Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase

Protein Science

Volumn 16, Issue 3, 2007, Pages 441-448

  Segall, Mark L ^a   Cashman, Meghan A ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

Adenylosuccinate lyase; Hydrogen bonding; Purine biosynthesis; Site directed mutagenesis

Indexed keywords

ADENYLOSUCCINATE LYASE; ALANINE; AMINO ACID; ASPARAGINE; ENZYME; HISTIDINE; MUTANT PROTEIN; S306A PROTEIN; S94A PROTEIN; SERINE; T140A PROTEIN; T93A PROTEIN; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CIRCULAR DICHROISM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME PH; ENZYME SUBSTRATE; HYDROGEN BOND; MUTAGENESIS; MUTANT; PH; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; WILD TYPE;

ADENYLOSUCCINATE LYASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACILLUS SUBTILIS; CIRCULAR DICHROISM; HYDROXY ACIDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; SERINE; THREONINE;

BACILLUS SUBTILIS;

EID: 33847323201     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062650007     Document Type: Article

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