Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti

Protein Science

Volumn 15, Issue 12, 2006, Pages 2729-2738

  Martínez Rodríguez, Sergio ^a,d   Andújar Sánchez, Montserrat ^a   Neira, Jose L ^b,c   Clemente Jiménez, Josefa M ^a   Jara Pérez, Vicente ^a   Rodríguez Vico, Felipe ^a   Las Heras Vázquez, Francisco J ^a  

^a UNIVERSITY OF ALMERÍA   (Spain)

^b MIGUEL HERNÁNDEZ UNIVERSITY   (Spain)

^c UNIVERSITY OF ZARAGOZA   (Spain)

^d VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

Author keywords

Circular dichroism; Fluorescence; Hydantoin racemase; Isothermal titration calorimetry; Mutagenesis; Reaction mechanism

Indexed keywords

ALANINE; CYSTEINE 181; CYSTEINE 76; CYSTEINE DERIVATIVE; HYDANTOIN DERIVATIVE; HYDANTOIN RACEMASE; RACEMASE;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME BINDING; FLUORESCENCE ANALYSIS; ISOMER; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; RACEMIZATION; SEQUENCE ANALYSIS; SINORHIZOBIUM MELILOTI; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BINDING SITES; CALORIMETRY; CATALYSIS; CIRCULAR DICHROISM; CLONING, MOLECULAR; COMPUTER SIMULATION; CONSERVED SEQUENCE; CYSTEINE; FLUORESCENCE; GUANIDINE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; RACEMASES AND EPIMERASES; SEQUENCE ANALYSIS, PROTEIN; SEQUENCE HOMOLOGY, AMINO ACID; SINORHIZOBIUM MELILOTI;

SINORHIZOBIUM MELILOTI;

EID: 33751505449     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062452106     Document Type: Article

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