Reference "Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)"

Reference ID

9026

Title

Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)

Source

European journal of biochemistry / FEBS, 1990, vol. 192, pp. 299-303

Authors (9)

Cretin-C	Luchetta-P
Joly-C	Decottignies-P
Lepiniec-L	Gadal-P
Sallantin-M	Huet-J-C
Pernollet-J-C

Abstract

Malate dehydrogenase (NADP) (NADP-MDH) is an important enzyme of the
photosynthetic CO2 fixation pathway of C4 plants. We have isolated two clones
from a sorghum lambda gt11 cDNA library (CM3, 932 bp, and CM7, 1441 bp).
Nucleotide sequence analysis of the cDNAs CM3 and CM7 showed the existence of
two NADP-MDH mRNA species encoding different enzyme subunits. Microsequencing of
the N-terminus of the mature protein indicated that a specific cleavage of 13
amino acids occurred during the purification steps of the enzyme. The full-
length cDNA CM7 contains a large open reading frame encoding an NH2-terminal
transit peptide of 40 amino acids and a mature protein of 389 amino acids
(42.207 kDa). Alignment of the NADP-MDH sequence with those of several malate
dehydrogenases revealed some similarities with NAD-MDHs.