Immobilization of Saccharomyces cerevisiae cystathionine gamma-lyase and application of the product to cystathionine synthesis.
Cystathionine gamma-lyase of Saccharomyces cerevisiae was immobilized to aminohexyl-Sepharose through the cofactor pyridoxal 5'-phosphate and was characterized with respect to its cystathionine gamma-synthase activity. The immobilized product was so stable that it repeatedly catalyzed as many as five cycles of the reaction without losing activity.
Yamagata
Shuzo
S
Department of Applied Life Sciences, Faculty of Applied Biological Sciences, Gifu University, Gifu 501-1193, Japan.
Akamatsu
Tsuyoshi
T
Iwama
Tomonori
T
D019757:Carbon-Oxygen Lyases / Q000378:metabolism; D003540:Cystathionine / Q000096:biosynthesis*; D003542:Cystathionine gamma-Lyase / Q000737:chemistry / Q000378:metabolism; D004800:Enzymes, Immobilized / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012685:Sepharose / Q000031:analogs & derivatives*
D004800:Enzymes, Immobilized; D003540:Cystathionine; C024903:aminohexyl-sepharose; D012685:Sepharose; C022696:O-succinylhomoserine (thiol)-lyase; D019757:Carbon-Oxygen Lyases; D003542:Cystathionine gamma-Lyase