading frame 1 (ORF1) encodes a 30-kDa 4-CBA-coenzyme A dehalogenase related to enoyl-coenzyme A hydratases functioning in fatty acid beta-oxidation. ORF2 encodes a 57-kDa protein which activates 4-CBA by acyl adenylation/thioesterification. This 4-CBA:coenzyme A ligase shares significant sequence similarity with a large group of proteins, many of which catalyze similar chemistry in beta-oxidation pathways or in siderophore and antibiotic synthetic pathways. These proteins have in common a short stretch of sequence, (T,S)(S,G)G(T,S)(T,E)G(L,X)PK(G,-), which is particularly highly conserved and which may represent an important new class of "signature" sequence. We were unable to find any proteins homologous in sequence to the 16-kDa 4-hydroxybenzoate-coenzyme A thioesterase encoded by ORF3. Analysis of the chemistry and function of the proteins found to be structurally related to the 4-CBA:coenzyme A ligase and the 4-CBA-coenzyme A dehalogenase supports the proposal that they evolved from a beta-oxidation pathway.
Asunto(s)
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Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Palmitoil-CoA Hidrolasa / Pseudomonas / Genes Bacterianos / Hidrolasas / Ligasas Límite: Animals Idioma: En Revista: Biochemistry Año: 1992 Tipo del documento: Article
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Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Palmitoil-CoA Hidrolasa / Pseudomonas / Genes Bacterianos / Hidrolasas / Ligasas Límite: Animals Idioma: En Revista: Biochemistry Año: 1992 Tipo del documento: Article