NH2-terminal proline acts as a nucleophile in the glycosylase/AP-Lyase reaction catalyzed by Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) protein

Journal of Biological Chemistry

Volumn 272, Issue 8, 1997, Pages 5335-5341

  Zharkov, Dmitry O ^a   Rieger, Robert A ^a   Iden, Charles R ^a   Grollman, Arthur P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA GLYCOSYLTRANSFERASE; LYASE; PROLINE; SCHIFF BASE; BACTERIAL DNA; DEOXYRIBONUCLEASE IV; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE; DNA FORMAMIDOPYRIMIDINE GLYCOSYLASE, E COLI; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE, E COLI; ENDONUCLEASE IV, E COLI; ESCHERICHIA COLI PROTEIN; GLYCOSIDASE;

ARTICLE; DNA PROTEIN COMPLEX; DNA REPAIR; EXCISION REPAIR; MASS SPECTROMETRY; PRIORITY JOURNAL; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; DNA DAMAGE; ESCHERICHIA COLI; GENETICS; METABOLISM; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; DEOXYRIBONUCLEASE IV (PHAGE T4-INDUCED); DNA DAMAGE; DNA, BACTERIAL; DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LYASES; MOLECULAR SEQUENCE DATA; N-GLYCOSYL HYDROLASES; PROLINE;

EID: 0030614471     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.8.5335     Document Type: Article

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