期刊
PLANT CELL
卷 23, 期 8, 页码 2978-2990出版社
OXFORD UNIV PRESS INC
DOI: 10.1105/tpc.111.088070
关键词
-
资金
- Deutsche Forschungsgemeinschaft
- Forschergruppe [FOR 1186-Promics]
Glycolate oxidase (GOX) is an essential enzyme involved in photorespiratory metabolism in plants. In cyanobacteria and green algae, the corresponding reaction is catalyzed by glycolate dehydrogenases (GlcD). The genomes of N-2-fixing cyanobacteria, such as Nostoc PCC 7120 and green algae, appear to harbor genes for both GlcD and GOX proteins. The GOX-like proteins from Nostoc (No-LOX) and from Chlamydomonas reinhardtii showed high L-lactate oxidase (LOX) and low GOX activities, whereas glycolate was the preferred substrate of the phylogenetically related At-GOX2 from Arabidopsis thaliana. Changing the active site of No-LOX to that of At-GOX2 by site-specific mutagenesis reversed the LOX/GOX activity ratio of No-LOX. Despite its low GOX activity, No-LOX overexpression decreased the accumulation of toxic glycolate in a cyanobacterial photorespiratory mutant and restored its ability to grow in air. A LOX-deficient Nostoc mutant grew normally in nitrate-containing medium but died under N-2-fixing conditions. Cultivation under low oxygen rescued this lethal phenotype, indicating that N-2 fixation was more sensitive to O-2 in the Dlox Nostoc mutant than in the wild type. We propose that LOX primarily serves as an O-2-scavenging enzyme to protect nitrogenase in extant N-2-fixing cyanobacteria, whereas in plants it has evolved into GOX, responsible for glycolate oxidation during photorespiration.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据