His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate

FEBS Letters

Volumn 571, Issue 1-3, 2004, Pages 17-20

  Kiss, András L ^a   Szeltner, Zoltán ^a   Fülöp, Vilmos ^b   Polgár, László ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

Acylaminoacyl peptidase; Catalytic mechanism; EDTA, ethylenediaminetetraacetic acid; Oligopeptidase; Oxyanion binding site; PCR, polymerase chain reaction

Indexed keywords

ACYLAMINOACYL PEPTIDASE; HISTIDINE; PEPTIDASE; PROLYL ENDOPEPTIDASE; SERINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CATALYSIS; ENZYME MODIFICATION; ENZYME STRUCTURE; LIVER; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; SWINE;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATALYSIS; ENZYME STABILITY; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SWINE;

EID: 3342962414     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.06.054     Document Type: Article

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