A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation

Protein Engineering

Volumn 9, Issue 1, 1996, Pages 61-67

  Morris, Aaron J ^a,b   Davenport, Robert C ^a   Tolan, Dean R ^a  

^a Boston University   (United States)

^b UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

Carbanion; Enzyme mechanism; Single turnover; Site directed mutagenesis

Indexed keywords

ARGININE; FRUCTOSE BISPHOSPHATE ALDOLASE; LYSINE; SCHIFF BASE; SODIUM BOROHYDRIDE;

ACID PRECIPITATION; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME DEGRADATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; RABBIT; SITE DIRECTED MUTAGENESIS; STEADY STATE;

EID: 0029970552     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.1.61     Document Type: Article

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