Sequence of DEOD_ECOLI
EC Number:2.4.2.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
purine 2'-deoxyribonucleoside + phosphate = purine + 2-deoxy-alpha-D-ribose 1-phosphate
Other sequences found for EC No. 2.4.2.1
General information:
Sequence
0 MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLEDAREV NNVRGMLGFT GTYKGRKISV
60 MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVLPHVK LRDVVIGMGA CTDSKVNRIR
120 FKDHDFAAIA DFDMVRNAVD AAKALGIDAR VGNLFSADLF YSPDGEMFDV MEKYGILGVE
180 MEAAGIYGVA AEFGAKALTI CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
789217
Hershfield M.S.,Chaffee S.,Koro-Johnson L.,Mary A.,Smith A.A.,Short S.A.
Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol.
Proc. Natl. Acad. Sci. U.S.A.
88
7185-7189
1991
789218
Burland V.D.,Plunkett G. III,Sofia H.J.,Daniels D.L.,Blattner F.R.
Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.
Nucleic Acids Res.
23
2105-2119
1995
789219
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
1453-1462
1997
789220
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
0-0
2006
789221
Henzel W.J.,Billeci T.M.,Stults J.T.,Wong S.C.,Grimley C.,Watanabe C.
Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases.
Proc. Natl. Acad. Sci. U.S.A.
90
5011-5015
1993
789222
Larsen J.E.L.,Albrechtsen B.,Valentin-Hansen P.
Analysis of the terminator region after the deoCABD operon of Escherichia coli K-12 using a new class of single copy number operon-fusion vectors.
Nucleic Acids Res.
15
5125-5140
1987
789223
Jensen K.F.,Nygaard P.
Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties.
Eur. J. Biochem.
51
253-265
1975
789224
Zhang J.,Sprung R.,Pei J.,Tan X.,Kim S.,Zhu H.,Liu C.F.,Grishin N.V.,Zhao Y.
Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
Mol. Cell. Proteomics
8
215-225
2009
789225
Mao C.,Cook W.J.,Zhou M.,Koszalka G.W.,Krenitsky T.A.,Ealick S.E.
The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology.
Structure
5
1373-1383
1997
789226
Koellner G.,Luic M.,Shugar D.,Saenger W.,Bzowska A.
Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (sulphate) at 2.1-A resolution.
J. Mol. Biol.
280
153-166
1998
789227
Koellner G.,Bzowska A.,Wielgus-Kutrowska B.,Luic M.,Steiner T.,Saenger W.,Stepinski J.
Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism.
J. Mol. Biol.
315
351-371
2002
789228
Mikleusevic G.,Stefanic Z.,Narczyk M.,Wielgus-Kutrowska B.,Bzowska A.,Luic M.
Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.
Biochimie
93
1610-1622
2011
789229
Stefanic Z.,Narczyk M.,Mikleusevic G.,Kazazic S.,Bzowska A.,Luic M.
Crystallographic snapshots of ligand binding to hexameric purine nucleoside phosphorylase and kinetic studies give insight into the mechanism of catalysis.
Sci. Rep.
8
15427-15427
2018
