Thermodynamic and mutational studies of l-N-carbamoylase from Sinorhizobium meliloti CECT 4114 catalytic centre

Biochimie

Volumn 88, Issue 7, 2006, Pages 837-847

  Martínez Rodríguez, Sergio ^a   Andújar Sánchez, Montserrat ^a   Clemente Jiménez, Josefa María ^a   Jara Pérez, Vicente ^a   Rodríguez Vico, Felipe ^a   Heras Vázquez, Francisco Javier Las ^a  

^a UNIVERSITY OF ALMERÍA   (Spain)

Author keywords

Isothermal titration calorimetry; l Amino acids; l N carbamoylase; Modelling; Mutagenesis

Indexed keywords

ALPHA AMINO ACID; ARGININE; ASPARAGINE; BACTERIAL ENZYME; GLUTAMINE; HISTIDINE; N CARBAMOYL AMINO ACID AMIDOHYDROLASE; NICKEL; UNCLASSIFIED DRUG; AMIDASE; MUTANT PROTEIN; N CARBAMOYLAMINO ACID AMIDOHYDROLASE; N-CARBAMOYLAMINO ACID AMIDOHYDROLASE;

ARTICLE; BACTERIUM MUTANT; BINDING SITE; CATALYSIS; CONTROLLED STUDY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS KINETICS; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR MECHANICS; MOLECULAR MODEL; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY; SINORHIZOBIUM MELILOTI; THERMODYNAMICS; WILD TYPE; AMINO ACID SEQUENCE; CALORIMETRY; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; MUTATION; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

SACCHAROMYCES KLUYVERI; SINORHIZOBIUM MELILOTI;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; CALORIMETRY; CATALYTIC DOMAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SINORHIZOBIUM MELILOTI; THERMODYNAMICS;

EID: 33746735563     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.01.012     Document Type: Article

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