Overview for MACiE Entry M0253
EC Number: 184.108.40.206 (A member of the Transferases, Transferring alkyl or aryl groups, other than methyl groups, Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date))
Enzyme Name: geranyltranstransferase
Biological Species: Gallus gallus (Chicken)
Catalytic Chain UniprotKB Accession Codes:
- P22939 - Farnesyl diphosphate synthase
Representative PDB Code: 1uby - STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE (Resolution = 2.40 Å).
Catalytic CATH Codes:
Display structure information
Overall Comment: This enzyme is annotated as catalysing the reactions for both EC 220.127.116.11 and 18.104.22.168. It is known that the residue at the fifth position before the first DDxxD motif , in this case Phe112 (Phe240 in E. coli) is responsible for determining product chain length. It has also been shown for the avian enzyme that Phe113 also helps to determine product chain length. It is not clear if any other active site amino acid residues are involved in the catalysis of the Avian enzyme. However, in the E. coli enzyme, which utilises a three metal mechanism and performs the elongation with cis- stereochemistry, rather than two metal trans- stereochemistry, the main chain carbonyl of Lys202 (Lys214 in avian protein) and side chain oxygens of Thr203 and Gln241 form the carbocation binding (and stabilisation) site .
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Stepwise Description of the Reaction
|Step 1||The substrate undergoes heterolysis. The diphosphate product remains associated with the active site, and the cabocation is delocalised over the three terminal carbon atoms of the intermediate.|
|Step 2||The double bond of isopentenyl diphosphate adds to the terminal carbocation in an electrophilic addition.|
|Step 3||The diphosphate formed in the initial heterolysis deprotonates the carbon adjacent to the newly formed carbocation, forming a new double bond in the trans,trans-farnesyl diphosphate product.|
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Catalytic Residues Involved
||Location of Function
Metal Cofactors for M0253
||No Available PDB Information
- P.-H. Liang et al. (2002), Eur. J. Biochem., 269, 3339-3354. Structure, mechanism and function of prenyltransferases.
- D. J. Hosfield et al. (2004), J. Biol. Chem., 279, 8526-8529. Structural Basis for Bisphosphonate-mediated Inhibition of Isoprenoid Biosynthesis.
- L. C. Tarshis et al. (1996), Proc. Natl Acad. Sci. USA, 93, 15018-15023. Regulation of product chain length by isoprenyl diphosphate synthases.
Homologue information for M0253 (1uby)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
Entries with at least one Catalytic CATH code in common (different mechanisms):
|M0264 ||squalene synthase |
|M0262 ||trichodiene synthase |
|M0089 ||pentalenene synthase |
|M0261 ||aristolochene synthase |
|M0265 ||aristolochene synthase |
|M0259 ||bornyl diphosphate synthase |
View a comparison of the other reactions in MACiE with the CATH domain 1.10.600.10
Links to this entry in other databases