The characterisation of the shikimate pathway enzyme dehydroquinase from Pisum sativum

FEBS Letters

Deka, Ranjit K.²  Anton, Ian A.²  Coggins, John R.²  Dunbar, Bryan¹ 

[1] Department of Molecular and Cell Biology, University of Aberdeen, Aberdeen AB9 1AS, Scotland, UK;Department of Biochemistry, University of Glasgow, Glasgow G12 8QQ, Scotland, UK

关键词: Type I dehydroquinase;    Shikimate dehydrogenase;    Pisum sativum;   

DOI  :  10.1016/0014-5793(94)00710-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Peptides accounting for 157 residues of the bifunctional shikimate pathway enzyme, dehydroquinase/shikimate dehydrogenase, of Pisum sativum were sequenced. Three of the peptides were homologous to regions in Escherichia coli dehydroquinase and two to E. coli shikimate dehydrogenase. The pea dehydroquinase activity was inhibited by treatment with dehydroquinate plus sodium borohydride, establishing it as a type I dehydroquinase. Synthetic oligonucleotides designed from the amino acid sequence were used as PCR primers to amplify fragments of P. sativum cDNA. DNA sequence analysis showed that these amplified products were derived from dehydroquinase/shikimate dehydrogenase CDNA. The complete amino acid sequence of the dehydroquinase domain has been defined; it is homologous to all other type I dehydroquinases and is N-terminal.

【 授权许可】

Unknown