Sequence of AATM_MOUSE
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
EC Number:2.6.1.7
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
Other sequences found for EC No. 2.6.1.7
General information:
Sequence
0 MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
60 NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV
120 LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
180 YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA
240 FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
300 AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS
360 NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY
420 LAHAIHQVTK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
259909
Obaru K.,Nomiyama H.,Shimada K.,Nagashima F.,Morino Y.
Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes.
J. Biol. Chem.
261
16976-16983
1986
259910
Tsuzuki T.,Obaru K.,Setoyama C.,Shimada K.
Structural organization of the mouse mitochondrial aspartate aminotransferase gene.
J. Mol. Biol.
198
21-31
1987
259911
Bradbury M.W.,Berk P.D.
Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA.
Biochem. J.
345
423-427
2000
259912
Carninci P.,Kasukawa T.,Katayama S.,Gough J.,Frith M.C.,Maeda N.,Oyama R.,Ravasi T.,Lenhard B.,Wells C.,Kodzius R.,Shimokawa K.,Bajic V.B.,Brenner S.E.,Batalov S.,Forrest A.R.,Zavolan M.,Davis M.J.,Wilming L.G.,Aidinis V.,Allen J.E.,Ambesi-Impiombato A.,Apweiler R.,Aturaliya R.N.,Bailey T.L.,Bansal M.,Baxter L.,Beisel K.W.,Bersano T.,Bono H.,Chalk A.M.,Chiu K.P.,Choudhary V.,Christoffels A.,Clutterbuck D.R.,Crowe M.L.,Dalla E.,Dalrymple B.P.,de Bono B.,Della Gatta G.,di Bernardo D.,Down T.,Engstrom P.,Fagiolini M.,Faulkner G.,Fletcher C.F.,Fukushima T.,Furuno M.,Futaki S.,Gariboldi M.,Georgii-Hemming P.,Gingeras T.R.,Gojobori T.,Green R.E.,Gustincich S.,Harbers M.,Hayashi Y.,Hensch T.K.,Hirokawa N.,Hill D.,Huminiecki L.,Iacono M.,Ikeo K.,Iwama A.,Ishikawa T.,Jakt M.,Kanapin A.,Katoh M.,Kawasawa Y.,Kelso J.,Kitamura H.,Kitano H.,Kollias G.,Krishnan S.P.,Kruger A.,Kummerfeld S.K.,Kurochkin I.V.,Lareau L.F.,Lazarevic D.,Lipovich L.,Liu J.,Liuni S.,McWilliam S.,Madan Babu M.,Madera M.,Marchionni L.,Matsuda H.,Matsuzawa S.,Miki H.,Mignone F.,Miyake S.,Morris K.,Mottagui-Tabar S.,Mulder N.,Nakano N.,Nakauchi H.,Ng P.,Nilsson R.,Nishiguchi S.,Nishikawa S.,Nori F.,Ohara O.,Okazaki Y.,Orlando V.,Pang K.C.,Pavan W.J.,Pavesi G.,Pesole G.,Petrovsky N.,Piazza S.,Reed J.,Reid J.F.,Ring B.Z.,Ringwald M.,Rost B.,Ruan Y.,Salzberg S.L.,Sandelin A.,Schneider C.,Schoenbach C.,Sekiguchi K.,Semple C.A.,Seno S.,Sessa L.,Sheng Y.,Shibata Y.,Shimada H.,Shimada K.,Silva D.,Sinclair B.,Sperling S.,Stupka E.,Sugiura K.,Sultana R.,Takenaka Y.,Taki K.,Tammoja K.,Tan S.L.,Tang S.,Taylor M.S.,Tegner J.,Teichmann S.A.,Ueda H.R.,van Nimwegen E.,Verardo R.,Wei C.L.,Yagi K.,Yamanishi H.,Zabarovsky E.,Zhu S.,Zimmer A.,Hide W.,Bult C.,Grimmond S.M.,Teasdale R.D.,Liu E.T.,Brusic V.,Quackenbush J.,Wahlestedt C.,Mattick J.S.,Hume D.A.,Kai C.,Sasaki D.,Tomaru Y.,Fukuda S.,Kanamori-Katayama M.,Suzuki M.,Aoki J.,Arakawa T.,Iida J.,Imamura K.,Itoh M.,Kato T.,Kawaji H.,Kawagashira N.,Kawashima T.,Kojima M.,Kondo S.,Konno H.,Nakano K.,Ninomiya N.,Nishio T.,Okada M.,Plessy C.,Shibata K.,Shiraki T.,Suzuki S.,Tagami M.,Waki K.,Watahiki A.,Okamura-Oho Y.,Suzuki H.,Kawai J.,Hayashizaki Y.
The transcriptional landscape of the mammalian genome.
Science
309
1559-1563
2005
259913
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
259915
Zhou S.-L.,Stump D.,Kiang C.L.,Isola L.M.,Berk P.D.
Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake.
Proc. Soc. Exp. Biol. Med.
208
263-270
1995
259916
Sacksteder C.A.,Qian W.-J.,Knyushko T.V.,Wang H.,Chin M.H.,Lacan G.,Melega W.P.,Camp D.G. II,Smith R.D.,Smith D.J.,Squier T.C.,Bigelow D.J.
Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease.
Biochemistry
45
8009-8022
2006
259917
Guidetti P.,Amori L.,Sapko M.T.,Okuno E.,Schwarcz R.
Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain.
J. Neurochem.
102
103-111
2007
259918
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
259919
Park J.,Chen Y.,Tishkoff D.X.,Peng C.,Tan M.,Dai L.,Xie Z.,Zhang Y.,Zwaans B.M.,Skinner M.E.,Lombard D.B.,Zhao Y.
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.
Mol. Cell
50
919-930
2013
259920
Rardin M.J.,Newman J.C.,Held J.M.,Cusack M.P.,Sorensen D.J.,Li B.,Schilling B.,Mooney S.D.,Kahn C.R.,Verdin E.,Gibson B.W.
Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Proc. Natl. Acad. Sci. U.S.A.
110
6601-6606
2013
259921
Guo A.,Gu H.,Zhou J.,Mulhern D.,Wang Y.,Lee K.A.,Yang V.,Aguiar M.,Kornhauser J.,Jia X.,Ren J.,Beausoleil S.A.,Silva J.C.,Vemulapalli V.,Bedford M.T.,Comb M.J.
Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
Mol. Cell. Proteomics
13
372-387
2014
259922
van Karnebeek C.D.M.,Ramos R.J.,Wen X.Y.,Tarailo-Graovac M.,Gleeson J.G.,Skrypnyk C.,Brand-Arzamendi K.,Karbassi F.,Issa M.Y.,van der Lee R.,Droegemoeller B.I.,Koster J.,Rousseau J.,Campeau P.M.,Wang Y.,Cao F.,Li M.,Ruiter J.,Ciapaite J.,Kluijtmans L.A.J.,Willemsen M.A.A.P.,Jans J.J.,Ross C.J.,Wintjes L.T.,Rodenburg R.J.,Huigen M.C.D.G.,Jia Z.,Waterham H.R.,Wasserman W.W.,Wanders R.J.A.,Verhoeven-Duif N.M.,Zaki M.S.,Wevers R.A.
Bi-allelic GOT2 mutations cause a treatable malate-aspartate shuttle-related encephalopathy.
Am. J. Hum. Genet.
105
534-548
2019
259923
Han Q.,Cai T.,Tagle D.A.,Li J.
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
Cell. Mol. Life Sci.
67
353-368
2010
259924
Han Q.,Robinson H.,Cai T.,Tagle D.A.,Li J.
Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV.
Biosci. Rep.
31
323-332
2011
