Geranylgeranyltransferase may be used to refer to either Geranylgeranyltransferase type 1 or Rab geranylgeranyltransferase
Geranylgeranyltransferase type 1 or simply geranylgeranyltransferase is one of the three enzymes in the prenyltransferase group. In specific terms, Geranylgeranyltransferase (GGTase 1) adds a 20-carbon isoprenoid called a geranylgeranyl group to proteins bearing a CaaX motif: a four-amino acid sequence at the carboxyl terminal of a protein. Geranylgeranyltransferase inhibitors are being investigated as anti-cancer agents.[1]
Prenyltransferases, including geranylgeranyltransferase, posttranslationally modify proteins by adding an isoprenoid lipid called a prenyl group to the carboxyl terminus of the target protein. This process, called prenylation, causes prenylated proteins to become membrane-associated due to the hydrophobic nature of the prenyl group. Most prenylated proteins are involved in cellular signaling, wherein membrane association is critical for function.[1]
Structure
Geranylgeranyltransferase contains two subunits, α and β that are encoded by the FNTA and PGGT1B genes, respectively. Both subunits are composed primarily of alpha helices. Geranylgeranyltransferase coordinates a zinc cation on its β subunit at the lip of the active site. Geranylgeranyltransferase has a hydrophobic binding pocket for geranylgeranyl diphosphate, the lipid donor molecule. All Geranylgeranyltransferase substrates invariably have a cysteine as their fourth-to-last residue. This cysteine, coordinated by the zinc, engages in an SN2 type attack on the geranylgeranyl diphosphate, displacing the diphosphate.[2][3]
^ abLane KT, Beese LS (April 2006). "Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I". J. Lipid Res. 47 (4): 681–99. doi:10.1194/jlr.R600002-JLR200. PMID 16477080.
^Reid TS, Terry KL, Casey PJ, Beese LS (October 2004). "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity". J. Mol. Biol. 343 (2): 417–33. doi:10.1016/j.jmb.2004.08.056. PMID 15451670.
^Long SB, Casey PJ, Beese LS (October 2002). "Reaction path of protein farnesyltransferase at atomic resolution". Nature. 419 (6907): 645–50. Bibcode:2002Natur.419..645L. doi:10.1038/nature00986. PMID 12374986. S2CID 4412580.
Further reading
Eastman RT, Buckner FS, Yokoyama K, Gelb MH, Van Voorhis WC (February 2006). "Thematic review series: lipid posttranslational modifications. Fighting parasitic disease by blocking protein farnesylation". J. Lipid Res. 47 (2): 233–40. doi:10.1194/jlr.R500016-JLR200. PMID 16339110.
El Oualid F, Cohen LH, van der Marel GA, Overhand M (2006). "Inhibitors of protein: geranylgeranyl transferases". Curr. Med. Chem. 13 (20): 2385–427. doi:10.2174/092986706777935078. PMID 16918362.
April 03, 2023
geranylgeranyltransferase, type, geranylgeranyltransferase, used, refer, either, geranylgeranyltransferase, simply, geranylgeranyltransferase, three, enzymes, prenyltransferase, group, specific, terms, geranylgeranyltransferase, ggtase, adds, carbon, isoprenoi. Geranylgeranyltransferase may be used to refer to either Geranylgeranyltransferase type 1 or Rab geranylgeranyltransferase Geranylgeranyltransferase type 1 or simply geranylgeranyltransferase is one of the three enzymes in the prenyltransferase group In specific terms Geranylgeranyltransferase GGTase 1 adds a 20 carbon isoprenoid called a geranylgeranyl group to proteins bearing a CaaX motif a four amino acid sequence at the carboxyl terminal of a protein Geranylgeranyltransferase inhibitors are being investigated as anti cancer agents 1 protein geranylgeranyltransferase type IIdentifiersEC no 2 5 1 59CAS no 135371 29 8DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteinsGGTase 1 a subunit farnesyltransferase CAAX box IdentifiersSymbolFNTANCBI gene2339HGNC3782OMIM134635PDB1S64RefSeqNM 002027UniProtP49354Other dataEC number2 5 1 59LocusChr 8 p11 21Search forStructuresSwiss modelDomainsInterProGGTase 1 b subunit protein geranylgeranyl transferase type I b subunit IdentifiersSymbolPGGT1BNCBI gene5229HGNC8895OMIM602031PDB1S64RefSeqNM 005023UniProtP53609Other dataEC number2 5 1 59LocusChr 5 q23 1Search forStructuresSwiss modelDomainsInterPro Contents 1 Function 2 Structure 3 See also 4 References 5 Further readingFunction EditPrenyltransferases including geranylgeranyltransferase posttranslationally modify proteins by adding an isoprenoid lipid called a prenyl group to the carboxyl terminus of the target protein This process called prenylation causes prenylated proteins to become membrane associated due to the hydrophobic nature of the prenyl group Most prenylated proteins are involved in cellular signaling wherein membrane association is critical for function 1 Structure EditGeranylgeranyltransferase contains two subunits a and b that are encoded by the FNTA and PGGT1B genes respectively Both subunits are composed primarily of alpha helices Geranylgeranyltransferase coordinates a zinc cation on its b subunit at the lip of the active site Geranylgeranyltransferase has a hydrophobic binding pocket for geranylgeranyl diphosphate the lipid donor molecule All Geranylgeranyltransferase substrates invariably have a cysteine as their fourth to last residue This cysteine coordinated by the zinc engages in an SN2 type attack on the geranylgeranyl diphosphate displacing the diphosphate 2 3 See also EditFarnesyltransferase Prenylation Rab geranylgeranyltransferase Geranylgeranyltransferase type 2References Edit a b Lane KT Beese LS April 2006 Thematic review series lipid posttranslational modifications Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I J Lipid Res 47 4 681 99 doi 10 1194 jlr R600002 JLR200 PMID 16477080 Reid TS Terry KL Casey PJ Beese LS October 2004 Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity J Mol Biol 343 2 417 33 doi 10 1016 j jmb 2004 08 056 PMID 15451670 Long SB Casey PJ Beese LS October 2002 Reaction path of protein farnesyltransferase at atomic resolution Nature 419 6907 645 50 Bibcode 2002Natur 419 645L doi 10 1038 nature00986 PMID 12374986 S2CID 4412580 Further reading EditEastman RT Buckner FS Yokoyama K Gelb MH Van Voorhis WC February 2006 Thematic review series lipid posttranslational modifications Fighting parasitic disease by blocking protein farnesylation J Lipid Res 47 2 233 40 doi 10 1194 jlr R500016 JLR200 PMID 16339110 El Oualid F Cohen LH van der Marel GA Overhand M 2006 Inhibitors of protein geranylgeranyl transferases Curr Med Chem 13 20 2385 427 doi 10 2174 092986706777935078 PMID 16918362 Retrieved from https en wikipedia org w index php title Geranylgeranyltransferase type 1 amp oldid 1116534485, wikipedia, wiki, book, books, library,
