title: Isolation and partial characterization of the Chlamydomonas reinhardtii γ-glutamyl kinase.
abstract: We isolated a Chlamydomonas gene encoding putative γ-glutamyl kinase (GK), an enzyme that catalyzes the first step of proline biosynthesis. Using an Escherichia coli auxotroph and a purified recombinant protein, we show that Chlamydomonas GK is a functional GK. The sensitivity of this kinase to feedback inhibition by proline was lower than in that of microbial GKs previously reported.
authors: Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.
authors: Keita
authors: K
authors: Miyoshi
authors: Hideyuki
authors: H
authors: Matsuura
authors: Takao
authors: T
authors: Kumon
authors: Keita
authors: K
authors: Matsuda
authors: Tomoaki
authors: T
authors: Yoshikawa
authors: Takeshi
authors: T
authors: Bamba
authors: Kazuo
authors: K
authors: Harada
authors: Kazumasa
authors: K
authors: Hirata
mesh_terms: D000595:Amino Acid Sequence; D016825:Chlamydomonas reinhardtii / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D017851:Phosphotransferases (Carboxyl Group Acceptor) / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011392:Proline / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D011392:Proline; D017851:Phosphotransferases (Carboxyl Group Acceptor); C020650:glutamate 5-kinase