The dimer contact area of sorghum NADP-malate dehydrogenase: Role of aspartate 101 in dimer stability and catalytic activity

FEBS Letters

Volumn 471, Issue 2-3, 2000, Pages 240-244

  Schepens, Isabelle ^a   Decottignies, Paulette ^a   Ruelland, Eric ^a   Johansson, Kenth ^b   Miginiac Maslow, Myroslawa ^a  

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

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

Author keywords

Dimer; Monomer; NADP malate dehydrogenase; Site directed mutagenesis; Thioredoxin

Indexed keywords

ASPARTIC ACID; DIMER; MALATE DEHYDROGENASE (NADP); MONOMER; THIOREDOXIN;

ARTICLE; CATALYSIS; DIMERIZATION; ENZYME KINETICS; ENZYME STABILITY; MUTANT; MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; SORGHUM; WESTERN BLOTTING;

AMINO ACID SUBSTITUTION; ARGININE; ASPARTIC ACID; BINDING SITES; BLOTTING, WESTERN; CATALYSIS; DIMERIZATION; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ELECTROSTATICS; ENZYME ACTIVATION; ENZYME STABILITY; KINETICS; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (NADP+); MODELS, MOLECULAR; MOLECULAR WEIGHT; MUTATION; POACEAE; PROTEIN STRUCTURE, QUATERNARY; THIOREDOXIN;

EID: 0034646943     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(00)01405-8     Document Type: Article

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