Identification
Name:2-isopropylmalate synthase
Synonyms:
  • Alpha-IPM synthase
  • Alpha-isopropylmalate synthase
Gene Name:leuA
Enzyme Class:
Biological Properties
General Function:Involved in 2-isopropylmalate synthase activity
Specific Function:Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate)
Cellular Location:Not Available
SMPDB Pathways:
  • Leucine Biosynthesis PW000811
  • Operon: leucine biosynthesis PW001880
  • Secondary Metabolite: Leucine biosynthesis PW000980
  • Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.03-Methyl-2-oxovaleric acid+1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.03-Methyl-2-oxovaleric acid + 1.0Water + 1.0Acetyl-CoA + 1.03-Methyl-2-oxovaleric acid → 1.0Coenzyme A + 1.0Hydrogen ion + 1.02-Isopropylmalic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB004022-Isopropylmalic acidMetaboCard
ECMDB040293-Carboxy-3-hydroxy-isocaproateMetaboCard
ECMDB004913-Methyl-2-oxovaleric acidMetaboCard
ECMDB00019a-Ketoisovaleric acidMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB04092alpha-Ketoisovaleric acidMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
2-isopropylmalate synthase activity
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
branched chain family amino acid metabolic process
carboxylic acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
leucine biosynthetic process
leucine metabolic process
metabolic process
organic acid metabolic process
oxoacid metabolic process
Gene Properties
Blattner:b0074
Gene OrientationCounterclockwise
Centisome Percentage:1.77
Left Sequence End81958
Right Sequence End83529
Gene Sequence:
>1572 bp
ATGAGCCAGCAAGTCATTATTTTCGATACCACATTGCGCGACGGTGAACAGGCGTTACAG
GCAAGCTTGAGTGTGAAAGAAAAACTGCAAATTGCGCTGGCCCTTGAGCGTATGGGTGTT
GACGTGATGGAAGTCGGTTTCCCCGTCTCTTCGCCGGGCGATTTTGAATCGGTGCAAACC
ATCGCCCGCCAGGTTAAAAACAGCCGCGTATGTGCGTTAGCTCGCTGCGTGGAAAAAGAT
ATCGACGTGGCGGCCGAATCCCTGAAAGTCGCCGAAGCCTTCCGTATTCATACCTTTATT
GCCACTTCGCCAATGCACATCGCCACCAAGCTGCGCAGCACGCTGGACGAGGTGATCGAA
CGCGCTATCTATATGGTGAAACGCGCCCGTAATTACACCGATGATGTTGAATTTTCTTGC
GAAGATGCCGGGCGTACACCCATTGCCGATCTGGCGCGAGTGGTCGAAGCGGCGATTAAT
GCCGGTGCCACCACCATCAACATTCCGGACACCGTGGGCTACACCATGCCGTTTGAGTTC
GCCGGAATCATCAGCGGCCTGTATGAACGCGTGCCTAACATCGACAAAGCCATTATCTCC
GTACATACCCACGACGATTTGGGCCTGGCGGTCGGAAACTCACTGGCGGCGGTACATGCC
GGTGCACGCCAGGTGGAAGGCGCAATGAACGGGATCGGCGAGCGTGCCGGAAACTGTTCC
CTGGAAGAAGTCATCATGGCGATCAAAGTTCGTAAGGATATTCTCAACGTCCACACCGCC
ATTAATCACCAGGAGATATGGCGCACCAGCCAGTTAGTTAGCCAGATTTGTAATATGCCG
ATCCCGGCAAACAAAGCCATTGTTGGCAGCGGCGCATTCGCACACTCCTCCGGTATACAC
CAGGATGGCGTGCTGAAAAACCGCGAAAACTACGAAATCATGACACCAGAATCTATTGGT
CTGAACCAAATCCAGCTGAATCTGACCTCTCGTTCGGGGCGTGCGGCGGTGAAACATCGC
ATGGATGAGATGGGGTATAAAGAAAGTGAATATAATTTAGACAATTTGTACGATGCTTTC
CTGAAGCTGGCGGACAAAAAAGGTCAGGTGTTTGATTACGATCTGGAGGCGCTGGCCTTC
ATCGGTAAGCAGCAAGAAGAGCCGGAGCATTTCCGTCTGGATTACTTCAGCGTGCAGTCT
GGCTCTAACGATATCGCCACCGCCGCCGTCAAACTGGCCTGTGGCGAAGAAGTCAAAGCA
GAAGCCGCCAACGGTAACGGTCCGGTCGATGCCGTCTATCAGGCAATTAACCGCATCACT
GAATATAACGTCGAACTGGTGAAATACAGCCTGACCGCCAAAGGCCACGGTAAAGATGCG
CTGGGTCAGGTGGATATCGTCGCTAACTACAACGGTCGCCGCTTCCACGGCGTCGGCCTG
GCTACCGATATTGTCGAGTCATCTGCCAAAGCCATGGTGCACGTTCTGAACAATATCTGG
CGTGCCGCAGAAGTCGAAAAAGAGTTGCAACGCAAAGCTCAACACAACGAAAACAACAAG
GAAACCGTGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:523
Protein Molecular Weight:57297
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-isopropylmalate synthase
MSQQVIIFDTTLRDGEQALQASLSVKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQT
IARQVKNSRVCALARCVEKDIDVAAESLKVAEAFRIHTFIATSPMHIATKLRSTLDEVIE
RAIYMVKRARNYTDDVEFSCEDAGRTPIADLARVVEAAINAGATTINIPDTVGYTMPFEF
AGIISGLYERVPNIDKAIISVHTHDDLGLAVGNSLAAVHAGARQVEGAMNGIGERAGNCS
LEEVIMAIKVRKDILNVHTAINHQEIWRTSQLVSQICNMPIPANKAIVGSGAFAHSSGIH
QDGVLKNRENYEIMTPESIGLNQIQLNLTSRSGRAAVKHRMDEMGYKESEYNLDNLYDAF
LKLADKKGQVFDYDLEALAFIGKQQEEPEHFRLDYFSVQSGSNDIATAAVKLACGEEVKA
EAANGNGPVDAVYQAINRITEYNVELVKYSLTAKGHGKDALGQVDIVANYNGRRFHGVGL
ATDIVESSAKAMVHVLNNIWRAAEVEKELQRKAQHNENNKETV
References
External Links:
ResourceLink
Uniprot ID:P09151
Uniprot Name:LEU1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674317
Ecogene ID:EG11226
Ecocyc:EG11226
ColiBase:b0074
Kegg Gene:b0074
EchoBASE ID:EB1208
CCDB:LEU1_ECOLI
BacMap:16128068
General Reference:
  • 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
  • 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
  • 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
  • Wessler, S. R., Calvo, J. M. (1981). "Control of leu operon expression in Escherichia coli by a transcription attenuation mechanism." J Mol Biol 149:579-597. Pubmed: 6171647
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901