Primary Information |
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| BoMiProt ID | Bomi4052 |
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| Protein Name | Aspartate aminotransferase, mitochondrial |
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| Organism | Bos taurus |
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| Uniprot ID | P12344 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_777231.1 |
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| Aminoacid Length | 430 |
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| Molecular Weight | 47514 |
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| FASTA Sequence |
Download |
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| Gene Name | GOT2 |
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| Gene ID | 286886 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | AST is the only enzyme, which supply of this amino acid as a substrate for many metabolic processes, such as urea cycle or purine and pyrimidine nucleotides in the liver, synthesis of L-arginine in the kidney and purine nucleotide cycle in the brain and the skeletal muscle. AST is also involved in D-aspartate production that regulates the metabolic activity at the auto-, para- and endocrine level. |
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| Biochemical Properties | There are two aspartate aminotransferase isoforms--cytoplasmic (AST1) and mitochondrial (AST2), that usually occur together and interact with each other metabolically. Both isoforms are homodimers containing highly conservative regions responsible for catalytic properties of enzyme. The common feature of all aspartate aminotransfeses is Lys - 259 residue covalent binding with prosthetic group - pyridoxal phosphate. The differences in the primary structure of AST isoforms determine their physico-chemical, kinetic and immunological properties. |
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| PTMs | Acetylation, Methylation, Nitration, Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P12344|AATM_BOVIN Aspartate aminotransferase, mitochondrial OS=Bos taurus OX=9913 GN=GOT2 PE=1 SV=2
MALLHSGRFLSGVAAAFHPGLAAAASARASSWWAHVEMGPPDPILGVT*48EAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEY*96LPIAGLAEFCKASAELALGENNEV
LKSGRYVTVQTISGTGALRIGAS*143FLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQSYR
YYDPKTCGFDFTGAIEDISKIPAQSVILLHACAHNPTGVDPRPEQWKEMATVVKKNNLFA
FFDMAYQGFASGDGNKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEE
AKRVESQLKILIRPMYSNPPINGARIASTILTSPDLRKQWLHEVKGMADRIISMRTQLVS
NLKKEGSSHNWQHIIDQIGMFCYTGLKPEQVERLTKEFSIYMTKDGRISVAGVTSGNVAY
LAHAIHQVTK
|
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | Aspartate aminotransferase is a part of the malate-aspartate shuttle in the myocardium, is involved in gluconeogenesis in the liver and kidney, glyceroneogenesis in the adipose tissue, and synthesis of neurotransmitters and neuro-glial pathway in the brain. |
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| Bibliography | 1.Mehta, P. K., Hale, T. I. & Christen, P. (1989).
Evolutionary Relationships Among Aminotransferases: Tyrosine Aminotransferase, Histidinol
Phosphate Aminotransferase, and Aspartate
Aminotransferase are Homologous Proteins. Eur.
J. Biochem. 186, 249-253. 2.Otto-Ślusarczyk D, Graboń W, Mielczarek-Puta M. Aminotransferaza asparaginianowa--kluczowy enzym w metabolizmie ogólnoustrojowym człowieka [Aspartate aminotransferase--key enzyme in the human systemic metabolism]. Postepy Hig Med Dosw (Online). 2016 Mar 16;70:219-30. Polish. doi: 10.5604/17322693.1197373. PMID: 27117097. |
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