The Gene e.1 (nudE.1) of T4 Bacteriophage Designates a New Member of the Nudix Hydrolase Superfamily Active on Flavin Adenine Dinucleotide, Adenosine 5′-Triphospho-5′-adenosine, and ADP-ribose
Open Access
- 1 June 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (26), 23181-23185
- https://doi.org/10.1074/jbc.m203325200
Abstract
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This publication has 18 references indexed in Scilit:
- The three-dimensional structure of the nudix enzyme diadenosine tetraphosphate hydrolase from Lupinus angustifolius LJournal of Molecular Biology, 2000
- Gapped BLAST and PSI-BLAST: a new generation of protein database search programsNucleic Acids Research, 1997
- Solution Structure of the Quaternary MutT−M2+−AMPCPP−M2+ Complex and Mechanism of Its Pyrophosphohydrolase Action,Biochemistry, 1997
- The Role of Glu 57 in the Mechanism of the Escherichia coli MutT Enzyme by Mutagenesis and Heteronuclear NMRBiochemistry, 1996
- Characterization of the mutX gene of Streptococcus pneumoniae as a homologue of Escherichia coli mutT, and tentative definition of a catalytic domain of the dGTP pyrophosphohydroiasesMolecular Microbiology, 1994
- MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesisNature, 1992
- Basic local alignment search toolJournal of Molecular Biology, 1990
- The isolation and characterization of TabR bacteria: Hosts that restrict bacteriophage T4 rII mutantsMolecular Genetics and Genomics, 1982
- Detection of proteolytic enzymes in polyacrylamide gelsAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976