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Information on EC 2.5.1.58 - protein farnesyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q04631
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2.5.1.58 protein farnesyltransferaseIUBMB Comments
This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
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Word Map
- 2.5.1.58
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farnesylation
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prenylation
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geranylgeranylation
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isoprenoids
- beta-subunits
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isoprenylation
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15-carbon
- lamins
- manumycin
-
geranylgeranyltransferase-i
-
farnesyl-protein
- h-ras
- medicine
-
peptidomimetic
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prelamin
- ggtase-i
-
p21ras
- tetrapeptide
- farnesol
- tetrahydroquinoline
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ras-dependent
- pharmacology
-
progerin
-
3hmevalonate
-
ras-induced
- lovastatin
- tipifarnib
- drug development
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ras-mediated
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ras-transformed
- lonafarnib
-
hutchinson-gilford
-
dimethylallyl
- geranylgeraniol
- isoprene
- analysis
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
protein farnesyltransferase, fptase, farnesyl protein transferase, pftase, prenyl transferase, protein farnesyl transferase, ras farnesyltransferase, protein prenyltransferase, caax farnesyltransferase, hftase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAAX farnesyltransferase
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farnesyl protein transferase
farnesyltransferase
farnesyltransferase, farnesyl pyrophosphate-protein
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farnesyltransferase, protein
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FPT
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-
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fptase
FTase
PFT
PFTase
prenylprotein transferase
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prenyltransferase
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protein cysteine farnesyltransferase
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protein farnesyltransferase
protein prenyltransferase
RAS farnesyltransferase
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farnesyl protein transferase
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farnesyltransferase
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fptase
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FTase
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PFT
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-
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protein farnesyltransferase
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protein prenyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
kinetic mechanism
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farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
enzyme constitutes the protein prenyltransferase family of enzymes
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farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
farnesyl diphosphate binds exclusively to the beta subunit
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farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
farnesyl diphosphate binds the enzyme in a two step process that may involve an enzyme conformational change, the enzyme-substrate complex then rapidly reacts with the peptide substrate to form a product, and product release is the rate-limiting step in catalysis
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farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
both subunits would appear to have a role in binding and orienting the leaving group of farnesyl diphosphate approximately for catalysis
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
farnesyl-diphosphate:protein-cysteine farnesyltransferase
This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
CAS REGISTRY NUMBER
COMMENTARY
131384-38-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + K Ras-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [H Ras]-L-cysteine
S-(2E,6E)-farnesyl-[H Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [K Ras]-L-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [N Ras]-L-cysteine
S-(2E,6E)-farnesyl-[N Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(2,3,5,6-tetrafluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2,3,5,6-tetrafluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(phenylsulfanyl)octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-(phenylsulfanyl)octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CCIQ
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CGGDD
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CSVL
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CTIQ
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CVIS
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CVLL
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate + CVLS
?
-
-
-
?
(2E,6E)-3,7-dimethyl-8-phenoxyocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-phenoxyocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[(2-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[(2-methylphenyl)amino]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[(3,4,5-trimethoxybenzyl)oxy]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[(3,4,5-trimethoxybenzyl)oxy]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[(3-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[(3-methylphenyl)amino]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[(4-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[(4-methylphenyl)amino]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[(4-nitrophenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[(4-nitrophenyl)amino]octa-2,6-dien-1-y)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[3-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[3-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethyl)phenoxy]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[4-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[4-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[4-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[4-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[[2-(trifluoromethyl)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[[2-(trifluoromethyl)phenyl]amino]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[[3-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[[3-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-8-[[4-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-8-[[4-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-3,7-dimethyl-9-phenylnona-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-3,7-dimethyl-9-phenylnona-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(2,3-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2,3-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(2,6-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2,6-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(2-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(2-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(2-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yll)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(2-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(2-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3,4-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3,4-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3,4-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3,4-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3,5-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3,5-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3,5-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3,5-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yll)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(3-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(3-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-benzylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-benzylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yll)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(4-nitrophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(4-nitrophenoxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(benzyloxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(benzyloxy)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-(isoxazol-3-ylamino)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-(isoxazol-3-ylamino)-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(2-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(2-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(2-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(2-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(2-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(2-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(3-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(3-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(3-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(3-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(3-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(3-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(3-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(3-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(3-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(3-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(3-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(3-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(4-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(4-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(4-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(4-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(4-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(4-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(4-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(4-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[(4-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[(4-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[3-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[3-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-8-[4-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-8-[4-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + (protein)-L-cysteine
S-(2E,6E)-farnesyl protein + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CCIQ
S-(2E,6E)-farnesyl-CCIQ + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CGGDD
S-(2E,6E)-farnesyl-CGGDD + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CSVL
S-(2E,6E)-farnesyl-CSVL + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CTIQ
S-(2E,6E)-farnesyl-CTIQ + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CVIS
S-(2E,6E)-farnesyl-CVIS + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CVLL
S-(2E,6E)-farnesyl-CVLL + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + CVLS
S-(2E,6E)-farnesyl-CVLS + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + dansyl-CGVLS
dansyl-G-(S-(2E,6E)-farnesyl)CVLS
-
assay at pH 7.5, 37°C
-
-
?
(2E,6E)-farnesyl diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-farnesyl)CVLS + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + [H Ras]-L-cysteine
S-(2E,6E)-farnesyl-[H Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [K Ras]-L-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [N Ras]-L-cysteine
S-(2E,6E)-farnesyl-[N Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CCIQ
?
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CGGDD
?
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CSVL
?
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CTIQ
?
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CVIS
?
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CVLL
?
-
-
-
?
(2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate + CVLS
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CCIQ
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CGGDD
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CSVL
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CTIQ
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CVIS
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CVLL
?
-
-
-
?
(2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate + CVLS
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CCIQ
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CGGDD
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CSVL
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CTIQ
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CVIS
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CVLL
?
-
-
-
?
(2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate + CVLS
?
-
-
-
?
10-benzyloxy-3-methyl-2-decen-1-ol-diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-(10-benzyloxy-3-methyl-2-decenyl)-Cys-Val-Leu-Ser
-
-
-
-
?
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate + dansyl-Gly-Cys-Lys-Thr-Gln
? + diphosphate
-
-
-
-
?
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate + dansyl-Gly-Cys-Lys-Val-Leu
? + diphosphate
-
-
-
-
?
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate + dansyl-Gly-Cys-Val-Ile-Met
? + diphosphate
-
-
-
-
?
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate + dansyl-Gly-Cys-Val-Leu-Ser
? + diphosphate
-
-
-
-
?
6-benzyloxy-3-methyl-2-hexen-1-ol-diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-(6-benzyloxy-3-methyl-2-hexenyl)-Cys-Val-Leu-Ser
-
-
-
-
?
7-benzyloxy-3-methyl-2-hepten-1-ol-diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-(7-benzyloxy-3-methyl-2-heptenyl)-Cys-Val-Leu-Ser
-
-
-
-
?
8-benzyloxy-3-methyl-2-octen-1-ol-diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-(8-benzyloxy-3-methyl-2-octenyl)-Cys-Val-Leu-Ser
-
-
-
-
?
9-benzyloxy-3-methyl-2-nonen-1-ol-diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-(9-benzyloxy-3-methyl-2-nonenyl)-Cys-Val-Leu-Ser
-
-
-
-
?
CALQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CALQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CALV + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CALV + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CAVQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CAVQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CCIF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CCIF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CCIL + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CCIL + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CDVK + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CDVK + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CEIQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CEIQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CFLS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CFLS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CFPS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CFPS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CFTN + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CFTN + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CFVN + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CFVN + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CGIA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CGIA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CGIM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CGIM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CGLF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CGLF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CGLY + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CGLY + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CGVV + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CGVV + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CHIM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CHIM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CHIQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CHIQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CHLM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CHLM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CHLS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CHLS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CHVM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CHVM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CHVQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CHVQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CIVA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CIVA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CKIF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CKIF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CKIS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CKIS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CKIV + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CKIV + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CLIT + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CLIT + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CLLM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CLLM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CLLV + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CLLV + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CLML + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CLML + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CLTS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CLTS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CLVM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CLVM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CNIM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CNIM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CNLF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CNLF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CNLK + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CNLK + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CNLM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CNLM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CNLQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CNLQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CQTA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CQTA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CRIS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CRIS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSFM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSFM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSIM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSIM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSIS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSIS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSLA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSLA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSLC + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSLC + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSLG + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSLG + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSLH + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSLH + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSLM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSLM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSVQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSVQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CSVS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CSVS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTII + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTII + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTIV + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTIV + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTKF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTKF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTLA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTLA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTLM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTLM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTLQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTLQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTMS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTMS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTTQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTTQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTVF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTVF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTVS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTVS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CTVV + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CTVV + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CVHF + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CVHF + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CVLA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CVLA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CVLH + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CVLH + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CVLQ + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CVLQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CVQM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CVQM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CVVT + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CVVT + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CYIS + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CYIS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CYLA + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CYLA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CYPD + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CYPD + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
CYVM + (2E,6E)-farnesyl diphosphate
S-(2E,6E)-farnesyl-CYVM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVAA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVAA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVAM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVAM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVAQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVAQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVAS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVAS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVCA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVCA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVCM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVCM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVCQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVCQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVCS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVCS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVDA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVDA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVDM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVDM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVDQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVDQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVDS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVDS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVEA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVEA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVEM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVEM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVEQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVEQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVES + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVES + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVFA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVFA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVFM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVFM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVFQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVFQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVFS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVFS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVGA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVGA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVGM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVGM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVGQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVGQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVGS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVGS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVHA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVHA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVHM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVHM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVHQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVHQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVHS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVHS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVIA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVIA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVIM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVIM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVIQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVIQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVIS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVIS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVKA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVKA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVKLQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVLQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVKM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVKM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVKQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVKQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVKS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVKS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVLA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVLA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVLM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVLM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVLS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVLS + diphosphate
dansyl-GCVLS + (E)-[4-[(3,7-dimethylocta-2,6-dien-1-yl)oxy]phenyl]-methanyl diphosphate
dansyl-G-(S-(E)-[4-[(3,7-dimethylocta-2,6-dien-1-yl)oxy]phenyl]-methanyl)CVLS + diphosphate
-
-
-
-
?
dansyl-GCVLS + [3-[(3-phenoxyphenoxy)methyl]phenyl]-methanyl diphosphate
dansyl-G-(S-[3-[(3-phenoxyphenoxy)methyl]phenyl]-methanyl)CVLS + diphosphate
-
-
-
-
?
dansyl-GCVMA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVMA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVMM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVMM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVMQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVMQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVMS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVMS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVNA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVNA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVNM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVNM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVNQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVNQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVNS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVNS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVPA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVPA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVPM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVPM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVPQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVPQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVPS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVPS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVQA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVQA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVQM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVQM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVQQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVQQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVQs + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVQS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVSA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVSA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVSM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVSM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVSQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVSQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVSS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVSS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVTA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVTA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVTM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVTM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVTQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVTQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVTS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVTS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVVA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVVA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVVM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVVM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVVQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVVQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVVS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVVS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVWA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVWA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVWM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVWM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVWQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVWQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVWS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVWS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVYA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVYA + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVYM + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVYM + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVYQ + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVYQ + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
dansyl-GCVYS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVYS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
farnesyl diphosphate + biotin-YRASNRSCAIM
diphosphate + biotin-YRASNRS-(S-farnesyl)CAIM
-
-
-
-
?
farnesyl diphosphate + dansyl-GCEV
diphosphate + farnesyl dansyl-GCEV
-
-
-
?
farnesyl diphosphate + dansyl-GCFT
diphosphate + farnesyl dansyl-GCFT
-
-
-
?
farnesyl diphosphate + dansyl-GCII
diphosphate + farnesyl dansyl-GCII
-
-
-
?
farnesyl diphosphate + dansyl-GCLL
diphosphate + farnesyl dansyl-GCLL
-
-
-
?
farnesyl diphosphate + dansyl-GCNV
diphosphate + farnesyl dansyl-GCNV
-
-
-
?
farnesyl diphosphate + dansyl-GCQL
diphosphate + farnesyl dansyl-GCQL
-
-
-
?
farnesyl diphosphate + dansyl-GCRL
diphosphate + farnesyl dansyl-GCRL
-
-
-
?
farnesyl diphosphate + dansyl-GCSV
diphosphate + farnesyl dansyl-GCSV
-
-
-
?
farnesyl diphosphate + dansyl-GCTV
diphosphate + farnesyl dansyl-GCTV
-
-
-
?
farnesyl diphosphate + dansyl-GCVL
diphosphate + farnesyl dansyl-GCVL
-
-
-
?
farnesyl diphosphate + dansyl-GCVLS
diphosphate + S-farnesyl dansyl-GCVLS
-
-
-
?
farnesyl diphosphate + dansyl-GCWI
diphosphate + farnesyl dansyl-GCWI
-
-
-
?
farnesyl diphosphate + dansyl-GCYL
diphosphate + farnesyl dansyl-GCYL
-
-
-
?
farnesyl diphosphate + dansyl-Gly-Cys-Lys-Thr-Gln
dansyl-Gly-S-farnesyl-Cys-Lys-Thr-Gln + diphosphate
-
-
-
-
?
farnesyl diphosphate + dansyl-Gly-Cys-Lys-Val-Leu
dansyl-Gly-S-farnesyl-Cys-Lys-Val-Leu + diphosphate
-
-
-
-
?
farnesyl diphosphate + dansyl-Gly-Cys-Val-Ile-Met
dansyl-Gly-S-farnesyl-Cys-Val-Ile-Met + diphosphate
-
-
-
-
?
farnesyl diphosphate + dansyl-Gly-Cys-Val-Leu-Ser
dansyl-Gly-S-farnesyl-Cys-Val-Leu-Ser + diphosphate
-
-
-
-
?
farnesyl diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-farnesyl-Cys-Val-Leu-Ser
-
the best substrate
-
-
?
farnesyl diphosphate + [protein]-L-cysteine
[protein]-S-((2E,6E)-farnesyl)-L-cysteine + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
farnesyl monophosphate + Gly-Cys-Val-Leu-Ser
phosphate + Gly-S-farnesyl-Cys-Val-Leu-Ser
-
-
-
-
?
geranyl diphosphate + dansyl-GCVLS
dansyl-G-(S-geranyl)CVLS + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + N-dansyl-Gly-Cys-Val-Leu-Ser
diphosphate + N-dansyl-Gly-S-geranylgeranyl-Cys-Val-Leu-Ser
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
diphosphate + S-geranylgeranylcysteinyl protein
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
dansyl-GCVLS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVLS + diphosphate
-
-
-
-
?
dansyl-GCVLS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVLS + diphosphate
-
assay at pH 7.8, 25°C
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
Ha-Ras-CVLS, which is a good substrate for mammalian enzyme, not farnesylated by the parasite enzyme, only the mammalian enzyme substrate RAS1-CVIM farnesylated by parasite enzyme
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
substrate are: Ras superfamiliy and Ras-related proteins for example Rap, Rab, Rac and Ral, large G proteins, nuclear lamins, rhodopsin kinase and the retinal cGMP phosphodiesterase
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
substrate are: Ras superfamiliy and Ras-related proteins for example Rap, Rab, Rac and Ral, large G proteins, nuclear lamins, rhodopsin kinase and the retinal cGMP phosphodiesterase
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
enzyme prefers linear residues in the X position of the CaaX box over branched residues, enzyme prefers Gln, Met and Ser at the X position
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
substrates are cellular proteins such as Ras at a cysteine residue near their carboxy-terminus
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F
-
ir
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
preferred CaaX-substrate: CAIM
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
process necessary for the subcellular localisation of substrate to the plasma membrane
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
enzyme responsible for catalysing isoprene lipid modifications
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
A series of steps modifies the C-terminus of Ras. Enzyme catalyses the first of these steps by transferring the farnesyl group from farnesyl diphosphates to the cysteine side chain in the CAAX sequence motif at the C-terminus of Ras
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
catalyzes the post-translational modification of many important cellular proteins
-
-
?
farnesyl diphosphate + Ras-Cys-Val-Ile-Met
diphosphate + Ras-S-farnesyl-Cys-Val-Ile-Met
-
-
-
-
?
farnesyl diphosphate + Ras-Cys-Val-Ile-Met
diphosphate + Ras-S-farnesyl-Cys-Val-Ile-Met
-
best substrate
-
-
?
additional information
?
-
ligand interaction analysis with FTase alpha subunit, mass spectrometry, overview. The enzyme alpha-subunit interacts with Vps4A protein in vitro and in vivo
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
-
although farnesyl diphosphate and geranylgeranyl diphosphate bind competitively, the geranyl geranyl diphosphate is not transferred efficiently to the protein substrate by enzyme
-
-
?
additional information
?
-
-
steady-state kinetics for modification of peptide substrates shows that the multiple-turnover activity depends on the analogue structure. Analogues in which the first isoprene is replaced with a benzyl group and an analogue in which each isoprene is replaced with an aryl group are good substrates. The single-turnover rate constant for alkylation depends on the Ca1a2X peptide sequence. The isoprenoid transition-state conformation is preferred over the inactive E-FPP-Ca1a2X ternary complex conformation and the farnesyl binding site in the exit groove may be significantly more selective for the farnesyl diphosphate substrate than the active site binding pocket
-
-
?
additional information
?
-
analogues of farnesyl diphosphate alter CaaX substrate specificity and reactions rates of protein farnesyltransferase, reactivity of four alkyne-containing analogs of farnesyl diphosphate with purified protein farnesyltransferase and a small library of dansylated peptides using an in vitro continuous spectrofluorimetric assay, overview. Activity with CGGDD, CVLL, and CSVL peptides is low with farnesyl diphosphate as well as with its analogues
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
FTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 15-carbon isoprenoid geranylgeranyl from its donor farnesyldiphosphate (FPP) is specific to FTase-I. Residues Lysalpha164, Hisbeta248, Argbeta291 and Tyrbeta300 in FTase can form hydrogen bonds with farnesyl diphosphate. When FTase is inhibited by a FTI, N-Ras and K-Ras can be alternatively prenylated by GGTase-I, EC 2.5.1.59, but H-Ras cannot
-
-
?
additional information
?
-
protein farnesytransferase catalyzes the farnesylation of proteins with a C-terminal tetrapeptide sequence denoted as a Ca1a2X box, determination of substrate recognition sequences, and substrate specificity, screening of the CVa2X library with alkyne-functionalized isoprenoid substrates, detailed overview
-
-
?
additional information
?
-
-
protein farnesytransferase catalyzes the farnesylation of proteins with a C-terminal tetrapeptide sequence denoted as a Ca1a2X box, determination of substrate recognition sequences, and substrate specificity, screening of the CVa2X library with alkyne-functionalized isoprenoid substrates, detailed overview
-
-
?
additional information
?
-
enzyme prefers farnesyl diphosphate over geranylgeranyl diphosphate, but catalyzes the reactions of both substrates, i.e. reactions of EC 2.5.1.58 and EC 2.5.1.59, respectively
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + [H Ras]-L-cysteine
S-(2E,6E)-farnesyl-[H Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [K Ras]-L-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [N Ras]-L-cysteine
S-(2E,6E)-farnesyl-[N Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + (protein)-L-cysteine
S-(2E,6E)-farnesyl protein + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [H Ras]-L-cysteine
S-(2E,6E)-farnesyl-[H Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [K Ras]-L-cysteine
S-(2E,6E)-farnesyl-[K Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [N Ras]-L-cysteine
S-(2E,6E)-farnesyl-[N Ras]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
additional information
?
-
ligand interaction analysis with FTase alpha subunit, mass spectrometry, overview. The enzyme alpha-subunit interacts with Vps4A protein in vitro and in vivo
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + [protein]-L-cysteine
S-(2E,6E)-farnesyl-[protein]-L-cysteine + diphosphate
-
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
process required for the transforming activity of oncogenic variants of Ras, making enzyme a prime target for anticancer therapeutics
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
process necessary for the subcellular localisation of substrate to the plasma membrane
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
enzyme responsible for catalysing isoprene lipid modifications
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
A series of steps modifies the C-terminus of Ras. Enzyme catalyses the first of these steps by transferring the farnesyl group from farnesyl diphosphates to the cysteine side chain in the CAAX sequence motif at the C-terminus of Ras
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
catalyzes the post-translational modification of many important cellular proteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the addition of Mg2+ ions causes a conformational change in the enzyme's active site, breaking interactions known to keep farnesyl diphosphate in its inactive conformation. Wild-type protein shows relevant Mg2+ ion binding motifs. In the first binding motif, WT1, the Mg2+ ion is coordinated to D352 of beta-subunit, zinc-bound D297 of beta-subunit, two water molecules, and one oxygen atom from the alpha- and beta-phosphates of farnesyl diphosphate. The second binding motif, WT2, is identical with the exception of the zinc-bound D297 of beta-subunit being replaced by a water molecule in the Mg2+ coordination complex. In both motifs, a key hydrogen bond between a magnesium bound water and Cys1p bridges the two metallic binding sites, and thereby reduces the equilibrium distance between the reacting atoms of farnesyl diphosphate and protein-cysteine Cys1p. The free energy profiles calculated for these systems demonstrate that the two reactive atoms approach each other more readily in the presence of Mg2+. The flexible WT2 model has the lowest barrier towards the conformational change, suggesting it is the prefered Mg2+ binding motif
Cd2+
-
substitution of the active site zinc with cadmium increases the affinity of the peptide substrate and decreases the rate constant for the chemical step
Co2+
Mg2+
Mn2+
-
in wild type FTase, Mg2+ can be replaced by Mn2+ with a 2-fold lower KMn2+ 2 mM
Zn2+
additional information
Co2+
-
evidence for a catalytically relevant interaction between the metal ion and the protein substrate in the enzyme
Mg2+
-
the magnesium affinity of enzyme increases with pH with a pka of 7.4, presumably reflecting the deprotonation of the farnesyl diphosphate to enhance magnesium coordination
Mg2+
-
magnesium is not required for formation of the thioether product but the presence increases the single-turnover rate constant by several orders of magnitude at saturating enzyme and substrate concentrations
Mg2+
-
appears to coordinate the diphosphate moiety of farnesyl diphosphate
Mg2+
-
enhances activity several hundred-fold, with a Km(Mg2+) value of 4 mM. Mg2+ coordinates the side chain carboxylate of Asp-beta352 and that the role of magnesium in the reaction includes positioning the FPP prior to catalysis. Mg2+ may accelerate catalysis both by stabilizing developing negative charge in the transition state and by stabilizing the active site conformation prior to catalysis
Zn2+
-
zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule
Zn2+
-
zinc plays a major catalytic role in the mechanism of enzyme, zinc seems to activate the cysteine thiol of protein substrate for attack at C-1 of the isoprenoid substrate
Zn2+
-
the zinc ion activates the cysteine thiolate for nucleophilic attack on the C1 atom of the farnesyl diphosphate substrate
Zn2+
-
there is no significant change in Zn-ligand distances when a substrate binds, demonstrating that the Zn remains four-coordinate. Structural characterization of the zinc site
Zn2+
-
FTase is a zinc metalloenzyme with a Zn2+ ion ligated to a histidine, cysteine and aspartate
Zn2+
required, binding and coordination structure, coordinated by residues Aspbeta297, Cysbeta299 and Hisbeta362 in FTase , overview
additional information
-
a metal-assisted nucleophile is involved in the catalytic mechanism of enzyme
additional information
-
a metal-assisted nucleophile is involved in the catalytic mechanism of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methylpropyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N-ethylpiperidine-1-carboxamide
-
ethyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
methyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
N-(1-bromoethenyl)-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-benzyl-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-(pyridin-2-ylsulfonyl)glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-(pyridin-3-ylsulfonyl)glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-(pyridin-4-ylsulfonyl)glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-[(1-methyl-1H-imidazol-2-yl)sulfonyl]glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-[(4-fluorophenyl)sulfonyl]glycinamide
-
N-[(1-acetylpiperidin-4-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[(1-bromonaphthalen-2-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-[(1-bromonaphthalen-2-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[(1-butanoylpiperidin-4-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[(6-chloro-2,1,3-benzothiadiazol-5-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[1-(tert-butylamino)ethenyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-(1-methylethenyl)-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-(2-methylbenzyl)-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-(thiophen-3-ylmethyl)-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(pyridin-2-ylmethyl)pyridine-2-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(5-methyl-3-phenylisoxazol-4-yl)methyl]pyridine-2-sulfonamide
-
tert-butyl 4-[([6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl][(1-methyl-1H-imidazol-4-yl)sulfonyl]amino)methyl]piperidine-1-carboxylate
-
tert-butyl N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(1-methyl-1H-imidazol-4-yl)sulfonyl]glycinate
-
(1R,4aR,5R,7S)-5-[[(1R,4aR,8aS)-8a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-6-methoxy-5,8-dioxo-1,4,4a,5,8,8a-hexahydronaphthalen-1-yl]methyl]-7-hydroxy-1,4a-dimethyl-6-methylidenedecahydronaphthalene-1-carbaldehyde
-
-
(1R,4aR,5R,7S)-5-[[(1R,4aR,8aS)-8a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-6-methoxy-5,8-dioxo-1,4,4a,5,8,8a-hexahydronaphthalen-1-yl]methyl]-7-hydroxy-1,4a-dimethyl-6-methylidenedecahydronaphthalene-1-carboxylic acid
-
-
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-2-methoxy-5-[[(1S,3S,7S,8aS)-1,3,7-trihydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-2-methoxy-6-methyl-5-[[(1R,8aS)-5,5,8a-trimethyl-2-methylidene-3-oxodecahydronaphthalen-1-yl]methyl]-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,3S,5R,8aS)-3-hydroxy-5-(hydroxymethyl)-5,8a-dimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,3S,7S,8aS)-3,7-dihydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(4aS,5R,8aR)-4a-(5-hydroxy-7-methoxy-4-oxo-4H-chromen-2-yl)-2-methoxy-6-methyl-5-[[(1R,8aS)-5,5,8a-trimethyl-2-methylidene-3-oxodecahydronaphthalen-1-yl]methyl]-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(4aS,5S,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,2R,7S,8aS)-2,7-dihydroxy-2,5,5,8a-tetramethyldecahydronaphthalen-1-yl]methyl]-6-hydroxy-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
-
-
(S)-N-(4-(3,4-dichlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
-
dual inhibitor for both farnesyl transferase and geranygeranyltransferase-I. Compound occupies both isoprenoid and peptide substrate binding sites
(S)-N-(4-(3-chlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
-
dual inhibitor for both farnesyl transferase and geranygeranyltransferase-I
1,4,8,10-tetrahydroxy-6-[(1E)-3-[(3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]-1-methylprop-1-en-1-yl]-5,6-dihydro-7H-benzo[c]xanthen-7-one
-
-
1-methyl-1H-imidazole-4-sulfonic acid [6-cyano-1-(3-methyl-3H-imidazol-4-yl-methyl)-1,2,3,4-tetrahydro-quinolin-3-yl]-(3-methoxy-propyl)-amide
-
-
1-methyl-N-[1-[(1-methyl-1H-imidazol-5-yl)methyl]-6-phenyl-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(5-methylisoxazol-4-yl)methyl]-1H-imidazole-4-sulfonamide
-
-
1-methylethyl 4-[([1-[(1-methyl-1H-imidazol-5-yl)methyl]-6-phenyl-1,2,3,4-tetrahydroquinolin-3-yl][(1-methyl-1H-imidazol-4-yl)sulfonyl]amino)methyl]piperidine-1-carboxylate
-
-
2-methylpropyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
-
farnesylation of dansyl-GCKVL, IC5=: 510 nM
4-(3-{[(4-cyano-3-naphthalen-1-yl-phenyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-methyl}-phenyl)-pyridine-2-carbonitrile
-
IC50: 0.37 nM, selective inhibitor
4-[(3'-Chloro-biphenyl-3-ylmethyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 0.45 nM, selective inhibitor
4-[(3-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 0.39 nM, selective inhibitor
4-[(3-Methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 31 nM
4-[(4-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 1.5 nM, selective inhibitor
4-[Biphenyl-3-ylmethyl-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 1.5 nM
4-[Hexyl-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 1.9 nM
4-[Methyl-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
-
IC50: 38 nM
4-[[[6-cyano-1-(3-methyl-3H-imidazol-4-ylmethyl)-1,2,3,4-tetrahydro-quinolin-3-yl]-(pyridine-2-sulfonyl)-amino]-methyl]-piperidine-1-carboxylic acid isobutyl ester
-
-
4-[[[6-cyano-1-(3-methyl-3H-imidazol-4-ylmethyl)-1,2,3,4-tetrahydro-quinolin-3-yl]-(pyridine-2-sulfonyl)-amino]-methyl]-piperidine-1-carboxylic acid methyl ester
-
-
4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N-ethylpiperidine-1-carboxamide
-
5,7-dihydroxy-2-[(5R)-1-hydroxy-5-[[(3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-6-methyl-4-oxo-1,5,8,8a-tetrahydronaphthalen-4a(4H)-yl]-4H-chromen-4-one
-
-
5,7-dihydroxy-2-[(5R)-1-hydroxy-5-[[(3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-6-methyl-2-oxo-1,5,8,8a-tetrahydronaphthalen-4a(2H)-yl]-4H-chromen-4-one
-
-
5-[(3-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2'-methyl-biphenyl-2-carbonitrile
-
IC50: 0.97 nM, selective inhibitor
5-[(4-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2'-methyl-biphenyl-2-carbonitrile
-
IC50: 10 nM, selective inhibitor
Biphenyl-3-carboxylic acid (4-cyano-3-naphthalen-1-yl-phenyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amide
-
IC50: 14 nM
Biphenyl-3-sulfonic acid (4-cyano-3-naphthalen-1-yl-phenyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amide
-
IC50: 18 nM
ethyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
-
ethyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
FTI-277
-
inhibition with potencies 10fold higher on parasite enzyme than on mammalian enzyme, however growth of bloodstream Trypanosoma brucei completely inhibited with 0.001 mM
GGTI-297
-
inhibition with potencies 10fold higher on parasite enzyme than on mammalian enzyme
GGTI-298
-
inhibition with potencies 10fold higher on parasite enzyme than on mammalian enzyme, however growth of bloodstream Trypanosoma brucei cmpletely inhibited with 0.005 mM
methyl 4-[([6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl][(1-methyl-1H-imidazol-4-yl)sulfonyl]amino)methyl]piperidine-1-carboxylate
-
85% inhibition at 0.005 mM
methyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
methyl 4-[[[6-cyano-1-[1-(1H-imidazol-5-yl)ethyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
69% inhibition at 50 nM
methyl N-(1-cysteinylpiperidin-4-yl)-N-(phenylcarbonyl)-L-methioninate
-
IC50: 22.8 nM
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-isoleucinate
-
IC50: 32.7 nM
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-methioninate
-
IC50: 4.6 nM
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-phenylalaninate
-
IC50: 22 nM
methyl N-(phenylcarbonyl)-N-{1-([1-[4-(trifluoromethyl)benzyl]-1H-imidazol-4-yl]methyl)piperidin-4-yl}-L-methioninate
-
IC50: 43.9 nM
methyl N-benzyl-N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-L-methioninate
-
IC50: 2.35 nM
methyl N-[1-[(1-benzyl-1H-imidazol-4-yl)methyl]piperidin-4-yl]-N-(phenylcarbonyl)-L-methioninate
-
IC50: 397 nM
N-(1-bromoethenyl)-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-benzyl-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-tert-butyl-N2-[6-cyano-1-(1-methyl-1H-imidazol-5-yl)-1,2,3,4-tetrahydroquinolin-3-yl]-N2-[(1-methyl-1H-imidazol-2-yl)sulfonyl]glycinamide
-
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-(pyridin-2-ylsulfonyl)glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-(pyridin-3-ylsulfonyl)glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-(pyridin-4-ylsulfonyl)glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-[(1-methyl-1H-imidazol-2-yl)sulfonyl]glycinamide
-
N-tert-butyl-N2-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N2-[(4-fluorophenyl)sulfonyl]glycinamide
-
N-[(1-acetylpiperidin-4-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[(1-bromonaphthalen-2-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-[(1-bromonaphthalen-2-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[(1-butanoylpiperidin-4-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl]pyridine-2-sulfonamide
-
-
N-[(1-butanoylpiperidin-4-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[(3-bromonaphthalen-2-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
-
N-[(6-chloro-2,1,3-benzothiadiazol-5-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
N-[1-(tert-butylamino)ethenyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
N-[1-[(1-methyl-1H-imidazol-5-yl)methyl]-6-phenyl-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
-
N-[6-bromo-1-[(1-methyl-1H-imidazol-5-yl)methyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
51% inhibition at 0.005 mM
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl]-N-[[1-(3,3-dimethylbutanoyl)piperidin-4-yl]methyl]pyridine-2-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl]-N-[[1-(phenylcarbonyl)piperidin-4-yl]methyl]pyridine-2-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-(1-methylethenyl)-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-(2-methylbenzyl)-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-(thiophen-3-ylmethyl)-1H-imidazole-4-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-[4-(1H-pyrazol-1-yl)benzyl]-1H-imidazole-4-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(2-fluorobenzyl)-1-methyl-1H-imidazole-4-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(pyridin-2-ylmethyl)pyridine-2-sulfonamide
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(4-phenyl-1,3-oxazol-5-yl)methyl]pyridine-2-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(5-methyl-3-phenylisoxazol-4-yl)methyl]pyridine-2-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[2-(1H-pyrrol-1-yl)ethyl]pyridine-2-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-1H-imidazole-4-sulfonamide
-
39% inhibition at 0.005 mM
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-[4-(methylsulfonyl)benzyl]-1H-imidazole-4-sulfonamide
-
47% inhibition at 0.005 mM
SCH-44342
-
2 orders of magnitude less potent on parasite enzyme than on mammalian enzyme
tert-butyl 4-[([6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl][(1-methyl-1H-imidazol-4-yl)sulfonyl]amino)methyl]piperidine-1-carboxylate
-
tert-butyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
-
69% inhibition at 50 nM
tert-butyl N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(1-methyl-1H-imidazol-4-yl)sulfonyl]glycinate
-
FTI-276
-
about 2fold more potent on parasite enzyme than on mammalian enzyme
N-[(6-chloro-2,1,3-benzothiadiazol-5-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
-
N-[(6-chloro-2,1,3-benzothiadiazol-5-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(pyridin-2-ylmethyl)pyridine-2-sulfonamide
-
-
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(pyridin-2-ylmethyl)pyridine-2-sulfonamide
-
additional information
-
two primary modes of inhibition: blocking the peptide substrate site and blocking the exit groove
-
additional information
-
hexapeptide containing a switch of leucine for methionine at the COOH terminus or a switch of cysteine for serine at the prenylation site is essentially inactive in competing for enzyme activity
-
additional information
-
enzyme inhibited by peptides containing the C-terminal CAAX sequence
-
additional information
-
tetrapeptides with sequence L-penicillamine-Val-Ile-X and Cys-Val-Phe-X
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
infection of Sf9 cells with the recombinant baculovirus containing DNA sequences encoding both enzyme activity results in a dramatic enhancement of enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0512
(2E,6E)-3,7-dimethyl-8-(2,3,5,6-tetrafluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.002
(2E,6E)-3,7-dimethyl-8-(phenylsulfanyl)octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.002
(2E,6E)-3,7-dimethyl-8-phenoxyocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.004
(2E,6E)-3,7-dimethyl-8-[(2-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.00017
(2E,6E)-3,7-dimethyl-8-[(3-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.004
(2E,6E)-3,7-dimethyl-8-[(4-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.015
(2E,6E)-3,7-dimethyl-8-[(4-nitrophenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0019
(2E,6E)-3,7-dimethyl-8-[3-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0003
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0011
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0214
(2E,6E)-3,7-dimethyl-8-[4-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0013
(2E,6E)-3,7-dimethyl-8-[4-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.01
(2E,6E)-3,7-dimethyl-8-[[2-(trifluoromethyl)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
value above, apparent Michaelis-Menten constant for peptide
0.0023
(2E,6E)-3,7-dimethyl-8-[[3-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0031
(2E,6E)-3,7-dimethyl-8-[[4-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0038
(2E,6E)-3,7-dimethyl-9-phenylnona-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0013
(2E,6E)-8-(2,3-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0165
(2E,6E)-8-(2,6-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0031
(2E,6E)-8-(2-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0025
(2E,6E)-8-(2-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0013
(2E,6E)-8-(2-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0032
(2E,6E)-8-(2-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0021
(2E,6E)-8-(3,4-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0007
(2E,6E)-8-(3,4-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0013
(2E,6E)-8-(3,5-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0005
(2E,6E)-8-(3,5-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.07
(2E,6E)-8-(3-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.00042
(2E,6E)-8-(3-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0021
(2E,6E)-8-(3-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0001
(2E,6E)-8-(3-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0004
(2E,6E)-8-(3-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0023
(2E,6E)-8-(4-benzylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0187
(2E,6E)-8-(4-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.033
(2E,6E)-8-(4-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0044
(2E,6E)-8-(4-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0045
(2E,6E)-8-(4-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0023
(2E,6E)-8-(4-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0063
(2E,6E)-8-(4-nitrophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.001
(2E,6E)-8-(benzyloxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0013
(2E,6E)-8-(isoxazol-3-ylamino)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.007
(2E,6E)-8-[(2-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0009
(2E,6E)-8-[(2-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0009
(2E,6E)-8-[(2-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.001
(2E,6E)-8-[(3-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.001
(2E,6E)-8-[(3-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0038
(2E,6E)-8-[(3-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.00034
(2E,6E)-8-[(3-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0009
(2E,6E)-8-[(3-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0043
(2E,6E)-8-[(3-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0017
(2E,6E)-8-[(4-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0102
(2E,6E)-8-[(4-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.00026
(2E,6E)-8-[(4-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0014
(2E,6E)-8-[(4-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.03
(2E,6E)-8-[(4-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.004
(2E,6E)-8-[3-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.008
(2E,6E)-8-[4-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0005
(E)-[4-[(3,7-dimethylocta-2,6-dien-1-yl)oxy]phenyl]-methanyl diphosphate
-
pH 7.8, 25°C
0.0015
[3-[(3-phenoxyphenoxy)methyl]phenyl]-methanyl diphosphate
-
pH 7.8, 25°C
0.0004
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate
-
apparent Michaelis-Menten constant for peptide, determined by continuous fluorescence assay
0.0005
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate
-
apparent Michaelis-Menten constant for peptide, determined by RP-HPLC product analysis
0.0008
(2E,6E)-farnesyl diphosphate
-
apparent Michaelis-Menten constant for peptide
0.0018
dansyl-Gly-Cys-Lys-Thr-Gln
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.0025
dansyl-Gly-Cys-Lys-Val-Leu
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.00014
dansyl-Gly-Cys-Val-Ile-Met
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.0007
dansyl-Gly-Cys-Val-Leu-Ser
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
additional information
additional information
kinetic analysis
-
additional information
additional information
-
correlation between Km and analogue hydrophobicity and length
-
additional information
additional information
-
comparison of KM-value of substrates with the structure Lys-Lys-Ser-Ser-Cys-Val-Ile-X for for farnesyltransferase and geranylgeranyltransferase
-
additional information
additional information
-
comparison of Km of mutant enzymes
-
additional information
additional information
-
wild-type enzyme and the H362E mutant possess similar Km for H-Ras
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
(2E,6E)-3,7-dimethyl-8-(2,3,5,6-tetrafluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.17
(2E,6E)-3,7-dimethyl-8-(phenylsulfanyl)octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.3
(2E,6E)-3,7-dimethyl-8-phenoxyocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.166
(2E,6E)-3,7-dimethyl-8-[(2-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.069
(2E,6E)-3,7-dimethyl-8-[(3-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.6
(2E,6E)-3,7-dimethyl-8-[(4-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
1.6
(2E,6E)-3,7-dimethyl-8-[(4-nitrophenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.21
(2E,6E)-3,7-dimethyl-8-[3-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.03
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.13
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.44
(2E,6E)-3,7-dimethyl-8-[4-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.16
(2E,6E)-3,7-dimethyl-8-[4-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.3
(2E,6E)-3,7-dimethyl-8-[[2-(trifluoromethyl)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.4
(2E,6E)-3,7-dimethyl-8-[[3-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.27
(2E,6E)-3,7-dimethyl-8-[[4-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.4
(2E,6E)-3,7-dimethyl-9-phenylnona-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.23
(2E,6E)-8-(2,3-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
1.67
(2E,6E)-8-(2,6-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.3
(2E,6E)-8-(2-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.11
(2E,6E)-8-(2-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.19
(2E,6E)-8-(2-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.11
(2E,6E)-8-(2-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.24
(2E,6E)-8-(3,4-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.11
(2E,6E)-8-(3,4-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.19
(2E,6E)-8-(3,5-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.1
(2E,6E)-8-(3,5-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.06
(2E,6E)-8-(3-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.04
(2E,6E)-8-(3-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.17
(2E,6E)-8-(3-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.004
(2E,6E)-8-(3-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.07
(2E,6E)-8-(3-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.3
(2E,6E)-8-(4-benzylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.5
(2E,6E)-8-(4-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
1.93
(2E,6E)-8-(4-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.28
(2E,6E)-8-(4-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.58
(2E,6E)-8-(4-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.27
(2E,6E)-8-(4-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.55
(2E,6E)-8-(4-nitrophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.17
(2E,6E)-8-(benzyloxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.04
(2E,6E)-8-(isoxazol-3-ylamino)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.17
(2E,6E)-8-[(2-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.15
(2E,6E)-8-[(2-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate
-
apparent turnover number
0.088
(2E,6E)-8-[(2-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.13
(2E,6E)-8-[(3-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.13
(2E,6E)-8-[(3-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.08
(2E,6E)-8-[(3-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.1
(2E,6E)-8-[(3-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate
-
apparent turnover number
0.24
(2E,6E)-8-[(3-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.53
(2E,6E)-8-[(3-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.27
(2E,6E)-8-[(4-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.7
(2E,6E)-8-[(4-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.095
(2E,6E)-8-[(4-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.17
(2E,6E)-8-[(4-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
1.4
(2E,6E)-8-[(4-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.44
(2E,6E)-8-[3-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
1.15
(2E,6E)-8-[4-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
apparent turnover number
0.053
(E)-[4-[(3,7-dimethylocta-2,6-dien-1-yl)oxy]phenyl]-methanyl diphosphate
-
pH 7.8, 25°C
0.009 - 0.058
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.046
TKCVIA
-
in 50 mM N2-hydroxyethylpiperazine-N-2-hydroxypropanesulfonic acid-NaOH, pH 7.8, 5 mM MgCl2, and 2 mM tris(2-carboxyethyl)phosphine hydrochloride
0.29
[3-[(3-phenoxyphenoxy)methyl]phenyl]-methanyl diphosphate
-
pH 7.8, 25°C
0.01
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate
-
apparent turnover number, measured by continuous fluorescence assay
0.12
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate
-
apparent turnover number, determined by RP-HPLC product analysis
0.009
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
-
cosubstrate: dansyl-Gly-Cys-Val-Ile-Met
0.015
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
-
cosubstrate: dansyl-Gly-Cys-Lys-Val-Leu
0.033
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
-
cosubstrate: dansyl-Gly-Cys-Lys-Thr-Gln
0.058
3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
-
cosubstrate: dansyl-Gly-Cys-Val-Leu-Ser
0.033
dansyl-Gly-Cys-Lys-Thr-Gln
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.015
dansyl-Gly-Cys-Lys-Val-Leu
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.009
dansyl-Gly-Cys-Val-Ile-Met
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
0.058
dansyl-Gly-Cys-Val-Leu-Ser
-
cosubstrate: 3-(3-methyl-2-butenyl)-7,11-dimethyldodeca-2(Z),6(E),10-triene 1-diphosphate
additional information
additional information
-
comparison of kcat of wild-type and mutant enzymes
-
additional information
additional information
-
comparison of kcat of metal-substituted enzymes, kcat for product formation decreases for C3 fluoromethyl farnesyl diphosphate substrates, paralleling the number of fluorines at the C3 methyl position
-
additional information
additional information
-
comparison of kcat of mutant enzymes
-
additional information
additional information
-
comparison of kcat-value of substrates with the structure Lys-Lys-Ser-Ser-Cys-Val-Ile-X for for farnesyltransferase and geranylgeranyltransferase
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
60
(2E,6E)-3,7-dimethyl-8-(2,3,5,6-tetrafluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
80
(2E,6E)-3,7-dimethyl-8-(phenylsulfanyl)octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
42
(2E,6E)-3,7-dimethyl-8-[(2-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
380
(2E,6E)-3,7-dimethyl-8-[(3-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
160
(2E,6E)-3,7-dimethyl-8-[(4-methylphenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
107
(2E,6E)-3,7-dimethyl-8-[(4-nitrophenyl)amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
110
(2E,6E)-3,7-dimethyl-8-[3-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
110
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
120
(2E,6E)-3,7-dimethyl-8-[3-(trifluoromethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
20
(2E,6E)-3,7-dimethyl-8-[4-(1-methylethyl)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
120
(2E,6E)-3,7-dimethyl-8-[4-(trifluoromethoxy)phenoxy]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
9
(2E,6E)-3,7-dimethyl-8-[[2-(trifluoromethyl)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
190
(2E,6E)-3,7-dimethyl-8-[[3-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
87
(2E,6E)-3,7-dimethyl-8-[[4-(trifluoromethoxy)phenyl]amino]octa-2,6-dien-1-yl trihydrogen diphosphate
-
-
110
(2E,6E)-3,7-dimethyl-9-phenylnona-2,6-dien-1-yl trihydrogen diphosphate
-
-
190
(2E,6E)-8-(2,3-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
100
(2E,6E)-8-(2,6-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
100
(2E,6E)-8-(2-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
40
(2E,6E)-8-(2-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
150
(2E,6E)-8-(2-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
50
(2E,6E)-8-(2-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
120
(2E,6E)-8-(3,4-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
160
(2E,6E)-8-(3,4-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
150
(2E,6E)-8-(3,5-dichlorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
180
(2E,6E)-8-(3,5-difluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
80
(2E,6E)-8-(3-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
100
(2E,6E)-8-(3-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
80
(2E,6E)-8-(3-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
85
(2E,6E)-8-(3-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
170
(2E,6E)-8-(3-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
130
(2E,6E)-8-(4-benzylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
30
(2E,6E)-8-(4-bromophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
60
(2E,6E)-8-(4-cyanophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
60
(2E,6E)-8-(4-ethylphenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
130
(2E,6E)-8-(4-fluorophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
120
(2E,6E)-8-(4-iodophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
80
(2E,6E)-8-(4-nitrophenoxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
170
(2E,6E)-8-(benzyloxy)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
28
(2E,6E)-8-(isoxazol-3-ylamino)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
24
(2E,6E)-8-[(2-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
160
(2E,6E)-8-[(2-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate
-
-
93
(2E,6E)-8-[(2-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
130
(2E,6E)-8-[(3-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
115
(2E,6E)-8-[(3-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
21
(2E,6E)-8-[(3-ethylphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
260
(2E,6E)-8-[(3-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl diphosphate
-
-
260
(2E,6E)-8-[(3-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
120
(2E,6E)-8-[(3-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
160
(2E,6E)-8-[(4-bromophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
68
(2E,6E)-8-[(4-cyanophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
350
(2E,6E)-8-[(4-fluorophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
120
(2E,6E)-8-[(4-iodophenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
50
(2E,6E)-8-[(4-methoxyphenyl)amino]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
100
(2E,6E)-8-[3-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
140
(2E,6E)-8-[4-(hydroxymethyl)phenoxy]-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
-
-
110
(E)-[4-[(3,7-dimethylocta-2,6-dien-1-yl)oxy]phenyl]-methanyl diphosphate
-
pH 7.8, 25°C
300
[3-[(3-phenoxyphenoxy)methyl]phenyl]-methanyl diphosphate
-
pH 7.8, 25°C
200
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate
-
measured by continuous fluorescence assay
240
(2E,6E)-3,7-dimethyl-8-(phenylamino)octa-2,6-dien-1-yl diphosphate
-
determined by RP-HPLC product analysis
150
(2E,6E)-3,7-dimethyl-8-phenoxyocta-2,6-dien-1-yl trihydrogen diphosphate
-
determined by continuous fluorescence assay
160
(2E,6E)-3,7-dimethyl-8-phenoxyocta-2,6-dien-1-yl trihydrogen diphosphate
-
determined by RP-HPLC product analysis
0.1
CCIQ
below, with (2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
0.1
CCIQ
below, with (2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
4
CCIQ
with (2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
6.6
CCIQ
with farnesyl diphosphate, pH and temperature not specified in the publication
32
CCIQ
with (2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate, pH and temperature not specified in the publication
0.1
CTIQ
below, with (2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
1.8
CTIQ
with (2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
4.9
CTIQ
with farnesyl diphosphate, pH and temperature not specified in the publication
12.1
CTIQ
with (2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
28
CTIQ
with (2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate, pH and temperature not specified in the publication
10.8
CVIS
with (2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
24
CVIS
with (2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate, pH and temperature not specified in the publication
41
CVIS
with (2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
41
CVIS
with (2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
59
CVIS
with farnesyl diphosphate, pH and temperature not specified in the publication
1.6
CVLS
with (2E,6E,10E)-3,7,11-trimethyl-12-(prop-2-yn-1-yloxy)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
2
CVLS
with (2E,6Z)-7-(but-3-yn-1-yl)-3,11-dimethyldodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
19
CVLS
with (2E,6Z)-3,11-dimethyl-7-(prop-2-yn-1-yl)dodeca-2,6,10-trien-1-yl diphosphate, pH and temperature not specified in the publication
24
CVLS
with (2E,6E)-3,7-dimethyl-8-(prop-2-yn-1-yloxy)octa-2,6-dien-1-yl diphosphate, pH and temperature not specified in the publication
47
CVLS
with farnesyl diphosphate, pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
comparison of KI-values of tetrapeptide inhibitors L-penicillamine-Val-Ile-X and Cys-Val-Phe-X for farnesyltransferase and geranylgeranyltransferase
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
(1R,4aR,5R,7S)-5-[[(1R,4aR,8aS)-8a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-6-methoxy-5,8-dioxo-1,4,4a,5,8,8a-hexahydronaphthalen-1-yl]methyl]-7-hydroxy-1,4a-dimethyl-6-methylidenedecahydronaphthalene-1-carbaldehyde
Rattus norvegicus
-
30°C, pH 7.5
0.04
(1R,4aR,5R,7S)-5-[[(1R,4aR,8aS)-8a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-6-methoxy-5,8-dioxo-1,4,4a,5,8,8a-hexahydronaphthalen-1-yl]methyl]-7-hydroxy-1,4a-dimethyl-6-methylidenedecahydronaphthalene-1-carboxylic acid
Rattus norvegicus
-
30°C, pH 7.5
0.086
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-2-methoxy-5-[[(1S,3S,7S,8aS)-1,3,7-trihydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.0032
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-2-methoxy-6-methyl-5-[[(1R,8aS)-5,5,8a-trimethyl-2-methylidene-3-oxodecahydronaphthalen-1-yl]methyl]-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.01
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,3S,5R,8aS)-3-hydroxy-5-(hydroxymethyl)-5,8a-dimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.04
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,3S,7S,8aS)-3,7-dihydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.0057
(4aS,5R,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.003
(4aS,5R,8aR)-4a-(5-hydroxy-7-methoxy-4-oxo-4H-chromen-2-yl)-2-methoxy-6-methyl-5-[[(1R,8aS)-5,5,8a-trimethyl-2-methylidene-3-oxodecahydronaphthalen-1-yl]methyl]-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.017
(4aS,5S,8aR)-4a-(5,7-dihydroxy-4-oxo-4H-chromen-2-yl)-5-[[(1R,2R,7S,8aS)-2,7-dihydroxy-2,5,5,8a-tetramethyldecahydronaphthalen-1-yl]methyl]-6-hydroxy-2-methoxy-4a,5,8,8a-tetrahydronaphthalene-1,4-dione
Rattus norvegicus
-
30°C, pH 7.5
0.0131
(S)-N-(4-(3,4-dichlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
Rattus norvegicus
-
pH 7.4, 30°C
0.0178
(S)-N-(4-(3-chlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
Rattus norvegicus
-
pH 7.4, 30°C
0.037
1,4,8,10-tetrahydroxy-6-[(1E)-3-[(3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]-1-methylprop-1-en-1-yl]-5,6-dihydro-7H-benzo[c]xanthen-7-one
Rattus norvegicus
-
30°C, pH 7.5
0.0000075
1-methyl-1H-imidazole-4-sulfonic acid [6-cyano-1-(3-methyl-3H-imidazol-4-yl-methyl)-1,2,3,4-tetrahydro-quinolin-3-yl]-(3-methoxy-propyl)-amide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000034
1-methyl-N-[1-[(1-methyl-1H-imidazol-5-yl)methyl]-6-phenyl-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(5-methylisoxazol-4-yl)methyl]-1H-imidazole-4-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000048
1-methylethyl 4-[([1-[(1-methyl-1H-imidazol-5-yl)methyl]-6-phenyl-1,2,3,4-tetrahydroquinolin-3-yl][(1-methyl-1H-imidazol-4-yl)sulfonyl]amino)methyl]piperidine-1-carboxylate
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.00000037
4-(3-{[(4-cyano-3-naphthalen-1-yl-phenyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-methyl}-phenyl)-pyridine-2-carbonitrile
Rattus norvegicus
-
IC50: 0.37 nM, selective inhibitor
0.00000045
4-[(3'-Chloro-biphenyl-3-ylmethyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 0.45 nM, selective inhibitor
0.000039
4-[(3-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 0.39 nM, selective inhibitor
0.000031
4-[(3-Methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 31 nM
0.0000015
4-[(4-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 1.5 nM, selective inhibitor
0.0000015
4-[Biphenyl-3-ylmethyl-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 1.5 nM
0.0000019
4-[Hexyl-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 1.9 nM
0.000038
4-[Methyl-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2-naphthalen-1-yl-benzonitrile
Rattus norvegicus
-
IC50: 38 nM
0.000025
4-[[[6-cyano-1-(3-methyl-3H-imidazol-4-ylmethyl)-1,2,3,4-tetrahydro-quinolin-3-yl]-(pyridine-2-sulfonyl)-amino]-methyl]-piperidine-1-carboxylic acid isobutyl ester
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000032
4-[[[6-cyano-1-(3-methyl-3H-imidazol-4-ylmethyl)-1,2,3,4-tetrahydro-quinolin-3-yl]-(pyridine-2-sulfonyl)-amino]-methyl]-piperidine-1-carboxylic acid methyl ester
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.025
5,7-dihydroxy-2-[(5R)-1-hydroxy-5-[[(3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-2-methoxy-6-methyl-4-oxo-1,5,8,8a-tetrahydronaphthalen-4a(4H)-yl]-4H-chromen-4-one
Rattus norvegicus
-
30°C, pH 7.5
0.007
5,7-dihydroxy-2-[(5R)-1-hydroxy-5-[[(3S,8aS)-3-hydroxy-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]-6-methyl-2-oxo-1,5,8,8a-tetrahydronaphthalen-4a(2H)-yl]-4H-chromen-4-one
Rattus norvegicus
-
30°C, pH 7.5
0.00000097
5-[(3-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2'-methyl-biphenyl-2-carbonitrile
Rattus norvegicus
-
IC50: 0.97 nM, selective inhibitor
0.00001
5-[(4-cyano-benzyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amino]-2'-methyl-biphenyl-2-carbonitrile
Rattus norvegicus
-
IC50: 10 nM, selective inhibitor
0.000014
Biphenyl-3-carboxylic acid (4-cyano-3-naphthalen-1-yl-phenyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amide
Rattus norvegicus
-
IC50: 14 nM
0.000018
Biphenyl-3-sulfonic acid (4-cyano-3-naphthalen-1-yl-phenyl)-(3-methyl-3H-imidazol-4-ylmethyl)-amide
Rattus norvegicus
-
IC50: 18 nM
0.0000055
ethyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000228
methyl N-(1-cysteinylpiperidin-4-yl)-N-(phenylcarbonyl)-L-methioninate
Rattus norvegicus
-
IC50: 22.8 nM
0.0000327
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-isoleucinate
Rattus norvegicus
-
IC50: 32.7 nM
0.0000046
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-methioninate
Rattus norvegicus
-
IC50: 4.6 nM
0.000022
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-phenylalaninate
Rattus norvegicus
-
IC50: 22 nM
0.0000439
methyl N-(phenylcarbonyl)-N-{1-([1-[4-(trifluoromethyl)benzyl]-1H-imidazol-4-yl]methyl)piperidin-4-yl}-L-methioninate
Rattus norvegicus
-
IC50: 43.9 nM
0.00000235
methyl N-benzyl-N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]piperidin-4-yl)-L-methioninate
Rattus norvegicus
-
IC50: 2.35 nM
0.000397
methyl N-[1-[(1-benzyl-1H-imidazol-4-yl)methyl]piperidin-4-yl]-N-(phenylcarbonyl)-L-methioninate
Rattus norvegicus
-
IC50: 397 nM
0.000005
N-tert-butyl-N2-[6-cyano-1-(1-methyl-1H-imidazol-5-yl)-1,2,3,4-tetrahydroquinolin-3-yl]-N2-[(1-methyl-1H-imidazol-2-yl)sulfonyl]glycinamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000065
N-[(1-butanoylpiperidin-4-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.00044
N-[(3-bromonaphthalen-2-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.00001
N-[(6-chloro-2,1,3-benzothiadiazol-5-yl)methyl]-N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.000105
N-[1-[(1-methyl-1H-imidazol-5-yl)methyl]-6-phenyl-1,2,3,4-tetrahydroquinolin-3-yl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000078
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl]-N-[[1-(3,3-dimethylbutanoyl)piperidin-4-yl]methyl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.000016
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl]-N-[[1-(phenylcarbonyl)piperidin-4-yl]methyl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000026
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-1-methyl-N-[4-(1H-pyrazol-1-yl)benzyl]-1H-imidazole-4-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.001
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(2-fluorobenzyl)-1-methyl-1H-imidazole-4-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000038
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-(pyridin-2-ylmethyl)pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.000003
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[(4-phenyl-1,3-oxazol-5-yl)methyl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.0000017
N-[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl]-N-[2-(1H-pyrrol-1-yl)ethyl]pyridine-2-sulfonamide
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
0.000007
tert-butyl 4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4-tetrahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]piperidine-1-carboxylate
Rattus norvegicus
-
at pH 7.5, in 50 mM HEPES, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, 0.01% Triton X-100
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
pH-dependence of the chemical step of product formation: the reaction is characterized by two ionizations, drastic differences in the pH dependence of farnesyl diphophate and farnesyl monophosphate, the magnesium affinity of enzyme increases with pH with a pka of 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity
physiological function
malfunction
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity
physiological function
additional information
physiological function
farnesyltransferase alpha subunit regulates vacuolar protein sorting-associated protein 4A (Vps4A)-dependent intracellular trafficking through recycling endosomes. The enzyme FTase alpha controls trafficking of transferrin receptor upstream of thie Vps4A protein
physiological function
FTase catalyzes farnesyl isoprenoid linked to the cysteine residue of the CAAX protein through a thioether linkage, which will enhance the hydrophobicity of the CAAX protein. Meanwhile, the formed CAAX-protein-isoprenoid complex is attached to the endoplasmic reticulum surface
physiological function
-
posttranslational modification of proteins involved in intracellular signal transduction network
physiological function
FTase catalyzes farnesyl isoprenoid linked to the cysteine residue of the CAAX protein through a thioether linkage, which will enhance the hydrophobicity of the CAAX protein. Meanwhile, the formed CAAX-protein-isoprenoid complex is attached to the endoplasmic reticulum surface
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
ligand interaction analysis with FTase alpha subunit, mass spectrometry, overview. Modelling of dimeric FTase alpha subunits
additional information
comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
-
comparison of the substrate specificities of PFTases from three organisms, Rattus norvegicus, Saccharomyces cerevisiae, and Candida albicans, using CVa2X libraries, overview. Rattus norvegicus PFTase shares more peptide substrates with Saccharomyces cerevisiae PFTase than with Candida albicans PFTase
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
additional information
FTase and GGTase-I recognize the same CAAX sequence motif in a protein substrate and catalyze the attachment of farnesyl and geranygeranyl groups to the protein, respectively. The X is the key residue that determines the farnesylation or geranylgeranylation of the CAAX-containing protein. When X is serine, methionine or glutamine the protein substrate is preferentially activated by FTase, but when X is leucine or phenylalanine the protein substrate is preferentially activated by GGTase-I
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FNTA_RAT
377
0
44049
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
78000
about, alpha-subunit dimer, multi-angle laser light scattering
44000
-
alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy
46000
46200
-
alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy
487000
-
alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy
50000
-
alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 41000, about, alpha-subunit, sequence calculation, in the absence of the beta subunit, the alpha subunit of FTase forms a stable autonomous dimeric structure in solution, which may indicate that it has other physiological functions outside the alpha/beta heterodimer
heterodimer
additional information
heterodimer
-
alpha,beta, 1 * 50000 + 1 * 44000, SDS-PAGE, 1 * 46200 + 1 * 487000, mass spectroscopy
additional information
-
the secondary structures of alpha subunit include 15 alpha helices, three short 3,10 helices and a beta strand, the beta subunit contains 14 alpha helices, seven short 3,10 helices and three beta strands
additional information
-
the alpha-subunit plays a direct role in the catalytic reaction in addition to its role in the stabilization of the beta-subunit
additional information
the alpha-subunit does not form homodimers. Crosslinking experiments reveal farnesyltransferase alpha-subunit trimers and higher oligomerization states
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a new crystalline form of enzyme for the mutant truncated 10 residues at the C-terminus
-
at 2.25 Angstrom, zinc occurs at a junction between a hydrophilic surface groove near the subunit interface: peptide binding site, and a deep lipophilic cleft in the beta subunit lined with aromatic residues: farnesyl diphosphate binding site
-
farnesyl diphosphate and peptide substrate can be accommodated in the hydrophobic active-site barrel, with the sole charged residue inside the barrel, Arg202 of the beta-subunit, forming a salt bridge with the negatively charged carboxy terminus of peptide substrate
-
molecular dynamics simulations to study enzyme flexibility in the 4 key intermediate states formed during the FTase catalytic mechanisms, ie. FTase resting state, binary complex FTase-FPP, ternary complex FTase-FPP-peptide, and product complex FTase-product. Relatively small-scale events such as substrate binding or product formation cause minor changes at the neighboring residues and corresponding helices, but ultimately induce much more dramatic effects on the more external regions of the enzyme
-
the isoprenoid moiety of farnsyl diphophate binds in an extended conformation in a hydrophobic cavity of the beta-subunit of the enzyme, and the diphosphate moiety binds to a positively charged cleft at the top of this cavity near the subunit interface
-
two crystal structures of enzyme complex: one containing farnesylated Ras peptide product alone and a complex that contains both the farnesylated peptide and an additional farnesyl diphosphate substrate
-
X-ray crystal structure, modelling indicates that geranylgeranyl diphosphate adopts a different conformation than the farnesyl chain of farnesyl diphosphate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D352A
in the D352A mutant of the beta subunit Mg2+ binding motif, three water molecules and one oxygen atom from the alpha- and beta-phosphates of farnesyl diphosphate complete the octahedral coordination sphere of Mg2+. The absence of D352beta makes the transition of the substrates towards a conformational change harder
Dbeta352A
-
drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. The Km(Mg2+) increases 28-fold to 110 mM, and the farnesylation rate constant at saturating Mg2+ decreases 27-fold to 0.30 per s
Dbeta352K
-
drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. Mutation removes the magnesium activation of farnesylation catalyzed by FTase but does not significantly enhance the rate constant for farnesylation in the absence of Mg2+
H248A
-
beta-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 10fold decreased in comparison of wild-type, the rate constant by chemical step using farnesyl monophosphate 5fold decreased
H362Q
K164A
-
alpha-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 30fold decreased in comparison of wild-type enzyme, the rate constant by chemical step using farnesyl monophosphate unaffected
K294A
-
slightly higher peptide affinity than wild-type enzyme, 7fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
K294Q
-
little alteration in peptide affinity, 2fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
R291A
-
2fold lower peptide affinity than wild-type enzyme, 3-4fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
R291G
-
little alteration in peptide affinity, 3-4fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type,decrease in rate constant for farnesylation in absence of Mg2+
R291K
-
slightly higher peptide affinity than wild-type enzyme, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
R291Q
-
little alteration in peptide affinity, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
Y300F
-
beta-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 500fold decreased in comparison of wild-type enzyme, the rate constant by chemical step using farnesyl monophosphate 300fold decreased. Transition state for farnesylation is stabilized by interactions between the alpha-phosphate of the isoprenoid substrate and the side chains of Y300beta
additional information
additional information
-
all five mutant enzymes bind farnesyl diphosphate with similar affinity to that of the wild-type enzyme, indicating that the targeted residues neither directly nor indirectly influence the farnesyl diphosphate binding site, only the wild-type enzyme able to bind zinc, while all five of the mutant enzymes lose this ability
additional information
-
mutations have a little effect on the pH and magnesium dependence: side chains K164alpha, H248beta and Y300beta not function either as general acid-base catalyst or as magnesium ligands
additional information
-
three beta-subunit C-terminal truncation mutants, deletion of 5, 10 and 14 residues, the overall catalytic efficiency of enzyme decreases gradually with increasing C-terminal deletion
additional information
-
deletion of 51 amino acids at the NH2 terminus of alpha subunit: activity the same as wild-type enzyme, deletion of 106 amino acids at the NH2 terminus: complete loss of activity, suggesting that residues between 51 and 106 are important for activity, deletion of 5 amino acids at the COOH terminus reduces alpha-subunit activity to about 50% of activity of wild-type enzyme, removal of 20 amino acids at the COOH terminus: complete loss of activity
additional information
-
S99betaA mutant, influence on forming hydrogen bonds of the side chains with peptide substrates
additional information
-
W102betaA mutant, influence on forming hydrogen bonds of the side chains with peptide substrates
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the heterodimer cannot be dissociated unless it is denaturated, and each individual subunit appears to be unstable in solution, the number of hydrogen bonds found in the enzyme subunit interface may explain the unusual stability of the heterodimer
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of alpha and beta subunits of enzyme by Sf9 cells infected with a recombinant baculovirus
-
coexpression of alpha and beta subunits of enzyme with a recombinant baculovirus
-
expression in Escherichia coli
translationally coupled two-cistron expression system for enzyme in Escherichia coli
-
wild-type enzyme and mutant enzymes expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers
medicine
-
prime target for development of anticancer therapeutics
medicine
-
inhibition of protein farnesyltransferase with influence for oncogenesis, potential target for treatment of cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Furfine, E.S; Leban, J.J.; Landavazo, A.; Moomaw, J.F.; Casey, P.J.
Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release
Biochemistry
34
6857-6862
1995
Rattus norvegicus
Long, S.B.; Casey, P.J.; Beese, L.S.
Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
Biochemistry
37
9612-9618
1998
Rattus norvegicus
Micali, E.; Chehade, K.A.; Isaacs, R.J.; Andres, D.A.; Spielmann, H.P.
Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups
Biochemistry
40
12254-12265
2001
Rattus norvegicus
Long, S.B.; Casey, P.J.; Beese, L.S.
Reaction path of protein farnesyltransferase at atomic resolution
Nature
419
645-650
2002
Rattus norvegicus
Chen, W.J.; Moomaw, J.F.; Overton, L.; Kost, T.A.; Casey, P.J.
High level expression of mammalian protein farnesyltransferase in a baculovirus system
J. Biol. Chem.
286
9675-9680
1993
Rattus norvegicus
Park, H.W.; Beese, L.S.
Protein farnesyltransferase
Curr. Opin. Struct. Biol.
7
873-880
1997
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
Yokoyama, K.; Trobridge, P.; Buckner, F.S.; Van Voorhis, W.C.; Stuart, K.D.; Gelb, M.H.
Protein farnesyltransferase from Trypanosoma brucei. A heterodimer of 61- and 65-kDa subunits as a new target for antiparasite therapeutics
J. Biol. Chem.
273
26497-26505
1998
Rattus norvegicus, Trypanosoma brucei brucei, Trypanosoma brucei brucei EATRO 140
Fu, H.W.; Beese, L.S.; Casey, P.J.
Kinetic analysis of zinc ligand mutants of mammalian protein farnesyltransferase
Biochemistry
37
4465-4472
1998
Rattus norvegicus
Huang, C.c.; Hightower, K.E.; Fierke, C.A.
Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state
Biochemistry
39
2593-2602
2000
Rattus norvegicus
Saderholm, M.J.; Hightower, K.E.; Fierke, C.A.
Role of metals in the reaction catalyzed by protein farnesyltransferase
Biochemistry
39
12398-12405
2000
Rattus norvegicus
Pickett, J.S.; Bowers, K.E.; Hartman, H.L.; Fu, H.W.; Embry, A.C.; Casey, P.J.; Fierke, C.A.
Kinetic studies of protein farnesyltransferase mutants establish active substrate conformation
Biochemistry
42
9741-9748
2003
Rattus norvegicus
Andres, D.A.; Goldstein, J.L.; Ho, Y.K.; Brown, M.S.
Mutational analysis of a-subunit of protein farnesyltransferase. Evidence for a catalytic role
J. Biol. Chem.
268
1383-1390
1993
Rattus norvegicus
Dunten, P.; Kammlott, U.; Crowther, R.; Weber, D.; Palermo, R.; Birktoft, J.
Protein farnesyltransferase: Structure and implications for substrate binding
Biochemistry
37
7907-7912
1998
Rattus norvegicus
Roskoski, R.Jr.; Ritchie, P.
Role of the carboxyterminal residue in peptide binding to protein farnesyltransferase and protein geranylgeranyltransferase
Arch. Biochem. Biophys.
356
167-176
1998
Rattus norvegicus
Wu, Z.; Demma, M.; Strickland, C.L.; Syto, R.; Le, H.V.; Windsor, W.T.; Weber, P.C.
High-level expression, purification, kinetic characterization and crystallization of protein farnesyltransferase b-subunit C-terminal mutants
Protein Eng.
12
341-348
1999
Homo sapiens, Rattus norvegicus
Park, H.W.; Boduluri, S.R.; Moomaw, J.F.; Casey, P.J.; Beese, L.S.
Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
Science
275
1800-1804
1997
Rattus norvegicus
Bowers, K.E.; Fierke, C.A.
Positively charged side chains in protein farnesyltransferase enhance catalysis by stabilizing the formation of the diphosphate leaving group
Biochemistry
43
5256-5265
2004
Rattus norvegicus
Reigard, S.A.; Zahn, T.J.; Haworth, K.B.; Hicks, K.A.; Fierke, C.A.; Gibbs, R.A.
Interplay of isoprenoid and peptide substrate specificity in protein farnesyltransferase
Biochemistry
44
11214-11223
2005
Rattus norvegicus
Curtin, M.L.; Florjancic, A.S.; Cohen, J.; Gu, W.Z.; Frost, D.J.; Muchmore, S.W.; Sham, H.L.
Novel and selective imidazole-containing biphenyl inhibitors of protein farnesyltransferase
Bioorg. Med. Chem. Lett.
13
1367-1371
2003
Rattus norvegicus
Tobin, D.A.; Pickett, J.S.; Hartman, H.L.; Fierke, C.A.; Penner-Hahn, J.E.
Structural characterization of the zinc site in protein farnesyltransferase
J. Am. Chem. Soc.
125
9962-9969
2003
Rattus norvegicus
Pickett, J.S.; Bowers, K.E.; Fierke, C.A.
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand
J. Biol. Chem.
278
51243-51250
2003
Rattus norvegicus
Hartman, H.L.; Hicks, K.A.; Fierke, C.A.
Peptide specificity of protein prenyltransferases is determined mainly by reactivity rather than binding affinity
Biochemistry
44
15314-15324
2005
Rattus norvegicus
Ryckebusch, A.; Gilleron, P.; Millet, R.; Houssin, R.; Lemoine, A.; Pommery, N.; Grellier, P.; Sergheraert, C.; Henichart, J.P.
Novel N-(4-piperidinyl)benzamide antimalarials with mammalian protein farnesyltransferase inhibitory activity
Chem. Pharm. Bull.
53
1324-1326
2005
Rattus norvegicus
Guida, W.C.; Hamilton, A.D.; Crotty, J.W.; Sebti, S.M.
Protein farnesyltransferase: flexible docking studies on inhibitors using computational modeling
J. Comput. Aided Mol. Des.
19
871-885
2006
Rattus norvegicus
Sousa, S.F.; Fernandes, P.A.; Ramos, M.J.
Effective tailor-made force field parameterization of the several Zn coordination environments in the puzzling FTase enzyme: opening the door to the full understanding of its elusive catalytic mechanism
Theoret. Chem. Accounts
117
171-181
2007
Rattus norvegicus
-
Olepu, S.; Suryadevara, P.K.; Rivas, K.; Yokoyama, K.; Verlinde, C.L.; Chakrabarti, D.; Van Voorhis, W.C.; Gelb, M.H.
2-Oxo-tetrahydro-1,8-naphthyridines as selective inhibitors of malarial protein farnesyltransferase and as anti-malarials
Bioorg. Med. Chem. Lett.
18
494-497
2008
Plasmodium falciparum, Rattus norvegicus
Bendale, P.; Olepu, S.; Suryadevara, P.K.; Bulbule, V.; Rivas, K.; Nallan, L.; Smart, B.; Yokoyama, K.; Ankala, S.; Pendyala, P.R.; Floyd, D.; Lombardo, L.J.; Williams, D.K.; Buckner, F.S.; Chakrabarti, D.; Verlinde, C.L.; Van Voorhis, W.C.; Gelb, M.H.
Second generation tetrahydroquinoline-based protein farnesyltransferase inhibitors as antimalarials
J. Med. Chem.
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2007
Plasmodium falciparum, Rattus norvegicus
Kim, S.J.; Kwon, B.; Kim, S.; Baek, N.; Yang, J.H.; Lee, J.J.; Lee, S.I.; Kwon, Y.; Park, H.W.; Lee, J.H.; Park, J.; Kim, D.K.
Farnesyl protein transferase inhibitory components of Lithospermum erythrorhizon
Nat. Prod. Sci.
13
328-331
2007
Homo sapiens, Rattus norvegicus
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Hougland, J.L.; Lamphear, C.L.; Scott, S.A.; Gibbs, R.A.; Fierke, C.A.
Context-dependent substrate recognition by protein farnesyltransferase
Biochemistry
48
1691-1701
2009
Rattus norvegicus
Sousa, S.F.; Fernandes, P.A.; Ramos, M.J.
Molecular dynamics simulations on the critical states of the farnesyltransferase enzyme
Bioorg. Med. Chem.
17
3369-3378
2009
Rattus norvegicus
Hast, M.A.; Fletcher, S.; Cummings, C.G.; Pusateri, E.E.; Blaskovich, M.A.; Rivas, K.; Gelb, M.H.; Van Voorhis, W.C.; Sebti, S.M.; Hamilton, A.D.; Beese, L.S.
Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase
Chem. Biol.
16
181-192
2009
Homo sapiens, Plasmodium falciparum, Rattus norvegicus
Subramanian, T.; Liu, S.; Troutman, J.M.; Andres, D.A.; Spielmann, H.P.
Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity
ChemBioChem
9
2872-2882
2008
Rattus norvegicus
Gupta, M.K.; Prabhakar, Y.S.
QSAR study on tetrahydroquinoline analogues as plasmodium protein farnesyltransferase inhibitors: a comparison of rationales of malarial and mammalian enzyme inhibitory activities for selectivity
Eur. J. Med. Chem.
43
2751-2767
2008
Plasmodium falciparum, Rattus norvegicus (Q02293), Rattus norvegicus (Q04631)
DeGraw, A.J.; Keiser, M.J.; Ochocki, J.D.; Shoichet, B.K.; Distefano, M.D.
Prediction and evaluation of protein farnesyltransferase inhibition by commercial drugs
J. Med. Chem.
53
2464-2471
2010
Rattus norvegicus
Hougland, J.L.; Hicks, K.A.; Hartman, H.L.; Kelly, R.A.; Watt, T.J.; Fierke, C.A.
Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities
J. Mol. Biol.
395
176-190
2010
Rattus norvegicus
Long, C.; Marcourt, L.; Raux, R.; David, B.; Gau, C.; Menendez, C.; Gao, M.; Laroche, M.F.; Schambel, P.; Delaude, C.; Ausseil, F.; Lavaud, C.; Massiot, G.
Meroterpenes from Dichrostachys cinerea inhibit protein farnesyl transferase activity
J. Nat. Prod.
72
1804-1815
2009
Rattus norvegicus
Subramanian, T.; Pais, J.E.; Liu, S.; Troutman, J.M.; Suzuki, Y.; Leela Subramanian, K.; Fierke, C.A.; Andres, D.A.; Spielmann, H.P.
Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferase
Biochemistry
51
8307-8319
2012
Rattus norvegicus
Qiao, Y.; Gao, J.; Qiu, Y.; Wu, L.; Guo, F.; Lo, K.K.; Li, D.
Design, synthesis, and characterization of piperazinedione-based dual protein inhibitors for both farnesyltransferase and geranylgeranyltransferase-I
Eur. J. Med. Chem.
46
2264-2273
2011
Rattus norvegicus
Yang, Y.; Wang, B.; Ucisik, M.N.; Cui, G.; Fierke, C.A.; Merz, K.M.
Insights into the mechanistic dichotomy of the protein farnesyltransferase peptide substrates CVIM and CVLS
J. Am. Chem. Soc.
134
820-823
2012
Rattus norvegicus (Q04631)
Wang, Y.C.; Dozier, J.K.; Beese, L.S.; Distefano, M.D.
Rapid analysis of protein farnesyltransferase substrate specificity using peptide libraries and isoprenoid diphosphate analogues
ACS Chem. Biol.
9
1726-1735
2014
Saccharomyces cerevisiae (P29703 AND P22007), Saccharomyces cerevisiae, Rattus norvegicus (Q04631 AND Q02293), Rattus norvegicus, Candida albicans (Q9Y765)
Kubala, M.H.; Norwood, S.J.; Gomez, G.A.; Jones, A.; Johnston, W.; Yap, A.S.; Mureev, S.; Alexandrov, K.
Mammalian farnesyltransferase alpha subunit regulates vacuolar protein sorting-associated protein 4A (Vps4A)-dependent intracellular trafficking through recycling endosomes
Biochem. Biophys. Res. Commun.
468
580-586
2015
Saccharomyces cerevisiae (P29703), Rattus norvegicus (Q04631)
Jennings, B.C.; Danowitz, A.M.; Wang, Y.C.; Gibbs, R.A.; Distefano, M.D.; Fierke, C.A.
Analogs of farnesyl diphosphate alter CaaX substrate specificity and reactions rates of protein farnesyltransferase
Bioorg. Med. Chem. Lett.
26
1333-1336
2016
Rattus norvegicus (Q04631 AND Q02293)
Shen, M.; Pan, P.; Li, Y.; Li, D.; Yu, H.; Hou, T.
Farnesyltransferase and geranylgeranyltransferase I: structures, mechanism, inhibitors and molecular modeling
Drug Discov. Today
20
267-276
2015
Homo sapiens (P49354), Homo sapiens (P49356), Rattus norvegicus (Q02293), Rattus norvegicus (Q04631)
Ashok, S.; Hildebrandt, E.R.; Ruiz, C.S.; Hardgrove, D.S.; Coreno, D.W.; Schmidt, W.K.; Hougland, J.L.
Protein farnesyltransferase catalyzes unanticipated farnesylation and geranylgeranylation of shortened target sequences
Biochemistry
59
1149-1162
2020
Rattus norvegicus (Q04631 AND Q02293)
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