Sequence of ASPG2_ECOLI
EC Number:3.5.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-asparagine + H2O = L-aspartate + NH3
Other sequences found for EC No. 3.5.1.1
General information:
Sequence
0 MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG KVGVENLVNA
60 VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD KTDGFVITHG TDTMEETAYF
120 LDLTVKCDKP VVMVGAMRPS TSMSADGPFN LYNAVVTAAD KASANRGVLV VMNDTVLDGR
180 DVTKTNTTDV ATFKSVNYGP LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY
240 NYANASDLPA KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT
300 TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
392109
Jennings M.P.,Beacham I.R.
Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins.
J. Bacteriol.
172
1491-1498
1990
392110
Bonthron D.T.
L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene.
Gene
91
101-105
1990
392111
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
392112
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
392113
Maita T.,Matsuda G.
The primary structure of L-asparaginase from Escherichia coli.
Hoppe-Seyler's Z. Physiol. Chem.
361
105-117
1980
392114
Maita T.,Morokuma K.,Matsuda G.
Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli.
Hoppe-Seyler's Z. Physiol. Chem.
360
1483-1495
1979
392115
Peterson R.G.,Richards F.F.,Handschumacher R.E.
Structure of peptide from active site region of Escherichia coli L-asparaginase.
J. Biol. Chem.
252
2072-2076
1977
392116
Greenquist A.C.,Wriston J.C. Jr.
Chemical evidence for identical subunits in L-asparaginase from Escherichia coli B.
Arch. Biochem. Biophys.
152
280-286
1972
392117
Harms E.,Wehner A.,Aung H.P.,Roehm K.H.
A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis.
FEBS Lett.
285
55-58
1991
392118
Wehner A.,Harms E.,Jennings M.P.,Beacham I.R.,Derst C.,Bast P.,Roehm K.H.
Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis.
Eur. J. Biochem.
208
475-480
1992
392119
Ders C.,Henseling J.,Roehm K.H.
Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis.
Protein Eng.
5
785-789
1992
392120
Swain A.L.,Jaskolski M.,Housset D.,Rao J.K.M.,Wlodawer A.
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.
Proc. Natl. Acad. Sci. U.S.A.
90
1474-1478
1993
392121
Palm G.J.,Lubkowski J.,Derst C.,Schleper S.,Roehm K.H.,Wlodawer A.
A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant.
FEBS Lett.
390
211-216
1996
392122
Sanches M.,Barbosa J.A.,de Oliveira R.T.,Abrahao Neto J.,Polikarpov I.
Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups.
Acta Crystallogr. D
59
416-422
2003
