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Journal of Biological Chemistry

Volumn 279, Issue 26, 2004, Pages 26876-26884

The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site

(2) O'Brien, Patrick J a Ellenberger, Tom a

a HARVARD MEDICAL SCHOOL (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; CATALYST ACTIVITY; CELLS; DNA; ENZYME KINETICS;

NUCLEOBASES; OLIGONUCLEOTIDES;

ESCHERICHIA COLI;

3 METHYLADENINE; ADENINE; ADENOSINE; CYTIDINE; DNA GLYCOSYLTRANSFERASE; GUANINE; GUANOSINE; NUCLEIC ACID BASE; OLIGONUCLEOTIDE; PURINE; THYMIDINE;

ARTICLE; BASE PAIRING; CATALYSIS; CELL PROTECTION; CHEMICAL BOND; DNA ALKYLATION; ENZYME ACTIVE SITE; ESCHERICHIA COLI; EXCISION REPAIR; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

BASE PAIR MISMATCH; BASE PAIRING; BINDING SITES; CATALYSIS; DNA; DNA DAMAGE; DNA GLYCOSYLASES; DNA METHYLATION; DNA REPAIR; ESCHERICHIA COLI; GLYCOSIDES; HUMANS; KINETICS; PROTEIN BINDING; PURINES; PYRIMIDINES; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 3042686671 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M403860200 Document Type: Article

Times cited : (89)

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