EC number:2.5.1.58

Enzyme

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     2. Transferases
        2.5 Transferring alkyl or aryl groups, other than methyl groups
            2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
ID:2.5.1.58
Description:Protein farnesyltransferase.
Alternative Name: FTase.
CAAX farnesyltransferase.
Prosite: PDOC00703;
PDB:
PDBScop
3E37 8029795; 8042174; 8029794; 8042173;
2IEJ 8029795; 8042174; 8029794; 8042173;
2H6G 8029795; 8042174; 8029794; 8042173;
1MZC 8029795; 8042174; 8029794; 8042173;
1LD8 8029795; 8042174; 8029794; 8042173;
 » show all
Cath: 3.80.10.10; 1.25.40.120; 1.50.10.20; 2.60.40.1130;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.5.1.58
BRENDA Enzyme Link: BRENDA 2.5.1.58
KEGG Enzyme Link: KEGG2.5.1.58
BioCyc Enzyme Link: BioCyc 2.5.1.58
ExPASy Enzyme Link: ExPASy2.5.1.58
EC2PDB Enzyme Link: EC2PDB 2.5.1.58
ExplorEnz Enzyme Link: ExplorEnz 2.5.1.58
PRIAM enzyme-specific profiles Link: PRIAM 2.5.1.58
IntEnz Enzyme Link: IntEnz 2.5.1.58
MEDLINE Enzyme Link: MEDLINE 2.5.1.58

EC number:2.5.1.58

MSA:

2.5.1.58;
Phylogenetic Tree:

2.5.1.58;
Uniprot:
M-CSA:
RHEA:13345 (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-farnesyl-L-cysteinyl-[protein]
RULE(radius=1) [*:1]-[CH2;+0:2]-[O;H0;+0:3]-[*:4].[*:5]-[SH;+0:6]>>[*:1]-[CH2;+0:2]-[S;H0;+0:6]-[*:5].[*:4]-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.Long SB, Casey PJ, Beese LS1998 Jul 79657673
Protein prenyltransferases.Casey PJ, Seabra MC1996 Mar 88621375
Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release.Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ1995 May 237756316
Reaction path of protein farnesyltransferase at atomic resolution.Long SB, Casey PJ, Beese LS2002 Oct 1012374986
Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups.Micali E, Chehade KA, Isaacs RJ, Andres DA, Spielmann HP2001 Oct 1611591144