Effect of modification of the length and flexibility of the acyl carrier protein-thioesterase interdomain linker on functionality of the animal fatty acid synthase

Biochemistry

Volumn 44, Issue 10, 2005, Pages 4100-4107

  Joshi, Anil K ^a   Witkowski, Andrzej ^a   Berman, Harvey A ^b   Zhang, Lei ^a   Smith, Stuart ^a  

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

^b UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBON; CHEMICAL BONDS; FLUORESCENCE; POLARIZATION; PROTEINS; REACTION KINETICS;

ACYL THIOESTERS; ANIMAL FATTY ACIDS; CATALYTIC PROPERTIES; COVALENT BOND;

FATTY ACIDS;

ACYL CARRIER PROTEIN; CARBON; FATTY ACID SYNTHASE; PANTETHEINE PHOSPHATE; POLYKETIDE SYNTHASE; PYRENE DERIVATIVE; SERINE; THIOL ESTER HYDROLASE;

AMINO ACID COMPOSITION; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; FLUORESCENCE POLARIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MODIFICATION;

ACYL CARRIER PROTEIN; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; FATTY ACID SYNTHETASE COMPLEX; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PALMITOYL-COA HYDROLASE; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; RATS; SEQUENCE DELETION; SUBSTRATE SPECIFICITY; THERMODYNAMICS; THIOLESTER HYDROLASES;

ANIMALIA;

EID: 14844357601     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047856r     Document Type: Article

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