Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition

Journal of Biological Chemistry

Volumn 274, Issue 49, 1999, Pages 34539-34542

  Krimm, Isabelle ^a   Goyer, Aymeric ^b   Issakidis Bourguet, Emmanuelle ^b   Miginiac Maslow, Myroslawa ^b   Lancelin, Jean Marc ^a  

^a UNIVERSITÉ LYON 1   (France)

^b INSTITUTE OF PLANT SCIENCES PARIS SACLAY IPS2   (France)

Author keywords

[No Author keywords available]

Indexed keywords

MALATE DEHYDROGENASE (NADP); THIOREDOXIN;

AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHLOROPLAST; ENZYME ACTIVATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; REVIEW; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CHLOROPLASTS; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ESCHERICHIA COLI; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (NADP+); MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; THIOREDOXIN;

EID: 0033521039     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.49.34539     Document Type: Review

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