Isolation and partial characterization of the Chlamydomonas reinhardtii γ-glutamyl kinase

Keita Miyoshi; Hideyuki Matsuura; Takao Kumon; Keita Matsuda; Tomoaki Yoshikawa; Takeshi Bamba; Kazuo Harada; Kazumasa Hirata

doi:10.1016/j.jbiosc.2011.02.012

Isolation and partial characterization of the Chlamydomonas reinhardtii γ-glutamyl kinase

J Biosci Bioeng. 2011 Jul;112(1):75-8. doi: 10.1016/j.jbiosc.2011.02.012. Epub 2011 Mar 27.

Authors

Keita Miyoshi¹, Hideyuki Matsuura, Takao Kumon, Keita Matsuda, Tomoaki Yoshikawa, Takeshi Bamba, Kazuo Harada, Kazumasa Hirata

Affiliation

¹ Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.

PMID: 21444242
DOI: 10.1016/j.jbiosc.2011.02.012

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.

MeSH terms

Amino Acid Sequence
Chlamydomonas reinhardtii / genetics
Chlamydomonas reinhardtii / metabolism*
Escherichia coli / genetics
Escherichia coli / metabolism
Molecular Sequence Data
Phosphotransferases (Carboxyl Group Acceptor) / genetics
Phosphotransferases (Carboxyl Group Acceptor) / isolation & purification*
Phosphotransferases (Carboxyl Group Acceptor) / metabolism
Proline / metabolism
Recombinant Proteins / metabolism

Substances

Recombinant Proteins
Proline
Phosphotransferases (Carboxyl Group Acceptor)
glutamate 5-kinase