Evolution of structure and substrate specificity ind-alanine:d-Alanine ligases and related enzymes
Autor: | Marc Galimand, Stefan Evers, Barbara Casadewall, Murielle Charles, Patrice Courvalin, Sylvie Dutka-Malen |
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Rok vydání: | 1996 |
Předmět: |
DNA
Bacterial Protein Conformation Molecular Sequence Data DNA Ribosomal Substrate Specificity Evolution Molecular chemistry.chemical_compound Bacterial Proteins RNA Ribosomal 16S Genetics Amino Acid Sequence Peptide Synthases Molecular Biology Gene Phylogeny Ecology Evolution Behavior and Systematics chemistry.chemical_classification DNA ligase Binding Sites Bacteria Base Sequence Sequence Homology Amino Acid biology Glycopeptides Substrate (chemistry) Drug Resistance Microbial biology.organism_classification Glycopeptide Amino acid RNA Bacterial Enzyme chemistry Biochemistry Peptidoglycan Sequence Alignment |
Zdroj: | Journal of Molecular Evolution. 42:706-712 |
ISSN: | 1432-1432 0022-2844 |
DOI: | 10.1007/bf02338803 |
Popis: | The D-alanine:D-alanine-ligase-related enzymes can have three preferential substrate specificities. Usually, these enzymes synthesize D-alanyl-D-alanine. In vancomycin-resistant Gram-positive bacteria, structurally related enzymes synthesize D-alanyl-D-lactate or d-alanyl-d-serine. The sequence of internal fragments of eight structural d-alanine:d-alanine ligase genes from enterococci has been determined. Alignment of the deduced amino acid sequences with those of other related enzymes from Gram-negative and Gram-positive bacteria revealed the presence of four distinct sequence patterns in the putative substrate-binding sites, each correlating with specificity to a particular substrate (D-alanine:D-lactate ligases exhibited two patterns). Phylogenetic analysis showed different clusters. The enterococcal subtree was largely superimposable on that derived from 16S rRNA sequences. In lactic acid bacteria, structural divergence due to differences in substrate specificity was observed. Glycopeptide resistance proteins VanA and VanB, the VanC-type ligases, and DdlA and DdlB from enteric bacteria and Haemophilus influenzae constituted separate clusters. |
Databáze: | OpenAIRE |
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