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PMID: 11172800 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Review

NADP-malic enzyme from plants: a ubiquitous enzyme involved in different metabolic pathways.

FEBS letters ·Vol. 490 ·No. 1-2 ·2001-02-09 ·Pages 1-6

Drincovich MF, Casati P, Andreo CS

Abstract

NADP-malic enzyme (NADP-ME) is a widely distributed enzyme that catalyzes the oxidative decarboxylation of L-malate. Photosynthetic NADP-MEs are found in C4 bundle sheath chloroplasts and in the cytosol of CAM plants, while non-photosynthetic NADP-MEs are either plastidic or cytosolic in various plants. We propose a classification of plant NADP-MEs based on their physiological function and localization and we describe recent advances in the characterization of each isoform. Based on the alignment of amino acid sequences of plant NADP-MEs, we identify putative binding sites for the substrates and analyze the phylogenetic origin of each isoform, revealing several features of the molecular evolution of this ubiquitous enzyme.

MeSH Terms
Amino Acid Sequence Binding Sites Evolution, Molecular Kinetics Malate Dehydrogenase/chemistry,classification Molecular Sequence Data Phylogeny Plants/enzymology Protein Isoforms
Chemicals
Protein Isoforms Malate Dehydrogenase malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Drincovich M F
Centro de Estudios Fotosintéticos y Bioquímicos, Universidad Nacional de Rosario, CONICET, Suipacha 531, 2000, Rosario, Argentina.
Casati P
Andreo C S
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2001-02-09
Pages
1-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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