Identification
Name:3-isopropylmalate dehydrogenase
Synonyms:
  • 3-IPM-DH
  • Beta-IPM dehydrogenase
  • IMDH
Gene Name:leuB
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate
Cellular Location:Cytoplasm
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:
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SMPDB Reactions:
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EcoCyc Reactions:
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Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
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Metabolites:
ECMDB IDNameView
ECMDB121492-Isopropyl-3-oxosuccinateMetaboCard
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB041583-IsopropylmalateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB20137D-Erythro-3-MethylmalateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00695KetoleucineMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
3-isopropylmalate dehydrogenase activity
binding
catalytic activity
cation binding
ion binding
magnesium ion binding
metal ion binding
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
branched chain family amino 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
oxidation reduction
Gene Properties
Blattner:b0073
Gene OrientationCounterclockwise
Centisome Percentage:1.74
Left Sequence End80867
Right Sequence End81958
Gene Sequence:
>1092 bp
ATGTCGAAGAATTACCATATTGCCGTATTGCCGGGGGACGGTATTGGTCCGGAAGTGATG
ACCCAGGCGCTGAAAGTGCTGGATGCCGTGCGCAACCGCTTTGCGATGCGCATCACCACC
AGCCATTACGATGTAGGCGGCGCAGCCATTGATAACCACGGGCAACCACTGCCGCCTGCG
ACGGTTGAAGGTTGTGAGCAAGCCGATGCCGTGCTGTTTGGCTCGGTAGGCGGCCCGAAG
TGGGAACATTTACCACCAGACCAGCAACCAGAACGCGGCGCGCTGCTGCCTCTGCGTAAG
CACTTCAAATTATTCAGCAACCTGCGCCCGGCAAAACTGTATCAGGGGCTGGAAGCATTC
TGTCCGCTGCGTGCAGACATTGCCGCAAACGGCTTCGACATCCTGTGTGTGCGCGAACTG
ACCGGCGGCATCTATTTCGGTCAGCCAAAAGGCCGCGAAGGTAGCGGACAATATGAAAAA
GCCTTTGATACCGAGGTGTATCACCGTTTTGAGATCGAACGTATCGCCCGCATCGCGTTT
GAATCTGCTCGCAAGCGTCGCCACAAAGTGACGTCGATCGATAAAGCCAACGTGCTGCAA
TCCTCTATTTTATGGCGGGAGATCGTTAACGAGATCGCCACGGAATACCCGGATGTCGAA
CTGGCGCATATGTACATCGACAACGCCACCATGCAGCTGATTAAAGATCCATCACAGTTT
GACGTTCTGCTGTGCTCCAACCTGTTTGGCGACATTCTGTCTGACGAGTGCGCAATGATC
ACTGGCTCGATGGGGATGTTGCCTTCCGCCAGCCTGAACGAGCAAGGTTTTGGACTGTAT
GAACCGGCGGGCGGCTCGGCACCAGATATCGCAGGCAAAAACATCGCCAACCCGATTGCA
CAAATCCTTTCGCTGGCACTGCTGCTGCGTTACAGCCTGGATGCCGATGATGCGGCTTGC
GCCATTGAACGCGCCATTAACCGCGCATTAGAAGAAGGCATTCGCACCGGGGATTTAGCC
CGTGGCGCTGCCGCCGTTAGTACCGATGAAATGGGCGATATCATTGCCCGCTATGTAGCA
GAAGGGGTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:363
Protein Molecular Weight:39517
Protein Theoretical pI:5
PDB File:1CM7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-isopropylmalate dehydrogenase
MSKNYHIAVLPGDGIGPEVMTQALKVLDAVRNRFAMRITTSHYDVGGAAIDNHGQPLPPA
TVEGCEQADAVLFGSVGGPKWEHLPPDQQPERGALLPLRKHFKLFSNLRPAKLYQGLEAF
CPLRADIAANGFDILCVRELTGGIYFGQPKGREGSGQYEKAFDTEVYHRFEIERIARIAF
ESARKRRHKVTSIDKANVLQSSILWREIVNEIATEYPDVELAHMYIDNATMQLIKDPSQF
DVLLCSNLFGDILSDECAMITGSMGMLPSASLNEQGFGLYEPAGGSAPDIAGKNIANPIA
QILSLALLLRYSLDADDAACAIERAINRALEEGIRTGDLARGAAAVSTDEMGDIIARYVA
EGV
References
External Links:
ResourceLink
Uniprot ID:P30125
Uniprot Name:LEU3_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321955
PDB ID:1CM7
Ecogene ID:EG11577
Ecocyc:EG11577
ColiBase:b0073
Kegg Gene:b0073
EchoBASE ID:EB1537
CCDB:LEU3_ECOLI
BacMap:90111082
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
  • Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., Oshima, T. (1994). "Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus." Eur J Biochem 220:275-281. Pubmed: 8119295
  • 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
  • Magyar, C., Szilagyi, A., Zavodszky, P. (1996). "Relationship between thermal stability and 3-D structure in a homology model of 3-isopropylmalate dehydrogenase from Escherichia coli." Protein Eng 9:663-670. Pubmed: 8875643
  • Wallon, G., Kryger, G., Lovett, S. T., Oshima, T., Ringe, D., Petsko, G. A. (1997). "Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus." J Mol Biol 266:1016-1031. Pubmed: 9086278
  • 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