Characterization of human cystathionine γ-lyase enzyme activities toward d-amino acids

Author:

Miyamoto Tetsuya1,Saitoh Yasuaki1,Katane Masumi1,Sekine Masae1,Sakai-Kato Kumiko1,Homma Hiroshi1

Affiliation:

1. Graduate School of Pharmaceutical Sciences, Kitasato University , 5-9-1 Shirokane, Minato-ku, Tokyo , Japan

Abstract

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.

Funder

Ito Science Foundation

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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1. Multifunctional enzymes related to amino acid metabolism in bacteria;Bioscience, Biotechnology, and Biochemistry;2024-03-04

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