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- W4295300846 abstract "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." @default.
- W4295300846 created "2022-09-12" @default.
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- W4295300846 date "2022-09-09" @default.
- W4295300846 modified "2023-10-18" @default.
- W4295300846 title "Characterization of human cystathionine γ-lyase enzyme activities toward <scp>d</scp>-amino acids" @default.
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- W4295300846 doi "https://doi.org/10.1093/bbb/zbac151" @default.
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