Molecular and Phylogenetic Analysis of Pyridoxal Phosphate- Dependent Acyltransferase of Exiguobacterium acetylicum
| Autor: | Narayanan Rajendran, Colby Smith, Williard Mazhawidza |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
DNA
Bacterial chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Transamination Molecular Sequence Data Corynebacterium Biology Amplicon Polymerase Chain Reaction General Biochemistry Genetics and Molecular Biology Amino acid Metabolic pathway Enzyme chemistry Biochemistry Exiguobacterium acetylicum Pyridoxal Phosphate Acyltransferase Amino Acid Sequence Primer (molecular biology) Base Pairing Sequence Alignment Acyltransferases Phylogeny |
| Zdroj: | Zeitschrift für Naturforschung C. 64:891-898 |
| ISSN: | 1865-7125 0939-5075 |
| DOI: | 10.1515/znc-2009-11-1222 |
| Popis: | The pyridoxal-5’-phosphate (PLP)-dependent family of enzymes is a very diverse group of proteins that metabolize small molecules like amino acids and sugars, and synthesize cofactors for other metabolic pathways through transamination, decarboxylation, racemization, and substitution reactions. In this study we employed degenerated primer-based PCR amplification, using genomic DNA isolated from the soil bacterium Exiguobacterium acetylicum strain SN as template. We revealed the presence of a PLP-dependent family of enzymes, such as PLP-dependent acyltransferase, and similarity to 8-amino-7-oxononoate synthase. Sequencing analysis and multiple alignment of the thymidine-adenine-cloned PCR amplicon revealed PLP-dependent family enzymes with specific confering codes and consensus amino acid residues specific to this group of functional proteins. Amino acid residues common to the majority of PLP-dependent enzymes were also revealed by the Lasergene MegAlign software. A phylogenetic tree was constructed. Its analysis revealed a close relationship of E. acetylicum to other bacteria isolated from extreme environments suggesting similarities in anabolic adaptability and evolutionary development. |
| Databáze: | OpenAIRE |
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