Characterization of human cystathionine γ-lyase enzyme activities toward d-amino acids
| Autor: | Tetsuya Miyamoto, Yasuaki Saitoh, Masumi Katane, Masae Sekine, Kumiko Sakai-Kato, Hiroshi Homma |
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| Rok vydání: | 2022 |
| Předmět: |
Mammals
Alanine Organic Chemistry Cystathionine gamma-Lyase Racemases and Epimerases Lyases General Medicine Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Cystathionine Homoserine Escherichia coli Serine Humans Animals Cysteine Amino Acids Molecular Biology Hydro-Lyases Biotechnology Amino Acid Isomerases |
| Zdroj: | Bioscience, biotechnology, and biochemistry. 86(11) |
| ISSN: | 1347-6947 |
| Popis: | Various d-amino acids play important physiological roles in mammals, but the pathways of their production remain unknown except for d-serine, which is generated by serine racemase. Previously, we found that Escherichia coli cystathionine β-lyase possesses amino acid racemase activity in addition to β-lyase activity. In the present work, we evaluated the enzymatic activities of human cystathionine γ-lyase, which shares a relatively high amino acid sequence identity with cystathionine β-lyase. The enzyme did not show racemase activity toward various amino acids including alanine and lyase and dehydratase activities were highest toward l-cystathionine and l-homoserine, respectively. The enzyme also showed weak activity toward l-cysteine and l-serine but no activity toward d-amino acids. Intriguingly, the pH and temperature profiles of lyase activity were distinct from those of dehydratase activity. Catalytic efficiency was higher for lyase activity than for dehydratase activity. |
| Databáze: | OpenAIRE |
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