Sequence of AGT1_MOUSE
EC Number:2.6.1.51
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
Other sequences found for EC No. 2.6.1.51
General information:
Sequence
show sequence in normal format
>O35423|serine-pyruvate transaminase|EC 2.6.1.51|Mus musculus|Swiss-Prot
MFRMLAKASVTLGSRAAGWVRTMGSYQLLVPPPEALSKPLSVPTRLLLGPGPSNLAPRVL
AAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGD
SFLTGTNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGES
STGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGIS
LISFNDKAKYKVYSRKTKPVSFYTDITYLAKLWGCEGETRVIHHTTPVTSLYCLRESLAL
IAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSY
VLDHFSIEISGGLGPTEERVLRIGLLGYNATTENVDRVAEALREALQHCPKNKL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
896139
Li X.M.,Salido E.C.,Shapiro L.J.
The mouse alanine:glyoxylate aminotransferase gene (Agxt1): cloning, expression, and mapping to chromosome 1.
Somat. Cell Mol. Genet.
25
67-77
1999
896140
Church D.M.,Goodstadt L.,Hillier L.W.,Zody M.C.,Goldstein S.,She X.,Bult C.J.,Agarwala R.,Cherry J.L.,DiCuccio M.,Hlavina W.,Kapustin Y.,Meric P.,Maglott D.,Birtle Z.,Marques A.C.,Graves T.,Zhou S.,Teague B.,Potamousis K.,Churas C.,Place M.,Herschleb J.,Runnheim R.,Forrest D.,Amos-Landgraf J.,Schwartz D.C.,Cheng Z.,Lindblad-Toh K.,Eichler E.E.,Ponting C.P.
Lineage-specific biology revealed by a finished genome assembly of the mouse.
PLoS Biol.
7
0-0
2009
896142
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
896143
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
896144
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
896145
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