Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps

Biochemistry

Volumn 38, Issue 36, 1999, Pages 11814-11826

  Osterman, Andrei L ^a,b   Brooks, Harold B ^a,c   Jackson, Laune ^a   Abbott, Jared J ^a   Phillips, Margaret A ^a  

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

^b Integrated Genomics Inc   (United States)

^c ELI LILLY AND COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; ORNITHINE DECARBOXYLASE; SCHIFF BASE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; DECARBOXYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; PRIORITY JOURNAL; TRYPANOSOMA BRUCEI;

ANIMALS; BASE SEQUENCE; CARBOXYLIC ACIDS; CATALYSIS; CIRCULAR DICHROISM; DNA PRIMERS; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MUTAGENESIS, SITE-DIRECTED; ORNITHINE DECARBOXYLASE; PROTEIN BINDING; PYRIDOXAL PHOSPHATE; SCHIFF BASES; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPANOSOMA BRUCEI BRUCEI;

FELIS CATUS; TRYPANOSOMA; TRYPANOSOMA BRUCEI;

EID: 0033533601     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9906221     Document Type: Article

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