Sequence of DEOC_ECOLI
EC Number:4.1.2.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
Other sequences found for EC No. 4.1.2.4
General information:
Sequence
0 MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL
60 KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD
120 LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE
180 SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL
240 LASLLKALGH GDGKSASSY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1049291
Valentin-Hansen P.,Boetius F.,Hammer-Jespersen K.,Svendsen I.
The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme.
Eur. J. Biochem.
125
561-566
1982
1049292
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
1049293
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
1049294
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
1049296
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
1049297
Stura E.A.,Ghosh S.,Garcia-Junceda E.,Chen L.,Wong C.H.,Wilson I.A.
Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: an application of reverse screening.
Proteins
22
67-72
1995
1049298
Sakuraba H.,Yoneda K.,Yoshihara K.,Satoh K.,Kawakami R.,Uto Y.,Tsuge H.,Takahashi K.,Hori H.,Ohshima T.
Sequential aldol condensation catalyzed by hyperthermophilic 2-deoxy-d-ribose-5-phosphate aldolase.
Appl. Environ. Microbiol.
73
7427-7434
2007
1049299
Heine A.,DeSantis G.,Luz J.G.,Mitchell M.,Wong C.-H.,Wilson I.A.
Observation of covalent intermediates in an enzyme mechanism at atomic resolution.
Science
294
369-374
2001
1049301
Heine A.,Luz J.G.,Wong C.H.,Wilson I.A.
Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A resolution.
J. Mol. Biol.
343
1019-1034
2004
