Sequence of AAT_ECOLI
EC Number:2.6.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Other sequences found for EC No. 2.6.1.1
General information:
Sequence
0 MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE
60 TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT PGGTGALRVA ADFLAKNTSV
120 KRVWVSNPSW PNHKSVFNSA GLEVREYAYY DAENHTLDFD ALINSLNEAQ AGDVVLFHGC
180 CHNPTGIDPT LEQWQTLAQL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV
240 ASSYSKNFGL YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN
300 DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKEQVLR
360 LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1152601
Kondo K.,Wakabayashi S.,Yagi T.,Kagamiyama H.
The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes.
Biochem. Biophys. Res. Commun.
122
62-67
1984
1152602
Kuramitsu S.,Okuno S.,Ogawa T.,Ogawa H.,Kagamiyama H.
Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene.
J. Biochem.
97
1259-1262
1985
1152603
Fotheringham I.G.,Dacey S.A.,Taylor P.P.,Smith T.J.,Hunter M.G.,Finlay M.E.,Primrose S.B.,Parker D.M.,Edwards R.M.
The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes.
Biochem. J.
234
593-604
1986
1152604
Kondo K.,Wakabayashi S.,Kagamiyama H.
Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure.
J. Biol. Chem.
262
8648-8657
1987
1152605
Oshima T.,Aiba H.,Baba T.,Fujita K.,Hayashi K.,Honjo A.,Ikemoto K.,Inada T.,Itoh T.,Kajihara M.,Kanai K.,Kashimoto K.,Kimura S.,Kitagawa M.,Makino K.,Masuda S.,Miki T.,Mizobuchi K.,Mori H.,Motomura K.,Nakamura Y.,Nashimoto H.,Nishio Y.,Saito N.,Sampei G.,Seki Y.,Tagami H.,Takemoto K.,Wada C.,Yamamoto Y.,Yano M.,Horiuchi T.
A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.
DNA Res.
3
137-155
1996
1152606
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
1152607
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
1152608
Link A.J.,Robison K.,Church G.M.
Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Electrophoresis
18
1259-1313
1997
1152609
Inoue K.,Kuramitsu S.,Okamoto A.,Hirotsu K.,Higuchi T.,Kagamiyama H.
Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.
Biochemistry
30
7796-7801
1991
1152610
Yano T.,Kuramitsu S.,Tanase S.,Morino Y.,Hiromi K.,Kagamiyama H.
The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.
J. Biol. Chem.
266
6079-6085
1991
1152611
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
1152612
Mahon M.M.,Graber R.,Christen P.,Malthouse J.P.
The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction.
Biochim. Biophys. Acta
1434
191-201
1999
1152613
Tan J.,Kan N.,Wang W.,Ling J.,Qu G.,Jin J.,Shao Y.,Liu G.,Chen H.
Construction of 2,4,6-trinitrotoluene biosensors with novel sensing elements from Escherichia coli K-12 MG1655.
Cell Biochem. Biophys.
72
417-428
2015
1152614
Smith D.L.,Almo S.C.,Toney M.D.,Ringe D.
2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
Biochemistry
28
8161-8167
1989
1152615
Danishefsky A.T.,Onnufer J.J.,Petsko G.A.,Ringe D.
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.
Biochemistry
30
1980-1985
1991
1152616
Oue S.,Okamoto A.,Yano T.,Kagamiyama H.
Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.
J. Biol. Chem.
274
2344-2349
1999
1152617
Mizuguchi H.,Hayashi H.,Okada K.,Miyahara I.,Hirotsu K.,Kagamiyama H.
Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
Biochemistry
40
353-360
2001
1152618
Liu D.,Pozharski E.,Lepore B.W.,Fu M.,Silverman R.B.,Petsko G.A.,Ringe D.
Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals 'a tale of two mechanisms'.
Biochemistry
46
10517-10527
2007
