Single mutation alters the substrate specificity of l-amino acid ligase

Biochemistry

Volumn 53, Issue 16, 2014, Pages 2650-2660

  Tsuda, Takeo ^a   Asami, Mana ^a   Koguchi, Yoshiaki ^a   Kojima, Shuichi ^a  

^a GAKUSHUIN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ORGANIC POLYMERS; PEPTIDES; SUBSTRATES;

ATP-ASE ACTIVITY; BACILLUS SUBTILIS; ENANTIOSELECTIVE RECOGNITION; HYDROPHOBIC AMINO ACIDS; L-AMINO ACID LIGASE; MUTANT PROTEINS; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING;

AMINO ACIDS;

ADENOSINE TRIPHOSPHATASE; AMINO ACID DERIVATIVE; DIPEPTIDE; LIGASE; MUTANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; IN VITRO STUDY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARGININE; BACILLUS SUBTILIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDES; HYDROLYSIS; LIGASES; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 84899660383     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500292b     Document Type: Article

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