Effect of Asp69 and Arg310 on the pK of His 68, a key catalytic residue of adenylosuccinate lyase

Protein Science

Volumn 16, Issue 8, 2007, Pages 1700-1707

  Sivendran, Sharmila ^a   Segall, Mark L ^a   Rancy, Pumtiwitt C ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

Adenylosuccinate lyase; pH Vmax profile; Site directed mutagenesis

Indexed keywords

ADENYLOSUCCINATE LYASE; ARGININE; ASPARTIC ACID; HISTIDINE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; KINETICS; LIGHT SCATTERING; MOLECULAR WEIGHT; NONHUMAN; PH; PKA; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; AMINO ACID SUBSTITUTION; CHEMISTRY; CIRCULAR DICHROISM; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

BACILLUS SUBTILIS;

ADENYLOSUCCINATE LYASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARGININE; ASPARTIC ACID; BACILLUS SUBTILIS; CATALYTIC DOMAIN; CIRCULAR DICHROISM; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; SEQUENCE ALIGNMENT;

EID: 34547601458     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072927207     Document Type: Article

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