Mutational and structural analysis of l-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member

Journal of Bacteriology

Volumn 194, Issue 21, 2012, Pages 5759-5768

  Martínez Rodríguez, Sergio ^a   García Pino, Abel ^b,c   Heras Vázquez, Francisco Javier Las ^a   Clemente Jiménez, Josefa María ^a   Rodríguez Vico, Felipe ^a   García Ruiz, Juan M ^d   Loris, Remy ^b,c   Gavira, Jose Antonio ^d  

^a UNIVERSITY OF ALMERÍA   (Spain)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^d LABORATORIO DE ESTUDIOS CRISTALOGRÁFICOS   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL ENZYME; DIMER; N CARBAMOYLASE; PEPTIDASE; UNCLASSIFIED DRUG;

ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SUBSTRATE; GEOBACILLUS STEAROTHERMOPHILUS; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; STRUCTURAL ANALYSIS;

AMIDOHYDROLASES; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; GEOBACILLUS STEAROTHERMOPHILUS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SUBSTRATE SPECIFICITY;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 84868611685     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01056-12     Document Type: Article

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