catalog number :
MBS1107718
products type :
Recombinant Protein
products full name :
Recombinant Mouse Serine--pyruvate aminotransferase, mitochondrial
products short name :
Serine--pyruvate aminotransferase
products name syn :
Alanine-glyoxylate aminotransferase (EC:2.6.1.44); AGT
other names :
serine--pyruvate aminotransferase, mitochondrial isoform 1; Serine--pyruvate aminotransferase, mitochondrial; serine--pyruvate aminotransferase, mitochondrial; serine--pyruvate aminotransferase, peroxisomal; alanine-glyoxylate aminotransferase; Alanine--glyoxylate aminotransferase (EC:2.6.1.44); AGT
products gene name :
Agxt
other gene names :
Agxt; Agxt; AGT; SPT; Agt1; Agxt1; Agxt1; SPT; AGT
uniprot entry name :
SPYA_MOUSE
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
25-414
sequence :
SYQLLVPPPEALSKPLSVPTRLLLGPGPSNLAPRVLAAG
SLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSG
SGHCAMETALFNLLEPGDSFLTGTNGIWGMRAAEIADRI
GARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGES
STGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQ
QGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTK
PVSFYTDITYLAKLWGCEGET
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products description :
Dual metabolic roles of gluconeogenesis (in the mitochondria) and glyoxylate detoxification (in the peroxisomes).
products references :
The mouse alanine:glyoxylate aminotransferase gene (Agxt1)
cloning, expression, and mapping to chromosome 1.Li X.M., Salido E.C., Shapiro L.J.Somat. Cell Mol. Genet. 25:67-77(1999)
Lineage-specific biology revealed by a finished genome assembly of the mouse.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.PLoS Biol. 7:E1000112-E1000112(2009)
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.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.Mol. Cell 50:919-930(2013)
Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.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.Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013)
Crystal structure of putative aminotransferase (AAH25799.1)
from Mus musculus at 1.65 A resolution.Joint center for structural genomics (JCSG)
Submitted (OCT-2009)
to the PDB data bank
ncbi acc num :
NP_057911.2
ncbi gb acc num :
NM_016702.3
ncbi pathways :
Alanine And Aspartate Metabolism Pathway (198303); Alanine, Aspartate And Glutamate Metabolism Pathway (101155); Alanine, Aspartate And Glutamate Metabolism Pathway (100063); Carbon Metabolism Pathway (815838); Carbon Metabolism Pathway (817567); Glycine, Serine And Threonine Metabolism Pathway (83149); Glycine, Serine And Threonine Metabolism Pathway (313); Glyoxylate And Dicarboxylate Metabolism Pathway (83200); Glyoxylate And Dicarboxylate Metabolism Pathway (383); Glyoxylate Metabolism And Glycine Degradation Pathway (1324442)
uniprot summary :
AGXT: Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1); also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Protein type: Amino Acid Metabolism - alanine, aspartate and glutamate; EC 2.6.1.44; Motility/polarity/chemotaxis; Transferase; EC 2.6.1.51; Mitochondrial; Amino Acid Metabolism - glycine, serine and threonine. Cellular Component: mitochondrial matrix; mitochondrion; peroxisomal matrix; peroxisome. Molecular Function: alanine-glyoxylate transaminase activity; amino acid binding; catalytic activity; protein homodimerization activity; protein self-association; pyridoxal phosphate binding; receptor binding; serine-pyruvate transaminase activity; transaminase activity; transferase activity. Biological Process: glycine biosynthetic process, by transamination of glyoxylate; glyoxylate catabolic process; glyoxylate metabolic process; L-alanine catabolic process; L-cysteine catabolic process; Notch signaling pathway; oxalic acid secretion; proteasomal protein catabolic process; pyruvate biosynthetic process; response to cAMP; response to glucocorticoid stimulus