Structural evidence for the involvement of the residues Ser187 and Tyr422 in substrate recognition in the 3-methylcrotonyl-coenzyme A carboxylase from Pseudomonas aeruginosa

Journal of Biochemistry

Volumn 154, Issue 3, 2013, Pages 291-297

  Díaz Pérez, César ^a   Díaz Pérez, Alma Laura ^a   Rodríguez Zavala, José Salud ^b   Campos García, Jesús ^a  

^a UNIVERSIDAD MICHOACANA DE SAN NICOLÁS DE HIDALGO   (Mexico)

^b INSTITUTO NACIONAL DE CARDIOLOGÍA IGNACIO CHÁVEZ   (Mexico)

Author keywords

3 methylcrotonyl CoA; biotin carboxylase; molecular modelling; Pseudomonas aeruginosa; site directed mutagenesis

Indexed keywords

METHYLCROTONOYL COENZYME A CARBOXYLASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; NONHUMAN; PSEUDOMONAS AERUGINOSA; SITE DIRECTED MUTAGENESIS; SUBSTITUTION REACTION;

3-METHYLCROTONYL-COA; BIOTIN-CARBOXYLASE; MOLECULAR MODELLING; PSEUDOMONAS AERUGINOSA; SITE-DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CARBON-CARBON LIGASES; CATALYTIC DOMAIN; ESCHERICHIA COLI; GENE EXPRESSION; KINETICS; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PSEUDOMONAS AERUGINOSA; RECOMBINANT PROTEINS; SERINE; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 84883483389     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvt055     Document Type: Article

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