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Identification
NameIsocitrate lyase
Synonyms
  • ICL
  • Threo-D(S)-isocitrate glyoxylate-lyase
  • Isocitrase
  • Isocitratase
Gene NameICL1
Enzyme Class
Biological Properties
General FunctionInvolved in isocitrate lyase activity
Specific FunctionCatalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2- methylisocitrate
Cellular LocationCytoplasm
SMPDB Pathways
Glyoxylate cyclePW002419 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glyoxylate and dicarboxylate metabolismec00630 Map00630
SMPDB Reactions
D-threo-Isocitric acidSuccinic acid + Glyoxylic acid
KEGG Reactions
Isocitric acidGlyoxylic acid + Succinic acid
Metabolites
YMDB IDNameView
YMDB00026Isocitric acidShow
YMDB00033Glyoxylic acidShow
YMDB00338Succinic acidShow
YMDB16142D-threo-Isocitric acidShow
GO Classification
Component
Not Available
Function
catalytic activity
oxo-acid-lyase activity
lyase activity
carbon-carbon lyase activity
isocitrate lyase activity
Process
metabolic process
cellular metabolic process
organic acid metabolic process
oxoacid metabolic process
carboxylic acid metabolic process
Gene Properties
Chromosome Locationchromosome 5
LocusYER065C
Gene Sequence>1674 bp ATGCCTATCCCCGTTGGAAATACGAAGAACGATTTTGCAGCTTTACAAGCAAAACTAGAT GCAGATGCTGCCGAAATTGAGAAATGGTGGTCTGACTCACGTTGGAGTAAGACTAAGAGA AATTATTCAGCCAGAGATATTGCTGTTAGACGCGGGACATTCCCACCAATCGAATACCCA TCTTCGGTCATGGCCAGAAAATTATTCAAGGTATTAGAGAAGCATCACAATGAGGGTACA GTCTCTAAAACTTTCGGTGCCCTAGATCCTGTCCAGATTTCTCAAATGGCAAAATACTTA GACACAATCTATATTTCTGGTTGGCAGTGTTCATCAACTGCTTCCACCTCAAATGAACCT GGTCCAGACTTAGCTGATTATCCAATGGACACCGTTCCAAACAAAGTGGAACATTTGTTC AAGGCCCAATTGTTTCACGACAGAAAACAACTAGAGGCACGGTCAAAGGCTAAATCTCAG GAAGAACTCGATGAGATGGGTGCCCCAATTGACTACCTAACACCAATTGTCGCTGATGCA GACGCAGGCCACGGCGGTTTAACCGCAGTCTTCAAATTGACCAAGATGTTCATTGAGCGT GGTGCTGCTGGGATCCACATGGAAGACCAGACATCTACAAATAAGAAATGTGGGCATATG GCAGGAAGATGTGTTATACCCGTTCAGGAACATGTTAACAGATTGGTGACTATTAGAATG TGTGCTGATATCATGCATTCTGACTTAATTGTCGTTGCTAGGACTGATTCAGAAGCAGCC ACTTTGATTAGCTCAACCATCGATACCAGAGATCATTATTTCATTGTCGGTGCCACCAAT CCAAATATCGAGCCATTTGCCGAAGTTTTAAATGATGCCATCATGAGTGGTGCATCAGGA CAAGAACTAGCTGACATTGAACAAAAATGGTGTAGAGACGCTGGACTCAAGTTATTCCAT GAAGCCGTCATTGATGAAATTGAAAGATCAGCCCTGTCAAATAAGCAAGAATTGATTAAG AAATTCACCTCTAAAGTGGGTCCATTGACTGAAACATCCCACAGAGAAGCCAAGAAGCTC GCTAAAGAAATTCTTGGCCACGAAATTTTCTTCGACTGGGAGCTACCACGCGTAAGGGAA GGGTTGTACCGTTACAGAGGTGGGACGCAATGTTCTATCATGAGGGCCCGTGCATTTGCT CCATATGCTGATTTGGTATGGATGGAATCTAACTACCCAGACTTCCAACAGGCCAAGGAG TTTGCAGAAGGTGTTAAAGAGAAATTCCCTGACCAATGGCTAGCTTACAACTTGTCTCCA TCCTTTAACTGGCCAAAAGCCATGTCCGTTGATGAACAACACACCTTCATCCAAAGGCTG GGTGATCTAGGTTACATCTGGCAATTTATCACATTGGCCGGTTTACACACTAACGCTTTA GCTGTCCATAACTTCTCTCGTGACTTTGCCAAGGATGGGATGAAAGCTTATGCCCAGAAT GTTCAGCAGAGGGAAATGGACGATGGTGTTGATGTGTTGAAACATCAAAAATGGTCTGGT GCGGAGTACATCGATGGGTTATTGAAGTTAGCTCAAGGTGGTGTTAGCGCAACAGCTGCT ATGGGAACCGGTGTCACAGAAGATCAATTCAAAGAAAATGGCGTAAAGAAATAG
Protein Properties
Pfam Domain Function
Protein Residues557
Protein Molecular Weight62408.30078
Protein Theoretical pI6.37
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Isocitrate lyase MPIPVGNTKNDFAALQAKLDADAAEIEKWWSDSRWSKTKRNYSARDIAVRRGTFPPIEYP SSVMARKLFKVLEKHHNEGTVSKTFGALDPVQISQMAKYLDTIYISGWQCSSTASTSNEP GPDLADYPMDTVPNKVEHLFKAQLFHDRKQLEARSKAKSQEELDEMGAPIDYLTPIVADA DAGHGGLTAVFKLTKMFIERGAAGIHMEDQTSTNKKCGHMAGRCVIPVQEHVNRLVTIRM CADIMHSDLIVVARTDSEAATLISSTIDTRDHYFIVGATNPNIEPFAEVLNDAIMSGASG QELADIEQKWCRDAGLKLFHEAVIDEIERSALSNKQELIKKFTSKVGPLTETSHREAKKL AKEILGHEIFFDWELPRVREGLYRYRGGTQCSIMRARAFAPYADLVWMESNYPDFQQAKE FAEGVKEKFPDQWLAYNLSPSFNWPKAMSVDEQHTFIQRLGDLGYIWQFITLAGLHTNAL AVHNFSRDFAKDGMKAYAQNVQQREMDDGVDVLKHQKWSGAEYIDGLLKLAQGGVSATAA MGTGVTEDQFKENGVKK
References
External Links
ResourceLink
Saccharomyces Genome Database ICL1
Uniprot IDP28240
Uniprot NameACEA_YEAST
GenBank Gene IDU18813
Genebank Protein ID603301
General Reference
  • Fernandez, E., Moreno, F., Rodicio, R. (1992). "The ICL1 gene from Saccharomyces cerevisiae." Eur J Biochem 204:983-990.1551398
  • Scholer, A., Schuller, H. J. (1993). "Structure and regulation of the isocitrate lyase gene ICL1 from the yeast Saccharomyces cerevisiae." Curr Genet 23:375-381.8319292
  • Dietrich, F. S., Mulligan, J., Hennessy, K., Yelton, M. A., Allen, E., Araujo, R., Aviles, E., Berno, A., Brennan, T., Carpenter, J., Chen, E., Cherry, J. M., Chung, E., Duncan, M., Guzman, E., Hartzell, G., Hunicke-Smith, S., Hyman, R. W., Kayser, A., Komp, C., Lashkari, D., Lew, H., Lin, D., Mosedale, D., Davis, R. W., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Nature 387:78-81.9169868
  • McFadden, B. A., Rose, I. A., Williams, J. O. (1972). "Production of pyruvate and succinate by action of isocitrate lyase on -methylisocitrate." Arch Biochem Biophys 148:84-88.4259654
  • Lopez-Boado, Y. S., Herrero, P., Fernandez, T., Fernandez, R., Moreno, F. (1988). "Glucose-stimulated phosphorylation of yeast isocitrate lyase in vivo." J Gen Microbiol 134:2499-2505.3076186
  • Lopez-Boado, Y. S., Herrero, P., Fernandez, M. T., Fernandez, R., Moreno, F. (1988). "Purification of isocitrate lyase from Saccharomyces cerevisiae." Yeast 4:41-46.3059712
  • Taylor, K. M., Kaplan, C. P., Gao, X., Baker, A. (1996). "Localization and targeting of isocitrate lyases in Saccharomyces cerevisiae." Biochem J 319 ( Pt 1):255-262.8870676
  • Ordiz, I., Herrero, P., Rodicio, R., Moreno, F. (1996). "Glucose-induced inactivation of isocitrate lyase in Saccharomyces cerevisiae is mediated by the cAMP-dependent protein kinase catalytic subunits Tpk1 and Tpk2." FEBS Lett 385:43-46.8641464
  • Heinisch, J. J., Valdes, E., Alvarez, J., Rodicio, R. (1996). "Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in Saccharomyces cerevisiae." Yeast 12:1285-1295.8923733
  • Chaves, R. S., Herrero, P., Ordiz, I., Angeles del Brio, M., Moreno, F. (1997). "Isocitrate lyase localisation in Saccharomyces cerevisiae cells." Gene 198:165-169.9370278
  • Rahner, A., Hiesinger, M., Schuller, H. J. (1999). "Deregulation of gluconeogenic structural genes by variants of the transcriptional activator Cat8p of the yeast Saccharomyces cerevisiae." Mol Microbiol 34:146-156.10540293