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- Title
Cystathionine β-lyase is involved in D-amino acid metabolism.
- Authors
Tetsuya Miyamoto; Masumi Katane; Yasuaki Saitoh; Masae Sekine; Hiroshi Homma
- Abstract
Non-canonical D-amino acids play important roles in bacteria including control of peptidoglycan metabolism and biofilm disassembly. Bacteria appear to produce non-canonical D-amino acids to adapt to various environmental changes and understanding the biosynthetic pathways is important. We identified novel amino acid racemases possessing the ability to produce non-canonical D-amino acids in Escherichia coli and Bacillus subtilis in our previous study, whereas the biosynthetic pathways of these D-amino acids still remain unclear. In the present study, we demonstrated that two cystathionine β-lyases (MetC and MalY) from E. coli produce non-canonical D-amino acids including non-proteinogenic amino acids. Furthermore, MetC displayed D- and L-serine (Ser) dehydratase activity. We characterised amino acid racemase, Ser dehydratase and cysteine lyase activities and all were higher for MetC. Interestingly, all three activities were at a comparable level for MetC, although optimal conditions for each reaction were distinct. These results indicate that MetC and MalY are multifunctional enzymes involved in L-methionine metabolism and the production of D-amino acids, as well as D- and L-Ser metabolism. To our knowledge, this is the first evidence that cystathionine β-lyase is a multifunctional enzyme with three different activities.
- Subjects
AMINO acids; ESCHERICHIA coli; METABOLISM; ENZYMES; RACEMASES
- Publication
Biochemical Journal, 2018, Vol 475, Issue 8, p1397
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BCJ20180039