Any feedback?
Information on EC 2.5.1.58 - protein farnesyltransferase and Organism(s) Homo sapiens and UniProt Accession P49356
for references in articles please use BRENDA:EC2.5.1.58Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 2.5.1.58
-
farnesylation
-
prenylation
-
geranylgeranylation
-
isoprenoids
- beta-subunits
-
isoprenylation
-
15-carbon
- lamins
- manumycin
-
geranylgeranyltransferase-i
-
farnesyl-protein
- h-ras
- medicine
-
peptidomimetic
-
prelamin
- ggtase-i
-
p21ras
- tetrapeptide
- farnesol
- tetrahydroquinoline
-
ras-dependent
- pharmacology
-
progerin
-
3hmevalonate
-
ras-induced
- lovastatin
- tipifarnib
- drug development
-
ras-mediated
-
ras-transformed
- lonafarnib
-
hutchinson-gilford
-
dimethylallyl
- geranylgeraniol
- isoprene
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
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
-
-
-
-
farnesyl protein transferase
farnesyltransferase
farnesyltransferase, farnesyl pyrophosphate-protein
-
-
-
-
farnesyltransferase, protein
-
-
-
-
FPT
-
-
-
-
fptase
FTase
PFT
-
-
-
-
prenylprotein transferase
-
-
-
-
prenyltransferase
-
-
-
-
protein cysteine farnesyltransferase
-
-
-
-
protein farnesyltransferase
protein prenyltransferase
-
-
-
-
RAS farnesyltransferase
-
-
-
-
farnesyl protein transferase
-
-
-
-
farnesyltransferase
-
-
-
-
fptase
-
-
-
-
FTase
-
-
-
-
FTase
-
-
protein farnesyltransferase
-
-
-
-
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
-
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 + (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 + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-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 + [protein]-L-cysteine
[protein]-S-((2E,6E)-farnesyl)-L-cysteine + diphosphate
-
assay at pH 7.5, 30°C
-
-
?
(2E,6E)-farnesyl diphosphate + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-L-cysteine + diphosphate
-
-
-
?
(2Z)-geranylgeranyl diphosphate + protein cysteine
diphosphate + S-(2Z)-geranylgeranylcysteinyl protein
-
-
-
-
?
dansyl-GCVDS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVDS + diphosphate
-
poor substrate for wild-type
-
-
?
dansyl-GCVKS + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVKS + diphosphate
-
poor substrate for wild-type
-
-
?
farnesyl diphosphate + Ras oncoprotein p21
diphosphate + Ras-S-farnesyl oncoprotein p21
-
-
-
-
?
farnesyl diphosphate + Ras protein
diphosphate + S-farnesyl Ras protein
-
-
-
-
?
farnesyl diphosphate + Ras-Cys-Val-Ile-Met
diphosphate + Ras-S-farnesyl-Cys-Val-Ile-Met
-
-
-
-
?
farnesyl diphosphate + Ras-Cys-Val-Leu-Met
diphosphate + Ras-S-farnesyl-Cys-Val-Leu-Met
-
-
-
-
?
farnesyl triphosphate + [Ras]-Cys-Val-Ile-Met
triphosphate + [Ras]-S-farnesyl-Cys-Val-Ile-Met
-
-
-
-
?
(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
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
ir
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
Ftase has an autonomous recognition sequence, referred to as the CAAX box, where C is a cysteine, A is usually an aliphatic amino acid, and X can be a variety of amino acids
-
-
?
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
-
the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are direcly involved in protein-protein interactions as well as in protein-membrane interactions
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
substrate motif: carboxy-terminal -Ca1a2X box
-
-
?
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
?
-
-
biotin-GPP is not transferred to the peptide substrate to any measurable extent
-
-
?
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
-
-
?
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 + (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 + [Rho]-L-cysteine
S-(2E,6E)-farnesyl-[Rho]-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)-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
-
the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are direcly involved in protein-protein interactions as well as in protein-membrane interactions
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
Mg2+
-
required, stabilizes the developing negative charge on the diphosphate as the bond breaks between the a-phosphate and the C1 atom of the farnesyl group
Zn2+
-
a single zinc ion bound to the beta subunit, near the subunit interface, which marks the location of the active site
Zn2+
-
contains one Zn2+ ion per dimer, required for catalysis and peptide binding
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile
binds into the CAAX peptide site and competes with the CAAX substrate of FTase
lonafarnib
active in Ras-dependent and -independent malignant tumors
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
-
(2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-1-[2-(methylsulfanyl)ethyl]hydrazinyl)acetic acid
-
-
(2E)-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]butanedioic acid
-
-
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
-
-
(2Z,6E)-3-(3-methylbut-2-enyl)-7,11-dimethyldodeca-2,6,10-triene monophosphate
-
IC50: 16 nM
(2Z,6E)-3-allyl-7,11-dimethyldodeca-2,6,10-trien-1-yl 5-nitrofurfuryl N-methyl-N-(4-chlorobutyl)phosphoramidate
-
-
(2Z,6E)-3-tert-butyl-7,11-dimethyldodeca-2,6,10-trien-1-yl 5-nitrofurfuryl N-methyl-N-(4-chlorobutyl)phosphoramidate
-
-
(2Z,6E)-3-tert-butyl-7,11-dimethyldodeca-2,6,10-triene monophosphate
-
IC50: 13 nM
(2Z,6E,10E)-3-(3-methyl-1-but-2-enyl)-7,11-dimethyldodeca-2,6,10-trien-1-yl 5-nitrofurfuryl N-methyl-N-(4-chlorobutyl)phosphoramidate
-
-
(4E,8E)-2-(ethoxycarbonyl)-5,9,13-trimethyl-2-[3-(1-methyl-1H-imidazol-2-yl)propyl]tetradeca-4,8,12-trienoic acid
-
-
(4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-4,8,12-trienoic acid
-
-
(4S)-4-([[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]amino)-5-tert-butoxy-5-oxopentanoic acid
-
-
1-(1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4,4-dicyano-1-oxobut-3-en-2-yl)-3-(dimethylamino)pyridinium
-
-
1-(1H-imidazol-5-ylmethyl)-7-pyridin-4-yl-4-[[2-(trifluoromethoxy)phenyl]carbonyl]-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine
-
-
1-[(3Z)-1-(4-bromophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-1-(4-chlorophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-1-(3,4-dimethoxyphenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-methoxypyridinium
-
-
1-[(3Z)-4-cyano-1-(4-cyanophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-1-(4-fluorophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-3-methoxypyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methylphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-nitrophenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-phenylhept-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-phenylhept-3-en-2-yl]-3-methylpyridinium
-
-
1-[1-(4-bromophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[1-(4-chlorophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(3,4-dimethoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
-
-
1-[4,4-dicyano-1-(4-cyanophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-fluorophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-methylphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-(4-nitrophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-2,4-dimethylpyridinium
-
-
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-3-(dimethylamino)pyridinium
-
-
18-oxa-2,5,9,11-tetraazahexacyclo[17.6.2.22,5.113,17.07,11.022,26]triaconta-1(26),7,9,13(28),14,16,19,21,22,24,26-undecaene-16-carbonitrile
-
-
2-amino-3-[2-butyl-4-(naphthalen-1-ylcarbonyl)piperazin-1-yl]propane-1-thiol
-
-
2-[(2E)-3,7-dimethyl-1-(1-methyl-1H-imidazol-2-yl)octa-2,6-dien-1-yl]butanedioic acid
-
-
29-oxo-18-oxa-2,6,9,11-tetraazahexacyclo[17.5.3.12,5.113,17.07,11.022,26]nonacosa-7,9,13(28),14,16,19,21,26-octaene-16-carbonitrile
-
-
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)-N-adamantylthiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-N'-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carbohydrazide
-
-
3-(4-chlorophenyl)-4-cyano-N-(naphthalen-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-cyano-N-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylic acid
-
-
3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
3-methyl-2-[2-oxo-2-(10H-phenothiazin-10-yl)ethyl]indeno[1,2-c]pyrazol-4(2H)-one
-
most potent in vitro cytostatic activity inhibiting the growth of HCT-116, LOX IMVI and SK-MEL-5 cell lines
3-oxo-3-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanoic acid
-
-
3-[3-[2-([2-[1-(tert-butoxycarbonyl)piperidin-4-yl]-1-([(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]methyl)ethyl]sulfamoyl)benzyl]phenyl]propanoic acid
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(3-cyclohexylpropanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(4-oxopentanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(5-oxohexanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(6-oxoheptanoyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(cycloheptylcarbonyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(cyclopentylcarbonyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-(ethoxyacetyl)-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-hexanoyl-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-pentanoyl-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-pentanoyl-N-pyrazin-2-ylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-pentanoyl-N-pyridin-3-ylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-[(3,3-dihydroxycyclobutyl)carbonyl]-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-1-[4-(dimethylamino)-4-oxobutanoyl]-N-(pyridin-3-ylmethyl)piperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-(1-oxidopyridin-3-yl)-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-(1H-imidazol-4-ylmethyl)-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-(2,5-dihydro-1H-imidazol-5-ylmethyl)-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-isoxazol-5-yl-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N-[2-(1H-imidazol-4-yl)ethyl]-1-pentanoylpiperazine-2-carboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-(1-methylethyl)-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-(2-methylpropyl)-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-(cyclohexylmethyl)-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-butyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cycloheptyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[(3,5-dimethylisoxazol-4-yl)methyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[2-(1-methyl-1H-imidazol-5-yl)ethyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[2-(1H-imidazol-4-yl)ethyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[2-(6-methylpyridin-3-yl)ethyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[3-(1H-imidazol-4-yl)propyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclohexyl-N2-[3-(2-oxopyrrolidin-1-yl)propyl]piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclopentyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-cyclopropyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-propyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-N1-tert-butyl-N2-(pyridin-3-ylmethyl)piperazine-1,2-dicarboxamide
-
-
4-cyano-3-(3,4-dihydroxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(3-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(4-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(4-methoxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(dibenzo[b,d]furan-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-(naphthalen-2-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-3-[3-(methoxycarbonyl)phenyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophene-2-carboxylic acid
-
-
4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylic acid
-
-
4-oxo-4-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]butanoic acid
-
-
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(5-oxido-7-propyl-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(7-butyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
-
-
4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile
binds into the CAAX peptide site and competes with the CAAX substrate of FTase
4-[5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1,2-oxazol-3-yl]-N,N-dimethylaniline
in a model structure, the dimethylamine is in front of the zinc atom. The conformation is stabilized by two well-conserved hydrogen bond groups, one from the triazine to Arg 702
4-[[4-([[4-(4-chlorophenyl)-3-ethynylthiophen-2-yl]amino]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
-
-
4-[[5-([4-[7-(3-morpholin-4-ylpropyl)-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl]azepan-1-yl]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
-
-
5,9,13-trimethyl-8,12-tetradecadiene-2,3-dione
-
0.093 mM causes a 94% reduction in enzyme activity after 30 min
5,9-dimethyl-8-decene-2,3-dione
-
0.017 mM causes a 62% reduction in enzyme activity after 30 min
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-(4-methoxyphenyl)pyrrolidin-2-thione
in S-configuration, the compound binds rather low in the site of the enzyme, at the end of the farnesyldiphosphate far from the zinc. In R-configuration, there is a hydrogen bond between one the methoxy groups and Arg 702
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-[3-(trifluoromethyl)phenyl]pyrrolidine-2-thione
-
5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylic acid
-
-
5-oxo-5-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]pentanoic acid
-
-
5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
-
-
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
-
-
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
-
-
5-[4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-2-[(pyridin-3-ylmethyl)carbamoyl]piperazin-1-yl]-5-oxopentyl acetate
-
-
6-[(4-hydroxyphenyl)(1H-imidazol-1-yl)methyl]-4-phenyl-1,2-dihydroquinolin-2-ol
-
-
di-tert-butyl 2-[(2E,6E,10E)-1,3,7-trimethyl-1-(1-methyl-1H-imidazol-2-yl)dodeca-2,6,10-trien-1-yl]butanedioate
-
-
ethyl (2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-1-[2-(methylsulfanyl)ethyl]hydrazinyl)acetate
-
-
ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
-
-
ethyl 4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
-
-
ethyl 4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylate
-
-
ethyl 5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylate
-
-
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
-
-
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
-
-
ethyl [[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetate
-
-
KTSCVAM
-
40% inhibition of farnesylation in Toxoplasma gondii, 100% inhibition of enzyme in HeLa cells
KTSCVFM
-
80% inhibition of farnesylation in Toxoplasma gondii and 80% inhibition of enzyme in HeLa cells
KTSCVIA
-
50% inhibition of farnesylation in Toxoplasma gondii and no inhibition of enzyme in HeLa cells
KTSCVIF
-
no inhibition of farnesylation in Toxoplasma gondii, 80% inhibition of enzyme in HeLa cells
KTSSVIM
-
80% inhibition of farnesylation in Toxoplasma gondii, 100% inhibition of enzyme in HeLa cells
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
a selective peptidomimetic enzme inhibitor
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-phenylalaninate
-
-
methyl N-([3-[methyl(1-methylidene-2,3-disulfanylpropyl)amino]-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-1-yl]acetyl)methioninate
-
-
methyl N-([5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophen-2-yl]carbonyl)-L-methioninate
-
-
methyl N-[(6E)-2-benzyl-5-(1-methylethyl)-8-(sulfanylmethyl)dec-6-enoyl]methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methioninate
-
-
methyl N-[[3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[4-cyano-3-(3,4-dihydroxyphenyl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]-L-methioninate
-
-
methyl N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methioninate
-
-
N'-[(1Z)-1-(3-hydroxy-1-oxo-1H-inden-2-yl)ethylidene]-3-(10H-phenothiazin-10-yl)propanehydrazide
-
-
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-1-methyl-1H-imidazole-4-sulfonamide
-
-
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-2-methylbenzenesulfonamide
-
-
N-([2-[(1E,6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-1,6,10,14-tetraen-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
-
-
N-([2-[(6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-6,10,14-trien-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
-
-
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-D-methionine
-
-
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-L-methionine
-
-
N-[2-([2-[(2-amino-3-sulfanylpropyl)amino]-3-methylbutyl]amino)-3-phenylpropyl]methionine
-
-
N-[2-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]acetyl]amino)-3-methylpentyl]-N-(naphthalen-1-ylmethyl)glycylmethionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-N-methyl-D-methionine
-
-
N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methionine
-
-
N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methionine
-
-
N2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-glutamine
-
-
Na-[(3S)-3-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-phenylbutanoyl]-L-phenylalaninamide
-
-
tert-butyl (2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoate
-
-
tert-butyl 4-(3-bromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl)-2-[(pyridin-3-ylmethyl)carbamoyl]piperazine-1-carboxylate
-
-
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(1-methyl-1H-imidazol-4-yl)sulfonyl]amino]propyl)piperidine-1-carboxylate
-
-
-
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(2-methylphenyl)sulfonyl]amino]propyl)piperidine-1-carboxylate
-
-
Zn2+
inhibition of human farnesyltransferase by zinc complexation can be improved with triazine-isoxazole moieties. The replacement of the isoxazole unit by a pyrrolidin-2-one is detrimental to the inhibitory activity while the pyrrolidin-2-thione derivatives conserves the biological potential
[3-(1-methyl-1H-imidazol-2-yl)propyl][(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
-
-
[[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetic acid
-
-
BMS-214662
bind into the CAAX peptide site and compete with the CAAX substrate of FTase
BMS-214662
bind into the CAAX peptide site and compete with the CAAX substrate of FTase
lonafarnib
active in Ras-dependent and -independent malignant tumors
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
-
higher concentrations of the alpha-dicarbonyl compound results in more rapid and more extensive inactivation
-
additional information
-
addition of a methionine residue at position 2 of 3-arylthiophenes greatly improves enzyme inhibition, antiparasitic effect of the compounds on proliferation of 4 protozoan parasites, i.e. Plasmodium falciparum, Trypanosoma brucei brucei, Trypanosoma cruzi and Leishmania donovani, overview. No inhibition by 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)-N-(adamant-1-ylmethyl)thiophene-2-carboxamide, 3-(4-chlorophenyl)-4-cyano-N-(naphthalen-1-ylmethyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide, methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-N-methyl-D-methioninate, ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate, and methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
inhibition mechanisms for FTase and GGTase-I, EC 2.5.1.59, are different. Two classes of FTase enzyme inhibitors, bisubstrate imidazole-containing derivatives linked by an acidic substituent and a peptidyl chain and peptidomimetic molecules, which can be divided into two groups, namely thiol and non-thiol compounds. Molecular modeling studies of FTase and protein-inhibitor interactions, overview
-
additional information
-
introduction of an N-benzylimidazole moiety on protein farnesyltransferase inhibitors highly improves their antiparasitic activity against parasite cell proliferation, e.g. of Plasmodium falciparum, Leishmania donovani, Trypanosoma cruzi, and Trypanosoma brucei, overview. Generally compounds of the arylthiophene series are not very active on Plasmodium falciparum. No inhibition by ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate and methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
-
additional information
-
synthesis of a family of 30 benzoylated N-ylides and evaluation for the inhibitory activity on human protein farnesyltransferase. Most of these novel compounds posses in vitro inhibition potencies in the micromolar range. The nature of the substituents on the pyridine and phenyl units proves to be important in determining inhibitory activity and generally, the replacement of the cyanoacrylonitrile function by a cyanoethylacrylate group decreases the biological potential on farnesyltransferase, structure-activity relationship, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
dansyl-GCVDS
-
Km value clearly above 0.01 mM, wild-type, pH 7.8, 25°C
additional information
dansyl-GCVKS
-
Km value clearly above 0.01 mM, wild-type, pH 7.8, 25°C
additional information
additional information
-
comparison of Km of mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
comparison of kcat of mutant enzymes
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00024
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
Homo sapiens
pH and temperature not specified in the publication
0.0065
(2E)-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]butanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.13
(2E,4E,8E)-5,9,13-trimethyltetradeca-2,4,8,12-tetraenoic acid
Homo sapiens
-
30°C, pH 7.5
0.012 - 0.175
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
0.000016
(2Z,6E)-3-(3-methylbut-2-enyl)-7,11-dimethyldodeca-2,6,10-triene monophosphate
Homo sapiens
-
IC50: 16 nM
0.000013
(2Z,6E)-3-tert-butyl-7,11-dimethyldodeca-2,6,10-triene monophosphate
Homo sapiens
-
IC50: 13 nM
0.5
(4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-4,8,12-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.2
(4E,8E)-5,9,13-trimethyl-N-(phenylsulfonyl)tetradeca-4,8,12-trienamide
Homo sapiens
-
value above, 30°C, pH 7.5
0.2
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienamide
Homo sapiens
-
value above, 30°C, pH 7.5
0.17
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.0104
(4S)-4-([[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]amino)-5-tert-butoxy-5-oxopentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.2
(6E,10E)-7,11,15-trimethyl-3-oxohexadeca-6,10,14-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.06
(7E,11E)-8,12,16-trimethyl-4-oxoheptadeca-7,11,15-trienoic acid
Homo sapiens
-
30°C, pH 7.5
0.0259
1-(1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4,4-dicyano-1-oxobut-3-en-2-yl)-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.000024
1-(1H-imidazol-5-ylmethyl)-7-pyridin-4-yl-4-[[2-(trifluoromethoxy)phenyl]carbonyl]-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine
Homo sapiens
-
-
0.0462
1-(4,4-dicyano-1-oxo-1-phenylbut-3-en-2-yl)-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0364
1-[(3Z)-1-(4-bromophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0319
1-[(3Z)-1-(4-chlorophenyl)-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
55.22
1-[(3Z)-1-[3,4-bis[(hydroxyacetyl)amino]phenyl]-4-cyano-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0208
1-[(3Z)-4-cyano-1-(3,4-dimethoxyphenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-methoxypyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0239
1-[(3Z)-4-cyano-1-(4-cyanophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0623
1-[(3Z)-4-cyano-1-(4-fluorophenyl)-5,5-dihydroxy-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0627
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methoxyphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0436
1-[(3Z)-4-cyano-5,5-dihydroxy-1-(4-methylphenyl)-1-oxohept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0435
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-2,4-dimethylpyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.048
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-(3,4,5-trimethoxyphenyl)hept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0309
1-[(3Z)-4-cyano-5,5-dihydroxy-1-oxo-1-phenylhept-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0197
1-[1-(4-bromophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0125
1-[1-(4-chlorophenyl)-4,4-dicyano-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0314
1-[4,4-dicyano-1-(3,4-dimethoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0462
1-[4,4-dicyano-1-(4-cyanophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0236
1-[4,4-dicyano-1-(4-fluorophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0274
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-2,4-dimethylpyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0222
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0273
1-[4,4-dicyano-1-(4-methoxyphenyl)-1-oxobut-3-en-2-yl]-3-methoxypyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0145
1-[4,4-dicyano-1-(4-methylphenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0282
1-[4,4-dicyano-1-(4-nitrophenyl)-1-oxobut-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0201
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-2,4-dimethylpyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0156
1-[4,4-dicyano-1-oxo-1-(3,4,5-trimethoxyphenyl)but-3-en-2-yl]-3-(dimethylamino)pyridinium
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
18-oxa-2,5,9,11-tetraazahexacyclo[17.6.2.22,5.113,17.07,11.022,26]triaconta-1(26),7,9,13(28),14,16,19,21,22,24,26-undecaene-16-carbonitrile
Homo sapiens
-
-
0.000001
2-amino-3-[2-butyl-4-(naphthalen-1-ylcarbonyl)piperazin-1-yl]propane-1-thiol
Homo sapiens
-
IC50 less than 0.000001 mM
0.59
2-[(2E)-3,7-dimethyl-1-(1-methyl-1H-imidazol-2-yl)octa-2,6-dien-1-yl]butanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.0054
2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]butanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.000001
29-oxo-18-oxa-2,6,9,11-tetraazahexacyclo[17.5.3.12,5.113,17.07,11.022,26]nonacosa-7,9,13(28),14,16,19,21,26-octaene-16-carbonitrile
Homo sapiens
-
IC50 less than 0.000001 mM
0.016
3-(4-chlorophenyl)-4-cyano-5-(isopropylthio)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.05
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)-N-adamantylthiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0019
3-(4-chlorophenyl)-4-cyano-N'-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carbohydrazide
Homo sapiens
-
pH and temperature not specified in the publication
0.0216
3-(4-chlorophenyl)-4-cyano-N-(naphthalen-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.024
3-(4-chlorophenyl)-4-cyano-N-[2-(methylsulfanyl)ethyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.022
3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00097
3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.0033
3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00335
3-methyl-2-[2-oxo-2-(10H-phenothiazin-10-yl)ethyl]indeno[1,2-c]pyrazol-4(2H)-one
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.16
3-oxo-3-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanoic acid
Homo sapiens
-
30°C, pH 7.5
0.0008
3-[3-[2-([2-[1-(tert-butoxycarbonyl)piperidin-4-yl]-1-([(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]methyl)ethyl]sulfamoyl)benzyl]phenyl]propanoic acid
Homo sapiens
-
-
0.039
4-cyano-3-(3-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.02
4-cyano-3-(4-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.007
4-cyano-3-(4-methoxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.015
4-cyano-3-(dibenzo[b,d]furan-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.0055
4-cyano-3-(naphthalen-2-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.0048
4-cyano-3-[3-(methoxycarbonyl)phenyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00001
4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.13
4-oxo-4-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]butanoic acid
Homo sapiens
-
30°C, pH 7.5
0.000285
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.00031
4-[(5-[[4-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.0000465
4-[(5-[[4-(5-oxido-7-propyl-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.000043
4-[(5-[[4-(7-butyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.0000448
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)azepan-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.000045
4-[(5-[[4-(7-methyl-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl)piperidin-1-yl]methyl]-1H-imidazol-1-yl)methyl]benzonitrile
Homo sapiens
-
-
0.0373
4-[5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1,2-oxazol-3-yl]-N,N-dimethylaniline
Homo sapiens
pH 7.5, 30°C
0.0051
4-[[4-([[4-(4-chlorophenyl)-3-ethynylthiophen-2-yl]amino]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
pH 7.5, 30°C
0.0000173
4-[[5-([4-[7-(3-morpholin-4-ylpropyl)-5-oxido-7,12-dihydrodibenzo[c,f][1,2,8]oxathiazocin-12-yl]azepan-1-yl]methyl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
-
0.0038
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-(4-methoxyphenyl)pyrrolidin-2-thione
Homo sapiens
pH 7.5, 30°C
0.0411
5-(4,6-dimethoxy-1,3,5-triazin-2-yl)-1-[3-(trifluoromethyl)phenyl]pyrrolidine-2-thione
Homo sapiens
pH 7.5, 30°C
0.02
5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophene-2-carboxylic acid
Homo sapiens
-
about, pH and temperature not specified in the publication
0.00037
5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.06
5-oxo-5-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]pentanoic acid
Homo sapiens
-
30°C, pH 7.5
0.00064
5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00038
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00098
5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.00018
6-[(4-hydroxyphenyl)(1H-imidazol-1-yl)methyl]-4-phenyl-1,2-dihydroquinolin-2-ol
Homo sapiens
-
-
0.7
di-tert-butyl 2-[(2E,6E,10E)-1,3,7-trimethyl-1-(1-methyl-1H-imidazol-2-yl)dodeca-2,6,10-trien-1-yl]butanedioate
Homo sapiens
-
30°C, pH 7.5
0.05
ethyl (2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-1-[2-(methylsulfanyl)ethyl]hydrazinyl)acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.0372
ethyl 3-(2,5-dimethoxyphenyl)-1,2-oxazole-5-carboxylate
Homo sapiens
pH 7.5, 30°C
0.021
ethyl 3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.0012
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.1
ethyl 3-(4-chlorophenyl)-4-ethynyl-5-[(1H-imidazol-4-ylacetyl)amino]thiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.034
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.000013
ethyl 3-(4-chlorophenyl)-5-([[1-(4-cyanobenzyl)-1H-imidazol-4-yl]methyl][[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00019
ethyl 4-ethynyl-5-([[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino)-3-phenylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00013
ethyl 5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00029
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.00033
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-4-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.0021
ethyl 5-[(tert-butoxycarbonyl)[[1-(4-nitrobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophene-2-carboxylate
Homo sapiens
-
pH 7.5, 30°C
0.0093
ethyl [[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.00024
methyl (2S)-2-([(2S)-2-[(2-[[(2R)-2-amino-3-sulfanylpropyl]amino]-3-methylpentyl)oxy]-3-phenylpropanoyl]amino)-4-(methylsulfonyl)butanoate
Homo sapiens
pH and temperature not specified in the publication
0.000022
methyl N-(1-[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]piperidin-4-yl)-N-(phenylcarbonyl)-L-phenylalaninate
Homo sapiens
-
-
0.00068
methyl N-([5-[(tert-butoxycarbonyl)[[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino]-3-(4-chlorophenyl)-4-ethynylthiophen-2-yl]carbonyl)-L-methioninate
Homo sapiens
-
pH 7.5, 30°C
0.00046
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
methyl N-[[3-(4-chlorophenyl)-4-ethynyl-5-(2l5-triaz-1-en-2-yn-1-yl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH 7.5, 30°C
0.023
methyl N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
methyl N-[[4-cyano-3-(3,4-dihydroxyphenyl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.0056
methyl N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.05
methyl N-[[5-(butan-2-yl)-3-(4-chlorophenyl)-4-cyanothiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
methyl N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methioninate
Homo sapiens
-
pH 7.5, 30°C
0.00373
N'-[(1Z)-1-(3-hydroxy-1-oxo-1H-inden-2-yl)ethylidene]-3-(10H-phenothiazin-10-yl)propanehydrazide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000056
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-1-methyl-1H-imidazole-4-sulfonamide
Homo sapiens
-
-
0.00016
N-(1-benzyl-2-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]ethyl)-2-methylbenzenesulfonamide
Homo sapiens
-
-
0.00064
N-([2-[(1E,6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-1,6,10,14-tetraen-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
Homo sapiens
-
30°C, pH 7.5
0.00024
N-([2-[(6E,10E)-4-carboxy-4-(ethoxycarbonyl)-7,11,15-trimethylhexadeca-6,10,14-trien-1-yl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methionine
Homo sapiens
-
30°C, pH 7.5
0.000112
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.000075
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
Homo sapiens
-
-
0.000053
N-([5-[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.000053
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-D-methionine
Homo sapiens
-
-
0.000055
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methoxybiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.00005
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-D-methionine
Homo sapiens
-
-
0.000045
N-([5-[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethoxy]-2'-methylbiphenyl-2-yl]carbonyl)-L-methionine
Homo sapiens
-
-
0.843
N-[(5-[[(2R)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
Homo sapiens
-
-
0.302
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-D-methionine
Homo sapiens
-
-
0.151
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methoxybiphenyl-2-yl)carbonyl]-L-methionine
Homo sapiens
-
-
0.012
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-D-methionine
Homo sapiens
-
-
0.016
N-[(5-[[(2S)-2,3-dihydro-1,4-benzodioxin-2-ylmethyl]carbamoyl]-2'-methylbiphenyl-2-yl)carbonyl]-L-methionine
Homo sapiens
-
-
0.0000021
N-[2-([2-[(2-amino-3-sulfanylpropyl)amino]-3-methylbutyl]amino)-3-phenylpropyl]methionine
Homo sapiens
-
-
0.00000015
N-[2-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]acetyl]amino)-3-methylpentyl]-N-(naphthalen-1-ylmethyl)glycylmethionine
Homo sapiens
-
-
0.0017
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonothioyl]-D-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.00045
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-D-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.0019
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-isoleucyl-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.000067 - 0.000077
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
0.0018
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-N-methyl-D-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.000042
N-[[3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
N-[[4-cyano-3-(dibenzo[b,d]furan-4-yl)-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.0087
N-[[4-cyano-5-(propan-2-ylsulfanyl)-3-(3,4,5-trihydroxyphenyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.0036
N-[[5-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-ethynyl-3-phenylthiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH 7.5, 30°C
0.000076
N2-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-glutamine
Homo sapiens
-
pH and temperature not specified in the publication
0.0000285
Na-[(3S)-3-([[1-(4-cyanobenzyl)-1H-imidazol-5-yl]methyl]amino)-4-phenylbutanoyl]-L-phenylalaninamide
Homo sapiens
-
-
0.3
tert-butyl (2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoate
Homo sapiens
-
30°C, pH 7.5
0.0037
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(1-methyl-1H-imidazol-4-yl)sulfonyl]amino]propyl)piperidine-1-carboxylate
Homo sapiens
-
-
-
0.00405
tert-butyl 4-(3-[(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino]-2-[[(2-methylphenyl)sulfonyl]amino]propyl)piperidine-1-carboxylate
Homo sapiens
-
-
0.0009
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.00088
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.085
[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]sulfamic acid
Homo sapiens
-
30°C, pH 7.5
0.021
[3-(1-methyl-1H-imidazol-2-yl)propyl][(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.01
[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.06
[[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]amino]propanedioic acid
Homo sapiens
-
30°C, pH 7.5
0.0037
[[2-([[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]amino)ethyl]sulfanyl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.012
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
Homo sapiens
-
30°C, pH 7.5
0.175
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
Homo sapiens
-
30°C, pH 7.5
0.016
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH 7.5, 30°C
0.016
3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000067
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
0.000077
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH 7.5, 30°C
0.000077
N-[[3-(4-chlorophenyl)-4-cyano-5-(propan-2-ylsulfanyl)thiophen-2-yl]carbonyl]-L-methionine
Homo sapiens
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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. Enzyme deficiency is involved in progeria, also known as Hutchinson-Gilford progeria syndrome, a fatal and rare genetic disease caused by the mutation of the LMNA gene
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. FTase is involvedin hematologic malignancies due via prenylation of Ras. The enzyme is also important in the pathological process of neurological diseases, such as neuroinflammatory disease and Parkinson's disease
physiological function
-
posttranslational modification of proteins involved in intracellular signal transduction network
additional information
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). FNTB_HUMAN
437
0
48774
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
additional information
additional information
the alpha-subunit does not form homodimers. Crosslinking experiments reveal farnesyltransferase alpha-subunit trimers and higher oligomerization states
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
FTase in ternary complexes with an FPP analog and peptides derived from the cognate substrates H-Ras (GCVLS) and Rap2a (DDPTA-SACNIQ), the cross-reactive substrate TC21 (KKSKTKCVIF), and the non-substrate Rap2b (TKCVIL). Structures of GGTase-I in ternary complexes with a GGPP analog (3'azaGGPP) and peptides derived from the cognate substrates Cdc42 splice isoform 2 (RRCVLL Ca1a2X motif) and the heterotrimeric G protein g2 subunit (FREKKFFCAIL), and the cross-reactive substrates RhoB (GCINCCKVL), K-Ras4B (KKKSKTKCVIM) and TC21
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D200N
-
decrease of protein substrate affinity without affecting the affinity for farnesyl diphosphate substrates
G249V
-
decrease in the affinity of both protein and farnesyl diphosphate substrates
G349S
-
decrease of protein substrate affinity without affecting the affinity for farnesyl diphosphate substrates
W102F/W106E
-
mutations in the beta-subunit. Mutations relax substrate selectivity without loss of activity
W102L/W106E
-
mutations in the beta-subunit. Mutations relax substrate selectivity without loss of activity
W102L/W106R
-
mutations in the beta-subunit. Mutations relax substrate selectivity without loss of activity
W102R/W106K
-
mutations in the beta-subunit. Mutations relax substrate selectivity without loss of activity
W102R/W106L
-
mutations in the beta-subunit. Mutations relax substrate selectivity without loss of activity
Y300F
-
the mutation adversely affects the reaction rate constant by 500fold under optimal catalytic conditions
additional information
additional information
-
H248beta, R291beta, K294beta, W303beta involved with the binding and utilization of the farnesyl diphophate substrate, mutations in R202beta affect the binding of the protein substrate
additional information
complex of HDAC6-microtubule directly bind to alpha subunit of FTase
additional information
-
complex of HDAC6-microtubule directly bind to alpha subunit of FTase
additional information
FTalphaKD, stable knockdown of the alpha subunit of FTase
additional information
-
FTalphaKD, stable knockdown of the alpha subunit of FTase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
the enzyme is a promising therapeutic target for the treatment of various Ras-induced cancers and several other kinds of diseases
medicine
pharmacology
the enzyme is a promising therapeutic target for the treatment of various Ras-induced cancers and several other kinds of diseases
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
-
possibility of development of specific inhibitors for parasitic protozoa
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, H.W.; Beese, L.S.
Protein farnesyltransferase
Curr. Opin. Struct. Biol.
7
873-880
1997
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
Okolotowicz, K.J.; Lee, W.J.; Hartman, R.F.; Kim, A.Y.; Ottersberg, S.R.; Robinson, D.E., Jr.; Lefler, S.R.; Rose, S.D.
Inactivation of protein farnesyltransferase by active-site-targeted dicarbonyl compounds
Arch. Pharm.
334
194-202
2001
Homo sapiens
Ibrahim, M.; Azzouz, N.; Gerold, P.; Schwarz, R.T.
Identification and characterisation of Toxoplasma gondii protein farnesyltransferase
Int. J. Parasitol.
31
1489-1497
2001
Homo sapiens, Toxoplasma gondii
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
Reid, T.S.; Long, S.B.; Beese, L.S.
Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes
Biochemistry
43
9000-9008
2004
Homo sapiens
Maurer-Stroh, S.; Washietl, S.; Eisenhaber, F.
Protein prenyltransferases
Genome Biol.
4
212
2003
Homo sapiens
Reid, T.S.; Terry, K.L.; Casey, P.J.; Beese, L.S.
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
J. Mol. Biol.
343
417-433
2004
Homo sapiens
Henriksen, B.S.; Zahn, T.J.; Evanseck, J.D.; Firestine, S.M.; Gibbs, R.A.
Computational and conformational evaluation of FTase alternative substrates: insight into a novel enzyme binding pocket
J. Chem. Inf. Model.
45
1047-1052
2005
Homo sapiens
Lane, K.T.; Beese, L.S.
Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I
J. Lipid Res.
47
681-699
2006
Homo sapiens
Clark, M.K.; Scott, S.A.; Wojtkowiak, J.; Chirco, R.; Mathieu, P.; Reiners, J.J.; Mattingly, R.R.; Borch, R.F.; Gibbs, R.A.
Synthesis, biochemical, and cellular evaluation of farnesyl monophosphate prodrugs as farnesyltransferase inhibitors
J. Med. Chem.
50
3274-3282
2007
Homo sapiens
Cui, G.; Merz, K.M.
Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate
Biochemistry
46
12375-12381
2007
Homo sapiens
Gilleron, P.; Wlodarczyk, N.; Houssin, R.; Farce, A.; Laconde, G.; Goossens, J.F.; Lemoine, A.; Pommery, N.; Henichart, J.P.; Millet, R.
Design, synthesis and biological evaluation of substituted dioxodibenzothiazepines and dibenzocycloheptanes as farnesyltransferase inhibitors
Bioorg. Med. Chem. Lett.
17
5465-5471
2007
Homo sapiens
Bolchi, C.; Pallavicini, M.; Rusconi, C.; Diomede, L.; Ferri, N.; Corsini, A.; Fumagalli, L.; Pedretti, A.; Vistoli, G.; Valoti, E.
Peptidomimetic inhibitors of farnesyltransferase with high in vitro activity and significant cellular potency
Bioorg. Med. Chem. Lett.
17
6192-6196
2007
Homo sapiens
Braun, T.; Fenaux, P.
Farnesyltransferase inhibitors and their potential role in therapy for myelodysplastic syndromes and acute myeloid leukaemia
Br. J. Haematol.
141
576-586
2008
Homo sapiens
Nguyen, U.T.; Cramer, J.; Gomis, J.; Reents, R.; Gutierrez-Rodriguez, M.; Goody, R.S.; Alexandrov, K.; Waldmann, H.
Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization
Chembiochem
8
408-423
2007
Homo sapiens
Equbal, T.; Silakari, O.; Ravikumar, M.
Exploring three-dimensional quantitative structural activity relationship (3D-QSAR) analysis of SCH 66336 (Sarasar) analogues of farnesyltransferase inhibitors
Eur. J. Med. Chem.
43
204-209
2008
Homo sapiens
Iwasaki, S.; Omura, S.
Search for protein farnesyltransferase inhibitors of microbial origin: our strategy and results as well as the results obtained by other groups
J. Antibiot.
60
1-12
2007
Homo sapiens
Puntambekar, D.S.; Giridhar, R.; Yadav, M.R.
Inhibition of farnesyltransferase: a rational approach to treat cancer?
J. Enzyme Inhib. Med. Chem.
22
127-140
2007
Homo sapiens
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
-
Duez, S.; Coudray, L.; Mouray, E.; Grellier, P.; Dubois, J.
Towards the synthesis of bisubstrate inhibitors of protein farnesyltransferase: Synthesis and biological evaluation of new farnesylpyrophosphate analogues
Bioorg. Med. Chem.
18
543-556
2010
Saccharomyces cerevisiae, Homo sapiens, Plasmodium falciparum, Trypanosoma brucei
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
Zhou, J.; Vos, C.C.; Gjyrezi, A.; Yoshida, M.; Khuri, F.R.; Tamanoi, F.; Giannakakou, P.
The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner
J. Biol. Chem.
284
9648-9655
2009
Homo sapiens (P49354), Homo sapiens
Coudray, L.; de Figueiredo, R.M.; Duez, S.; Cortial, S.; Dubois, J.
Synthesis of imidazole-containing analogues of farnesyl pyrophosphate and evaluation of their biological activity on protein farnesyltransferase
J. Enzyme Inhib. Med. Chem.
24
972-985
2009
Saccharomyces cerevisiae, Homo sapiens, Plasmodium falciparum
Baciu-Atudosie, L.; Ghinet, A.; Farce, A.; Dubois, J.; Belei, D.; Bicu, E.
Synthesis and biological evaluation of new phenothiazine derivatives bearing a pyrazole unit as protein farnesyltransferase inhibitors
Bioorg. Med. Chem. Lett.
22
6896-6902
2012
Homo sapiens
Hougland, J.L.; Gangopadhyay, S.A.; Fierke, C.A.
Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: development of bioengineered prenylation pathways
J. Biol. Chem.
287
38090-38100
2012
Homo sapiens
Lethu, S.; Bosc, D.; Mouray, E.; Grellier, P.; Dubois, J.
New protein farnesyltransferase inhibitors in the 3-arylthiophene 2-carboxylic acid series: diversification of the aryl moiety by solid-phase synthesis
J. Enzyme Inhib. Med. Chem.
28
163-171
2013
Saccharomyces cerevisiae, Homo sapiens, Trypanosoma brucei
Abuhaie, C.M.; Ghinet, A.; Farce, A.; Dubois, J.; Rigo, B.; Bicu, E.
Synthesis and biological evaluation of a new series of N-ylides as protein farnesyltransferase inhibitors
Bioorg. Med. Chem. Lett.
23
5887-5892
2013
Homo sapiens
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)
Bosc, D.; Mouray, E.; Cojean, S.; Franco, C.H.; Loiseau, P.M.; Freitas-Junior, L.H.; Moraes, C.B.; Grellier, P.; Dubois, J.
Highly improved antiparasitic activity after introduction of an N-benzylimidazole moiety on protein farnesyltransferase inhibitors
Eur. J. Med. Chem.
109
173-186
2016
Homo sapiens, Trypanosoma brucei
Bosc, D.; Mouray, E.; Grellier, P.; Cojean, S.; Loiseau, P.; Dubois, J.
Introduction of methionine mimics on 3-arylthiophene: Influence on protein farnesyltransferase inhibition and on antiparasitic activity
MedChemComm
4
1034-1041
2013
Homo sapiens, Trypanosoma brucei
-
Lucescu, L.; Ghinet, A.; Shova, S.; Magnez, R.; Thuru, X.; Farce, A.; Rigo, B.; Belei, D.; Dubois, J.; Bicu, E.
Exploring isoxazoles and pyrrolidinones decorated with the 4,6-dimethoxy-1,3,5-triazine unit as human farnesyltransferase inhibitors
Arch. Pharm.
352
e1800227
2019
Homo sapiens (P49354 and P49356)
EXTERNAL LINKS (specific for EC-Number 2.5.1.58)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
