Aspartate aminotransferase (P00509)

• AspAT
• Transaminase A

• 2.6.1.1

• Asparagine biosynthesis PW000813
• Aspartate metabolism PW000787
• Collection of Reactions without pathways PW001891
• Hydrogen Sulfide Biosynthesis I PW002066
• L-glutamate metabolism PW000789
• Phenylalanine metabolism PW000921
• phenylalanine biosynthesis PW000807
• threonine biosynthesis PW000817

• Alanine, aspartate and glutamate metabolism ec00250
• Arginine and proline metabolism ec00330
• Carbon fixation in photosynthetic organisms ec00710
• Cysteine and methionine metabolism ec00270
• Isoquinoline alkaloid biosynthesis ec00950
• Metabolic pathways eco01100
• Microbial metabolism in diverse environments ec01120
• Novobiocin biosynthesis ec00401
• Phenylalanine metabolism ec00360
• Phenylalanine, tyrosine and tryptophan biosynthesis ec00400
• Tropane, piperidine and pyridine alkaloid biosynthesis ec00960
• Tyrosine metabolism ec00350

>1191 bp
ATGTTTGAGAACATTACCGCCGCTCCTGCCGACCCGATTCTGGGCCTGGCCGATCTGTTT
CGTGCCGATGAACGTCCCGGCAAAATTAACCTCGGGATTGGTGTCTATAAAGATGAGACG
GGCAAAACCCCGGTACTGACCAGCGTGAAAAAGGCTGAACAGTATCTGCTCGAAAATGAA
ACCACCAAAAATTACCTCGGCATTGACGGCATCCCTGAATTTGGTCGCTGCACTCAGGAA
CTGCTGTTTGGTAAAGGTAGCGCCCTGATCAATGACAAACGTGCTCGCACGGCACAGACT
CCGGGGGGCACTGGCGCACTACGCGTGGCTGCCGATTTCCTGGCAAAAAATACCAGCGTT
AAGCGTGTGTGGGTGAGCAACCCAAGCTGGCCGAACCATAAGAGCGTCTTTAACTCTGCA
GGTCTGGAAGTTCGTGAATACGCTTATTATGATGCGGAAAATCACACTCTTGACTTCGAT
GCACTGATTAACAGCCTGAATGAAGCTCAGGCTGGCGACGTAGTGCTGTTCCATGGCTGC
TGCCATAACCCAACCGGTATCGACCCTACGCTGGAACAATGGCAAACACTGGCACAACTC
TCCGTTGAGAAAGGCTGGTTACCGCTGTTTGACTTCGCTTACCAGGGTTTTGCCCGTGGT
CTGGAAGAAGATGCTGAAGGACTGCGCGCTTTCGCGGCTATGCATAAAGAGCTGATTGTT
GCCAGTTCCTACTCTAAAAACTTTGGCCTGTACAACGAGCGTGTTGGCGCTTGTACTCTG
GTTGCTGCCGACAGTGAAACCGTTGATCGCGCATTCAGCCAAATGAAAGCGGCGATTCGC
GCTAACTACTCTAACCCACCAGCACACGGCGCTTCTGTTGTTGCCACCATCCTGAGCAAC
GATGCGTTACGTGCGATTTGGGAACAAGAGCTGACTGATATGCGCCAGCGTATTCAGCGT
ATGCGTCAGTTGTTCGTCAATACGCTGCAGGAAAAAGGCGCAAACCGCGACTTCAGCTTT
ATCATCAAACAGAACGGCATGTTCTCCTTCAGTGGCCTGACAAAAGAACAAGTGCTGCGT
CTGCGCGAAGAGTTTGGCGTATATGCGGTTGCTTCTGGTCGCGTAAATGTGGCCGGGATG
ACACCAGATAACATGGCTCCGCTGTGCGAAGCGATTGTGGCAGTGCTGTAA

• Aminotran_1_2 (PF00155 )

• None

• None

>Aspartate aminotransferase
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENE
TTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSV
KRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQAGDVVLFHGC
CHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV
ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLR
LREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL

• Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
• Danishefsky, A. T., Onnufer, J. J., Petsko, G. A., Ringe, D. (1991). "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase." Biochemistry 30:1980-1985. Pubmed: 1993208
• Fotheringham, I. G., Dacey, S. A., Taylor, P. P., Smith, T. J., Hunter, M. G., Finlay, M. E., Primrose, S. B., Parker, D. M., Edwards, R. M. (1986). "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 234:593-604. Pubmed: 3521591
• Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
• Inoue, K., Kuramitsu, S., Okamoto, A., Hirotsu, K., Higuchi, T., Kagamiyama, H. (1991). "Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes." Biochemistry 30:7796-7801. Pubmed: 1868057
• Kondo, K., Wakabayashi, S., Kagamiyama, H. (1987). "Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure." J Biol Chem 262:8648-8657. Pubmed: 3298240
• Kondo, K., Wakabayashi, S., Yagi, T., Kagamiyama, H. (1984). "The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes." Biochem Biophys Res Commun 122:62-67. Pubmed: 6378205
• Kuramitsu, S., Okuno, S., Ogawa, T., Ogawa, H., Kagamiyama, H. (1985). "Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene." J Biochem 97:1259-1262. Pubmed: 3897210
• Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
• Liu, D., Pozharski, E., Lepore, B. W., Fu, M., Silverman, R. B., Petsko, G. A., Ringe, D. (2007). "Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms"." Biochemistry 46:10517-10527. Pubmed: 17713924
• Mahon, M. M., Graber, R., Christen, P., Malthouse, J. P. (1999). "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 1434:191-201. Pubmed: 10556573
• Mizuguchi, H., Hayashi, H., Okada, K., Miyahara, I., Hirotsu, K., Kagamiyama, H. (2001). "Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase." Biochemistry 40:353-360. Pubmed: 11148029
• 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
• Oue, S., Okamoto, A., Yano, T., Kagamiyama, H. (1999). "Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues." J Biol Chem 274:2344-2349. Pubmed: 9891001
• Smith, D. L., Almo, S. C., Toney, M. D., Ringe, D. (1989). "2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli." Biochemistry 28:8161-8167. Pubmed: 2513875
• Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., Hiromi, K., Kagamiyama, H. (1991). "The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase." J Biol Chem 266:6079-6085. Pubmed: 2007566