title: Immobilization of Saccharomyces cerevisiae cystathionine gamma-lyase and application of the product to cystathionine synthesis.
abstract: 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.
authors.affiliation: Department of Applied Life Sciences, Faculty of Applied Biological Sciences, Gifu University, Gifu 501-1193, Japan.
authors.forename: Shuzo
authors.initials: S
authors.lastname: Yamagata
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Akamatsu
authors.forename: Tomonori
authors.initials: T
authors.lastname: Iwama
mesh_terms: 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*
chemical_list: D004800:Enzymes, Immobilized; D003540:Cystathionine; C024903:aminohexyl-sepharose; D012685:Sepharose; C022696:O-succinylhomoserine (thiol)-lyase; D019757:Carbon-Oxygen Lyases; D003542:Cystathionine gamma-Lyase