The malonyl/acetyltransferase and β-ketoacyl synthase domains of the animal fatty acid synthase can cooperate with the acyl carrier protein domain of either subunit

Biochemistry

Volumn 37, Issue 8, 1998, Pages 2515-2523

  Joshi, Anil K ^a   Witkowski, Andrzej ^a   Smith, Stuart ^a  

^a CHILDREN S HOSPITAL OAKLAND RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; ACYL CARRIER PROTEIN; ACYLTRANSFERASE; FATTY ACID SYNTHASE; MUTANT PROTEIN; PALMITIC ACID; POLYPEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME SUBUNIT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SYNTHESIS;

3-OXOACYL-(ACYL-CARRIER-PROTEIN) SYNTHASE; ACYL-CARRIER PROTEIN S-MALONYLTRANSFERASE; ACYLTRANSFERASES; ANIMALS; BINDING SITES; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FATTY ACID SYNTHETASE COMPLEX; GENETIC COMPLEMENTATION TEST; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; RATS; RECOMBINANT PROTEINS;

ANIMALIA;

EID: 0032562216     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971886v     Document Type: Article

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