Aspartate aminotransferase
Details
- Name
- Aspartate aminotransferase
- Synonyms
- 2.6.1.1
- AspAT
- Transaminase A
- Gene Name
- aspC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010848|Aspartate aminotransferase MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENE TTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGC CHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
- Number of residues
- 396
- Molecular Weight
- 43572.965
- Theoretical pI
- 5.5
- GO Classification
- Functionsidentical protein binding / L-aspartate / L-phenylalanine / L-tyrosine / pyridoxal phosphate bindingProcessesL-phenylalanine biosynthetic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvateComponentscytoplasm / cytosol
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Pfam Domain Function
- Aminotran_1_2 (PF00155)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0010849|Aspartate aminotransferase (aspC) ATGTTTGAGAACATTACCGCCGCTCCTGCCGACCCGATTCTGGGCCTGGCCGATCTGTTT CGTGCCGATGAACGTCCCGGCAAAATTAACCTCGGGATTGGTGTCTATAAAGATGAGACG GGCAAAACCCCGGTACTGACCAGCGTGAAAAAGGCTGAACAGTATCTGCTCGAAAATGAA ACCACCAAAAATTACCTCGGCATTGACGGCATCCCTGAATTTGGTCGCTGCACTCAGGAA CTGCTGTTTGGTAAAGGTAGCGCCCTGATCAATGACAAACGTGCTCGCACGGCACAGACT CCGGGGGGCACTGGCGCACTACGCGTGGCTGCCGATTTCCTGGCAAAAAATACCAGCGTT AAGCGTGTGTGGGTGAGCAACCCAAGCTGGCCGAACCATAAGAGCGTCTTTAACTCTGCA GGTCTGGAAGTTCGTGAATACGCTTATTATGATGCGGAAAATCACACTCTTGACTTCGAT GCACTGATTAACAGCCTGAATGAAGCTCAGGCTGGCGACGTAGTGCTGTTCCATGGCTGC TGCCATAACCCAACCGGTATCGACCCTACGCTGGAACAATGGCAAACACTGGCACAACTC TCCGTTGAGAAAGGCTGGTTACCGCTGTTTGACTTCGCTTACCAGGGTTTTGCCCGTGGT CTGGAAGAAGATGCTGAAGGACTGCGCGCTTTCGCGGCTATGCATAAAGAGCTGATTGTT GCCAGTTCCTACTCTAAAAACTTTGGCCTGTACAACGAGCGTGTTGGCGCTTGTACTCTG GTTGCTGCCGACAGTGAAACCGTTGATCGCGCATTCAGCCAAATGAAAGCGGCGATTCGC GCTAACTACTCTAACCCACCAGCACACGGCGCTTCTGTTGTTGCCACCATCCTGAGCAAC GATGCGTTACGTGCGATTTGGGAACAAGAGCTGACTGATATGCGCCAGCGTATTCAGCGT ATGCGTCAGTTGTTCGTCAATACGCTGCAGGAAAAAGGCGCAAACCGCGACTTCAGCTTT ATCATCAAACAGAACGGCATGTTCTCCTTCAGTGGCCTGACAAAAGAACAAGTGCTGCGT CTGCGCGAAGAGTTTGGCGTATATGCGGTTGCTTCTGGTCGCGTAAATGTGGCCGGGATG ACACCAGATAACATGGCTCCGCTGTGCGAAGCGATTGTGGCAGTGCTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00509 UniProtKB Entry Name AAT_ECOLI GenBank Protein ID 41011 GenBank Gene ID X03629 - General References
- Kondo K, Wakabayashi S, Yagi T, Kagamiyama H: The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes. Biochem Biophys Res Commun. 1984 Jul 18;122(1):62-7. [Article]
- Kuramitsu S, Okuno S, Ogawa T, Ogawa H, Kagamiyama H: Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene. J Biochem. 1985 Apr;97(4):1259-62. [Article]
- Fotheringham IG, Dacey SA, Taylor PP, Smith TJ, Hunter MG, Finlay ME, Primrose SB, Parker DM, Edwards RM: The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem J. 1986 Mar 15;234(3):593-604. [Article]
- Kondo K, Wakabayashi S, Kagamiyama H: Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure. J Biol Chem. 1987 Jun 25;262(18):8648-57. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Kagamiyama H: Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes. Biochemistry. 1991 Aug 6;30(31):7796-801. [Article]
- Yano T, Kuramitsu S, Tanase S, Morino Y, Hiromi K, Kagamiyama H: The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. J Biol Chem. 1991 Apr 5;266(10):6079-85. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Mahon MM, Graber R, Christen P, Malthouse JP: The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction. Biochim Biophys Acta. 1999 Sep 14;1434(1):191-201. [Article]
- Smith DL, Almo SC, Toney MD, Ringe D: 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. Biochemistry. 1989 Oct 3;28(20):8161-7. [Article]
- Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D: Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase. Biochemistry. 1991 Feb 19;30(7):1980-5. [Article]
- Oue S, Okamoto A, Yano T, Kagamiyama H: Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J Biol Chem. 1999 Jan 22;274(4):2344-9. [Article]
- Mizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H: Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Biochemistry. 2001 Jan 16;40(2):353-60. [Article]
- Liu D, Pozharski E, Lepore BW, Fu M, Silverman RB, Petsko GA, Ringe D: Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms". Biochemistry. 2007 Sep 18;46(37):10517-27. Epub 2007 Aug 22. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01639 N-Methyl-Pyridoxal-5'-Phosphate experimental unknown Details DB02024 3-phenylpropionic acid experimental unknown Details DB02758 Indolepropionic acid experimental unknown Details DB02981 Vitamin B6 Complexed with 2-Amino-Hexanoic Acid experimental unknown Details DB03553 Glutaric Acid experimental unknown Details DB03629 Pyridoxal-5'-Phosphate-N-Oxide experimental unknown Details DB03662 Vitamin B6 Complexed with 2-Amino-Pentanoic Acid experimental unknown Details DB03750 Isovaleric Acid experimental unknown Details DB04083 N(6)-(pyridoxal phosphate)-L-lysine experimental unknown Details DB04299 Maleic acid experimental unknown Details DB04467 N-(5'-phosphopyridoxyl)-L-alanine experimental unknown Details DB04762 N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATE experimental unknown Details DB04765 N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE experimental unknown Details DB08845 Oxogluric acid experimental, investigational, nutraceutical unknown Details