Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD).
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.
Laboratoire de Physiologie Végétale Moléculaire, Université de Paris-Sud, France.
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Crétin
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Luchetta
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Joly
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Decottignies
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Lepiniec
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Gadal
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Sallantin
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Huet
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Pernollet
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D008291:Malate Dehydrogenase / Q000235:genetics*; D050538:Malate Dehydrogenase (NADP+); D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology* / Q000235:genetics; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D004247:DNA; D008291:Malate Dehydrogenase; D050538:Malate Dehydrogenase (NADP+)