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.

作者: Patricia C. Babbitt , George L. Kenyon , Brian M. Martin , Hugues Charest , Michel Slyvestre

DOI: 10.1021/BI00139A024

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摘要: We have deduced the nucleotide sequence of genes encoding three components 4-chlorobenzoate (4-CBA) dehalogenase from Pseudomonas sp. CBS-3 and examined origin these proteins by homology analysis. Open reading frame 1 (ORF1) encodes a 30-kDa 4-CBA-coenzyme A related to enoyl-coenzyme hydratases functioning in fatty acid beta-oxidation. ORF2 57-kDa protein which activates 4-CBA acyl adenylation/thioesterification. This 4-CBA:coenzyme ligase shares significant similarity with large group proteins, many catalyze similar chemistry beta-oxidation pathways or siderophore antibiotic synthetic pathways. These common short stretch sequence, (T,S)(S,G)G(T,S)(T,E)G(L,X)PK(G,-), is particularly highly conserved may represent an important new class "signature" sequence. were unable find any homologous 16-kDa 4-hydroxybenzoate-coenzyme thioesterase encoded ORF3. Analysis function found be structurally supports proposal that they evolved pathway.

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