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Volumn 39, Issue 2, 2006, Pages 223-227
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Activity of human dihydrolipoamide dehydrogenase is largely reduced by mutation at isoleucine-51 to alanine.
a
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Author keywords
[No Author keywords available]
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Indexed keywords
ALANINE;
DIHYDROLIPOAMIDE DEHYDROGENASE;
ISOLEUCINE;
AMINO ACID SUBSTITUTION;
ARTICLE;
CATALYSIS;
CHEMISTRY;
COMPARATIVE STUDY;
ENZYME ACTIVATION;
GENE EXPRESSION REGULATION;
GENETICS;
HUMAN;
MUTATION;
PHYSIOLOGY;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PROTEIN CONFORMATION;
SITE DIRECTED MUTAGENESIS;
ALANINE;
AMINO ACID SUBSTITUTION;
CATALYSIS;
DIHYDROLIPOAMIDE DEHYDROGENASE;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENZYME ACTIVATION;
GENE EXPRESSION REGULATION, ENZYMOLOGIC;
HUMANS;
ISOLEUCINE;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PROTEIN CONFORMATION;
MLCS;
MLOWN;
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EID: 33744482599
PISSN: 12258687
EISSN: None
Source Type: Journal
DOI: 10.5483/bmbrep.2006.39.2.223 Document Type: Article |
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Times cited : (9)
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References (0)
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