[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R.,
Plunkett G. III,
Bloch C.A.,
Perna N.T.,
Burland V.,
Riley M.,
Collado-Vides J.,
Glasner J.D.,
Rode C.K.,
Mayhew G.F.,
Gregor J.,
Davis N.W.,
Kirkpatrick H.A.,
Goeden M.A.,
Rose D.J.,
Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K.,
Morooka N.,
Yamamoto Y.,
Fujita K.,
Isono K.,
Choi S.,
Ohtsubo E.,
Baba T.,
Wanner B.L.,
Mori H.,
Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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[3]
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CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12297000 [NCBI, ExPASy, EBI, Israel, Japan]
Chung J.H.,
Park H.-Y.,
Lee J.H.,
Jang Y.;
"Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli.";
J. Biochem. Mol. Biol. 35:403-408(2002).
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[4]
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SUBSTRATE SPECIFICITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.M608708200; PubMed=17090528 [NCBI, ExPASy, EBI, Israel, Japan]
Burgis N.E.,
Cunningham R.P.;
"Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase.";
J. Biol. Chem. 282:3531-3538(2007).
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[5]
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X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
Midwest center for structural genomics (MCSG);
"Putative ribosomal protein.";
Submitted (JAN-2005) to the PDB data bank.
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- FUNCTION: Hydrolyzes O6 atom-containing purine bases deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) to nucleotide monophosphate and pyrophosphate. Probably excludes non-standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions.
- CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
- COFACTOR: Divalent cations. Maximum activity is obtained with magnesium. Activity with manganese and nickel makes up 60-75% of the maximum rate.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=0.33 mM for XTP; | | KM=0.36 mM for dITP; | | KM=0.41 mM for ITP; | | KM=16.5 µM for dHAPTP; | | Note=Vmax values are similar for XTP, dITP and ITP; | | pH dependence: |
Optimum pH is 10-10.5; | |
- SUBUNIT: Homodimer.
- MISCELLANEOUS: Activity toward dATP, dCTP and dTTP is less than 1% of the rate of XTP hydrolysis. Activity toward dGTP and dUTP is 10-12% lower than activity toward XTP. Modified or damaged nucleotides such as 6-chloropurine deoxyribose triphosphate, 8-Br-dGTP, 5-Br-dCTP, 5-Br-dUTP, 7-deaza-dGTP, 7-methyl-GTP, N6-etheno-ATP, NAD, NADH, FAD, ADP-ribose, UPD-glucose, AppA and ApppA are not hydrolyzed.
- SIMILARITY: Belongs to the HAM1 NTPase family.
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