Open AccessPrimary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence
Author(s) -
CRÉTIN Claude,
LUCHETTA Philippe,
JOLY Cécile,
DECOTTIGNIES Paulette,
LEPINIEC Loïc,
GADAL Pierre,
SALLANTIN Marc,
HUET JeanClaude,
PERNOLLET JeanClaude
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19227.x
Subject(s) - malate dehydrogenase , biology , complementary dna , biochemistry , amino acid , open reading frame , peptide sequence , nad+ kinase , cdna library , nucleic acid sequence , microbiology and biotechnology , protein primary structure , enzyme , dehydrogenase , gene
Malate dehydrogenase (NADP) (NADP‐MDH) is an important enzyme of the photosynthetic CO 2 fixation pathway of C 4 plants. We have isolated two clones from a sorghum λgt11 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 NH 2 ‐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.