Cysteine 351 is an essential nucleophile in catalysis by Porphyromonas gingivalis peptidylarginine deiminase

Archives of Biochemistry and Biophysics

Volumn 504, Issue 2, 2010, Pages 190-196

  Rodríguez, Sofía B ^a   Stitt, Barbara L ^a   Ash, David E ^b  

^a TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b CENTRAL MICHIGAN UNIVERSITY   (United States)

Author keywords

Chemical modification; Cysteine; Peptidylarginine deiminase; Porphyromonas gingivalis; Site directed mutagenesis

Indexed keywords

CYSTEINE 351; CYSTEINE DERIVATIVE; NUCLEOPHILE; PROTEIN ARGININE DEIMINASE; SERINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; LIGAND BINDING; MASS SPECTROMETRY; PORPHYROMONAS GINGIVALIS; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

CATALYSIS; CYSTEINE; HYDROGEN-ION CONCENTRATION; HYDROLASES; IODOACETAMIDE; IODOACETIC ACID; LIGANDS; MASS SPECTROMETRY; MUTAGENESIS, SITE-DIRECTED; PEPTIDE MAPPING; PORPHYROMONAS GINGIVALIS; PROTEIN BINDING; RECOMBINANT PROTEINS;

PORPHYROMONAS GINGIVALIS;

EID: 77958197062     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2010.09.008     Document Type: Article

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