The characterisation of the shikimate pathway enzyme dehydroquinase from Pisum sativum.
FEBS Lett
; 349(3): 397-402, 1994 Aug 08.
Article
en En
| MEDLINE
| ID: mdl-8050603
ABSTRACT
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.
Search on Google
Banco de datos:
MEDLINE
Asunto principal:
Plantas Medicinales
/
Hidroliasas
/
Fabaceae
Idioma:
En
Año:
1994
Tipo del documento:
Article