Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation

Biochemistry

Volumn 35, Issue 27, 1996, Pages 8934-8941

  Tan, Dongwei ^a   Ferreira, Gloria C ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; ARGININE; DIMER; DNA; HEME; PYRIDOXAL 5 PHOSPHATE; SCHIFF BASE;

ARTICLE; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; MUTANT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL;

5-AMINOLEVULINATE SYNTHETASE; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; ERYTHROCYTES; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; KINETICS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030054651     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952918m     Document Type: Article

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