Branched-chain amino acid metabolon: Interaction of glutamate dehydrogenase with the mitochondrial branched-chain aminotransferase (BCATm)

Journal of Biological Chemistry

Volumn 285, Issue 1, 2010, Pages 265-276

  Islam, Mohammad Mainul ^a   Nautiyal, Manisha ^b   Wynn, R Max ^c   Mobley, James A ^d   Chuang, David T ^c   Hutson, Susan M ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b WAKE FOREST SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^d Kentucky   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC ACTIVATOR; BRANCHED-CHAIN AMINOTRANSFERASE; CATABOLIC PATHWAY; DECARBOXYLASES; ENZYME COMPLEXES; GLUTAMATE DEHYDROGENASE; KETO ACIDS; MOLAR RATIO; OXIDATIVE DEAMINATION; OXIDATIVE DECARBOXYLATION; PROTEIN COMPLEXES; PYRUVATE CARBOXYLASE;

AMINES; CARBOXYLATION; COMPLEXATION; ORGANIC ACIDS; PROTEINS;

AMINO ACIDS;

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); 4 NITROPHENYL PHOSPHATE; ADENOSINE DIPHOSPHATE; GLUTAMATE DEHYDROGENASE; ISOLEUCINE; LEUCINE; MULTIENZYME COMPLEX; PYRIDOXAMINE PHOSPHATE; PYRUVATE CARBOXYLASE; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; VALINE;

AFFINITY CHROMATOGRAPHY; ALLOSTERISM; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CATABOLISM; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; DEAMINATION; ENZYME ACTIVATION; ENZYME KINETICS; MALE; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; TISSUE DISTRIBUTION;

ALLOSTERIC REGULATION; AMINO ACIDS, BRANCHED-CHAIN; ANIMALS; BIOCATALYSIS; CHROMATOGRAPHY, AFFINITY; CROSS-LINKING REAGENTS; DEAMINATION; DECARBOXYLATION; GLUTAMATE DEHYDROGENASE; MALE; METABOLOME; MITOCHONDRIA; OXIDATION-REDUCTION; PHOSPHORYLATION; PROTEIN BINDING; PYRIDOXAMINE; RATS; RATS, SPRAGUE-DAWLEY; TISSUE DISTRIBUTION; TRANSAMINASES;

EID: 73649126526     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.048777     Document Type: Article

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