Aminotransferase
From Proteopedia
FunctionAminotransferase or transaminase catalyze the reversible exchange of amino group of an amino acid with a keto group of an alpha-keto acid. Aminotransferases use pyridoxal phosphate (PLP) as cofactor. Histidinol-phosphate aminotransferase (HPA) catalyzes the interconversion of L-histidinol phosphate and 2-oxoglutarate to L-glutarate and 3-(imidazole-4-yl)-2-oxopropyl phosphate. HPA is part of the metabolism of histidine, phenylalanine and tyrosine. [1] Gamma-aminobutyrate aminotransferase (GABA) catalyzes the intercorversion of 4-aminobutanoate and 2-oxoglutarate to succinate semialdehyde and L-glutamate. Aspartate aminotransferase (AAT) catalyzes the intercorversion of aspartate and α-ketoglutarate to oxaloacetate and glutamate. For details on AAT see Aspartate Aminotransferase.[2] Phosphoserine aminotransferase (PSAT) catalyzes the intercorversion of phosphoserine and oxoglutarate to phosphonooxypyruvate and glutamate. For details on PSAT see Phosphoserine aminotransferase.[3] Alanine glyoxylate aminotransferase (AGA) catalyzes the intercorversion of alanine and glyoxate to methyloxopropanoate and glycine. D-amino acid aminotransferase (AAT) catalyzes the intercorversion of D-alanine and oxoglutarate to pyruvate and D-glutamate. Aromatic amino acid aminotransferase (AROAT) catalyzes the intercorversion of aromatic amino acid and oxoglutarate to aromatic oxo acid and glutamate. Lysine aminotransferase (LYSAT) catalyzes the intercorversion of lysine and oxoglutarate to aminoadipate semialdeyde and glutamate. ArnB aminotransferase is a PLP-dependent aminotransferase in the pathway of biosynthesis of arabinose-4N lipid A[4]. PseC aminotransferase is an aminotransferase in the pathway of biosynthesis of pseudaminic acid[5]. WbpE aminotransferase is a PLP-dependent aminotransferase in the pathway of biosynthesis of Pseudomonas aerugingsa central carbohydrate[6]. RelevanceElevated levels of alanine aminotransferase and aspartate aminotransferase are indicators of liver damage. Structural highlightsThe active site of histidinol-phosphate aminotransferase contains PLP.[7] 3D structures of aminotransferaseAminotransferase 3D structures
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References
- ↑ Mizuguchi H, Hayashi H, Miyahara I, Hirotsu K, Kagamiyama H. Characterization of histidinol phosphate aminotransferase from Escherichia coli. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):321-4. PMID:12686152
- ↑ Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol. 1984 Apr 15;174(3):497-525. PMID:6143829 doi:http://dx.doi.org/10.1016/0022-2836(84)90333-4
- ↑ Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol. 1984 Apr 15;174(3):497-525. PMID:6143829 doi:http://dx.doi.org/10.1016/0022-2836(84)90333-4
- ↑ Lee M, Sousa MC. Structural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative Bacteria. Biochemistry. 2014 Feb 4;53(4):796-805. doi: 10.1021/bi4015677. Epub 2014 Jan 24. PMID:24460375 doi:http://dx.doi.org/10.1021/bi4015677
- ↑ Schoenhofen IC, Lunin VV, Julien JP, Li Y, Ajamian E, Matte A, Cygler M, Brisson JR, Aubry A, Logan SM, Bhatia S, Wakarchuk WW, Young NM. Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori. J Biol Chem. 2006 Mar 31;281(13):8907-16. Epub 2006 Jan 18. PMID:16421095 doi:10.1074/jbc.M512987200
- ↑ Larkin A, Olivier NB, Imperiali B. Structural Analysis of WbpE from Pseudomonas aeruginosa PAO1: A Nucleotide Sugar Aminotransferase Involved in O-Antigen Assembly . Biochemistry. 2010 Jul 28. PMID:20604544 doi:10.1021/bi100805b
- ↑ Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H. Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Biochemistry. 2001 Apr 17;40(15):4633-44. PMID:11294630
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