The role of phosphagen specificity loops in arginine kinase

Protein Science

Volumn 13, Issue 3, 2004, Pages 575-585

  Azzi, Arezki ^a   Clark, Shawn A ^a   Ellington, W Ross ^a   Chapman, Michael S ^a  

^a FLORIDA STATE UNIVERSITY   (United States)

Author keywords

Creatine kinase; Kinetics; Mutation; Phosphagen kinase; Structure; Substrate specificity

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE; ARGININE KINASE; CREATINE KINASE; CREATINE PHOSPHATE; GLUTAMIC ACID; GUANIDINE DERIVATIVE; PHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; CELL ENERGY; CHIMERA; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HOMEOSTASIS; HYDROPHILICITY; HYDROPHOBICITY; MOLECULAR SIZE; MUTANT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; REACTION ANALYSIS;

ADENOSINE DIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; ARGININE; ARGININE KINASE; BINDING SITES; CREATINE KINASE; CRYSTALLOGRAPHY, X-RAY; DATABASES, PROTEIN; HORSESHOE CRABS; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; ORGANOPHOSPHORUS COMPOUNDS; PHOSPHOCREATINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 1342331873     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03428304     Document Type: Article

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