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
Functions
identical protein binding / L-aspartate / L-phenylalanine / L-tyrosine / pyridoxal phosphate binding
Processes
L-phenylalanine biosynthetic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Components
cytoplasm / cytosol
General Function
Pyridoxal phosphate binding
Specific Function
Not Available
Pfam Domain Function
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
ResourceLink
UniProtKB IDP00509
UniProtKB Entry NameAAT_ECOLI
GenBank Protein ID41011
GenBank Gene IDX03629
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01639N-Methyl-Pyridoxal-5'-PhosphateexperimentalunknownDetails
DB020243-phenylpropionic acidexperimentalunknownDetails
DB02758Indolepropionic acidexperimentalunknownDetails
DB02981Vitamin B6 Complexed with 2-Amino-Hexanoic AcidexperimentalunknownDetails
DB03553Glutaric AcidexperimentalunknownDetails
DB03629Pyridoxal-5'-Phosphate-N-OxideexperimentalunknownDetails
DB03662Vitamin B6 Complexed with 2-Amino-Pentanoic AcidexperimentalunknownDetails
DB03750Isovaleric AcidexperimentalunknownDetails
DB04083N(6)-(pyridoxal phosphate)-L-lysineexperimentalunknownDetails
DB04299Maleic acidexperimentalunknownDetails
DB04467N-(5'-phosphopyridoxyl)-L-alanineexperimentalunknownDetails
DB04762N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATEexperimentalunknownDetails
DB04765N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATEexperimentalunknownDetails
DB08845Oxogluric acidexperimental, investigational, nutraceuticalunknownDetails