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Information on EC 2.5.1.58 - protein farnesyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P29703
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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
-
farnesylation
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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: Saccharomyces cerevisiae
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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-
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farnesyl protein transferase
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-
-
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farnesyltransferase
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-
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farnesyltransferase, farnesyl pyrophosphate-protein
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-
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farnesyltransferase, protein
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-
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FPT
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-
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fptase
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FTase
PFT
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-
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PFTase
prenylprotein transferase
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-
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prenyltransferase
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protein cysteine farnesyltransferase
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protein farnesyltransferase
protein prenyltransferase
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-
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RAS farnesyltransferase
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-
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FTase
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-
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protein farnesyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
kinetic mechanism
-
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
enzyme constitutes the protein prenyltransferase family of enzymes
-
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
The enzyme preferentially farnesylates CaaX sequences ending in methionine, cysteine or serine. Enzyme also attaches geranylgeraniol to some CaaX sequences ending in methionine, leucine and cysteine. Substrate overlap may occur between the Saccharomyces cerevisae farnesyl transferase and geranylgeranyltransferase types I in vivo
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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
-
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
(1E)-1-[(2E,6E,10E)-12-azido-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]-2-oxodiphosphane + protein-cysteine
?
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + (protein)-L-cysteine
S-(2E,6E)-farnesyl protein + diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + dansyl-GCVLS
dansyl-G-(S-(2E,6E)-farnesyl)CVLS + diphosphate
-
assay at pH 7.5, 30°C
-
-
?
12-propargoxyfarnesyl diphosphate + N-dansyl-Gly-Cys-Val-Ile-Ala-OH
diphosphate + propargoxyfarnesyl N-dansyl-Gly-Cys-Val-Ile-Ala-OH
-
-
-
-
?
3-(azidomethyl)-N-[(2E,6E,8E)-2,6-dimethyl-8-(oxodiphosphanylidene)octa-2,6-dien-1-yl]aniline + protein-cysteine
?
-
-
-
-
?
3-(azidomethyl)-N-[(4E,8E,10E)-4,8-dimethyl-10-(oxodiphosphanylidene)deca-4,8-dien-1-yl]aniline + protein-cysteine
?
-
-
-
-
?
dansyl-GCVIA + (2E,6E)-farnesyl diphosphate
dansyl-G-(S-(2E,6E)-farnesyl)CVIA + diphosphate
-
100% enzyme activity, specific activity 0.765 microM/min
-
-
?
dansyl-GCVIA + 1-(4,5-dimethoxy-nitrophenyl)ethyl (2E,6E)-farnesyl diphosphate
?
-
7.6% enzyme activity, specific activity 0.058 microM/min
-
-
?
dansyl-GCVIA + 2-nitrophenyl (2E,6E)-farnesyl diphosphate
?
-
14% enzyme activity, specific activity 0.104 microM/min
-
-
?
farnesyl diphosphate + dansyl-GCVLS
diphosphate + S-farnesyl dansyl-GCVLS
-
-
-
-
?
farnesyl diphosphate + GST-CIIL
diphosphate + S-farnesyl-GST-Cys-Ile-Ile-Ser
-
-
-
-
?
farnesyl diphosphate + GST-CIIS
?
-
GST-CIIS is glutathione S-transferase fused to the C-terminal 12 amino acids of yeast RAS2 protein
-
-
?
farnesyl diphosphate + [GST]-Cys-Ile-Ile-Ser
diphosphate + S-farnesyl-[GST]-Cys-Ile-Ile-Ser
-
-
-
-
?
geranyl alkyne diphosphate + N-dansyl-GCVIA
N-dansyl-G-(alkyne geranyl)CVIA + diphosphate
-
-
-
-
ir
[(4E,8E,10E)-4,8-dimethyl-10-(oxodiphosphanylidene)deca-4,8-dien-1-yl]oxyacetonitrile + protein-cysteine
?
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
?
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
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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
-
-
?
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
?
-
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
-
-
?
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
-
-
-
?
farnesyl diphosphate + protein-cysteine
diphosphate + S-farnesyl protein
-
-
-
-
?
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1aR,2S,3aS,6aR,7aR)-2,6-dimethyl-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
-
-
(1aR,2S,3aS,6aR,7aR)-2-methyl-6-methylidene-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
-
-
(1aS,2S,3aS,6aR,7aS)-2,6-dimethyl-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
-
-
(1aS,2S,3aS,6aR,7aS)-2-methyl-6-methylidene-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
-
-
(2E)-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]butanedioic acid
-
-
(2E)-3-[(3aR,7S,8aS)-3,7-dimethyl-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]-1-methylprop-2-en-1-yl acetate
-
-
(2E,4E,8E)-5,9,13-trimethyltetradeca-2,4,8,12-tetraenoic acid
-
-
(2Z)-3-(1H-imidazol-2-yl)-5-methylhexa-2,4-dienoic acid
-
8% inhibition at 0.001 M
(2Z)-5-methyl-3-(1-methyl-1H-imidazol-2-yl)hexa-2,4-dienoic acid
-
8% inhibition at 0.001 M
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
-
-
(3aR,7S,8aS)-3,7-dimethyl-6-[(1E)-3-oxobut-1-en-1-yl]-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
-
-
(3aR,7S,8aS)-6-[(1E)-3-hydroxybut-1-en-1-yl]-3,7-dimethyl-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
-
-
(3aR,7S,8aS)-7-methyl-3-methylidene-6-[(1E)-3-oxobut-1-en-1-yl]-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
-
-
(3aR,8S,9aS)-6-acetyl-3,8-dimethyl-3,3a,4,8,9,9a-hexahydro-2H-cyclohepta[1,2-b:4,5-b']difuran-2-one
-
-
(3R,3aR,7S,8aS)-3,7-dimethyl-6-(3-oxobutyl)-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
-
-
(3R,3aR,7S,8aS)-6-(3-hydroxybutyl)-3,7-dimethyl-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
-
-
(4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-4,8,12-trienoic acid
-
-
(4E,8E)-5,9,13-trimethyl-N-(phenylsulfonyl)tetradeca-4,8,12-trienamide
-
-
(E,E)-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene 1-diphosphate
-
-
(E,E)-8-O-(4-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene 1-diphosphate
-
-
1-[(3aR,7S,8aS)-3,7-dimethyl-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]-3-(1-hydroxyethoxy)butyl acetate
-
-
1-[(3aR,7S,8aS)-3,7-dimethyl-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]butane-1,3-diyl diacetate
-
-
1-[(3aR,7S,8aS)-7-methyl-3-methylidene-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]-3-oxobutyl acetate
-
-
1-[(3aR,7S,8aS)-7-methyl-3-methylidene-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]butane-1,3-diyl diacetate
-
-
2-[(2E)-3,7-dimethyl-1-(1-methyl-1H-imidazol-2-yl)octa-2,6-dien-1-yl]butanedioic acid
-
-
2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]butanedioic acid
-
-
3-(1H-imidazol-2-yl)-5-methylhex-4-enoic acid
-
21% inhibition at 0.001 M
3-(4-chlorophenyl)-4-cyano-1-methyl-5-[(1-methylethyl)sulfanyl]-1H-pyrrole-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-(cyclohexylsulfanyl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-(ethylsulfanyl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-(isopropylthio)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-(methylsulfanyl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-(morpholin-4-ylsulfanyl)thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]furan-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxamide
-
-
3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-[(1-methylpropyl)sulfanyl]thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-5-[(2-methylpropyl)sulfanyl]thiophene-2-carboxylic acid
-
-
3-(4-chlorophenyl)-4-cyano-N-cyclopropyl-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxamide
-
-
3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
-
-
3-hydroxy-1-[(3aR,7S,8aS)-7-methyl-3-methylidene-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]butyl acetate
-
-
3-oxo-3-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanoic acid
-
-
4-(4-chlorophenyl)-2-[(1-methylethyl)sulfanyl]-1,3-thiazole-5-carboxylic acid
-
-
4-(4-chlorophenyl)-5-(hydroxyacetyl)-2-[(1-methylethyl)sulfanyl]thiophene-3-carbonitrile
-
-
4-(4-chlorophenyl)-5-(methoxyacetyl)-2-[(1-methylethyl)sulfanyl]thiophene-3-carbonitrile
-
-
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-(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-oxo-4-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]butanoic acid
-
-
5-(butylsulfanyl)-3-(4-chlorophenyl)-4-cyanothiophene-2-carboxylic acid
-
-
5-acetyl-4-(4-chlorophenyl)-2-[(1-methylethyl)sulfanyl]thiophene-3-carbonitrile
-
-
5-methyl-3-(1-methyl-1H-imidazol-2-yl)hex-4-enoic acid
-
25% inhibition at 0.001 M
5-oxo-5-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]pentanoic acid
-
-
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 3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxylate
-
-
methyl N-([2-[4-ethoxy-2-(ethoxycarbonyl)-4-oxobutyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methioninate
-
-
methyl N-([2-[4-ethoxy-2-(ethoxycarbonyl)-4-oxobutyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-Lisoleucyl-L-alaninate
-
-
methyl N-([2-[5-ethoxy-3-(methoxycarbonyl)-5-oxopentyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-isoleucyl-L-alaninate
-
-
methyl N-([2-[5-ethoxy-3-(methoxycarbonyl)-5-oxopentyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methioninate
-
-
methyl N-([2-[6-ethoxy-4-(ethoxycarbonyl)-6-oxohexyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-isoleucyl-L-alaninate
-
-
methyl N-([2-[6-ethoxy-4-(ethoxycarbonyl)-6-oxohexyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methioninate
-
-
N-[[2-(2,3-dicarboxypropyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-isoleucyl-L-alanine
-
-
N-[[2-(2,3-dicarboxypropyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-phenylalanyl-L-methionine
-
-
N-[[2-(3,4-dicarboxybutyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-isoleucyl-L-alanine
-
-
N-[[2-(3,4-dicarboxybutyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-phenylalanyl-L-methionine
-
-
N-[[2-(4,5-dicarboxypentyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-phenylalanyl-L-methionine
-
-
N-[[2-(4,5-dicarboxypentyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-Lisoleucyl-L-alanine
-
-
tert-butyl (2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoate
-
-
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]propanedioic acid
-
-
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
-
-
[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]sulfamic acid
-
-
[3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophen-2-yl]methyl acetate
-
-
[[(2E,4E,8E)-5,9,13-trimethyltetradeca-2,4,8,12-tetraenoyl]amino]propanedioic acid
-
-
[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanedioic acid
-
-
[[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]amino]propanedioic acid
-
-
additional information
-
enzyme inhibited by peptides containing the C-terminal CAAX sequence
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
N-dansyl-GCVIA
-
in 50 mM Tris-HCl (pH 7.0) containing 10 mM MgCl2, 0.01 mM ZnCl2, 20 nM enzyme, and 5 mM DTT, at 30°C
0.00042
farnesyl diphosphate
-
in 50 mM Tris-HCl (pH 7.0) containing 10 mM MgCl2, 0.01 mM ZnCl2, and 20 nM enzyme, at 30°C
additional information
additional information
kinetic analysis
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.049
(E,E)-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene 1-diphosphate
-
-
0.045
(E,E)-8-O-(4-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene 1-diphosphate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
(1aR,2S,3aS,6aR,7aR)-2,6-dimethyl-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.1
(1aR,2S,3aS,6aR,7aR)-2-methyl-6-methylidene-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.066
(1aS,2S,3aS,6aR,7aS)-2,6-dimethyl-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.5
(1aS,2S,3aS,6aR,7aS)-2-methyl-6-methylidene-1a-[(1E)-3-oxobut-1-en-1-yl]octahydro-5H-oxireno[4,5]cyclohepta[1,2-b]furan-5-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.016
(2E)-2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylidene]butanedioic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.9
(2E)-3-[(3aR,7S,8aS)-3,7-dimethyl-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]-1-methylprop-2-en-1-yl acetate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.04
(2E,4E,8E)-5,9,13-trimethyltetradeca-2,4,8,12-tetraenoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.028 - 0.13
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
0.21
(3aR,7S,8aS)-3,7-dimethyl-6-[(1E)-3-oxobut-1-en-1-yl]-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
1
(3aR,7S,8aS)-6-[(1E)-3-hydroxybut-1-en-1-yl]-3,7-dimethyl-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
Saccharomyces cerevisiae
-
value above, 30°C, pH 7.5
0.1
(3aR,7S,8aS)-7-methyl-3-methylidene-6-[(1E)-3-oxobut-1-en-1-yl]-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
1
(3aR,8S,9aS)-6-acetyl-3,8-dimethyl-3,3a,4,8,9,9a-hexahydro-2H-cyclohepta[1,2-b:4,5-b']difuran-2-one
Saccharomyces cerevisiae
-
value above, 330°C, pH 7.5
0.24
(3R,3aR,7S,8aS)-3,7-dimethyl-6-(3-oxobutyl)-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
Saccharomyces cerevisiae
-
30°C, pH 7.5
1
(3R,3aR,7S,8aS)-6-(3-hydroxybutyl)-3,7-dimethyl-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-2-one
Saccharomyces cerevisiae
-
value above, 30°C, pH 7.5
0.7
(4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-4,8,12-trienoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.2
(4E,8E)-5,9,13-trimethyl-N-(phenylsulfonyl)tetradeca-4,8,12-trienamide
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.042
(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.08
(6E,10E)-7,11,15-trimethyl-3-oxohexadeca-6,10,14-trienoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.015
(7E,11E)-8,12,16-trimethyl-4-oxoheptadeca-7,11,15-trienoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.633
1-[(3aR,7S,8aS)-3,7-dimethyl-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]-3-(1-hydroxyethoxy)butyl acetate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.04
1-[(3aR,7S,8aS)-3,7-dimethyl-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]butane-1,3-diyl diacetate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.15
1-[(3aR,7S,8aS)-7-methyl-3-methylidene-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]-3-oxobutyl acetate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.04
1-[(3aR,7S,8aS)-7-methyl-3-methylidene-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]butane-1,3-diyl diacetate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.85
2-[(2E)-3,7-dimethyl-1-(1-methyl-1H-imidazol-2-yl)octa-2,6-dien-1-yl]butanedioic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.0025
2-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]butanedioic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.047
3-(4-chlorophenyl)-4-cyano-1-methyl-5-[(1-methylethyl)sulfanyl]-1H-pyrrole-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00145
3-(4-chlorophenyl)-4-cyano-5-(cyclohexylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.000325
3-(4-chlorophenyl)-4-cyano-5-(ethylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00011
3-(4-chlorophenyl)-4-cyano-5-(isopropylthio)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.00061
3-(4-chlorophenyl)-4-cyano-5-(methylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.028
3-(4-chlorophenyl)-4-cyano-5-(morpholin-4-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.002
3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]furan-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.0011
3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxamide
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00011
3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.000345
3-(4-chlorophenyl)-4-cyano-5-[(1-methylpropyl)sulfanyl]thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00089
3-(4-chlorophenyl)-4-cyano-5-[(2-methylpropyl)sulfanyl]thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.022
3-(4-chlorophenyl)-4-cyano-N-cyclopropyl-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxamide
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00064
3-(biphenyl-3-yl)-4-cyano-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
1
3-hydroxy-1-[(3aR,7S,8aS)-7-methyl-3-methylidene-2-oxo-3,3a,4,7,8,8a-hexahydro-2H-cyclohepta[b]furan-6-yl]butyl acetate
Saccharomyces cerevisiae
-
value above, 30°C, pH 7.5
0.08
3-oxo-3-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.051
4-(4-chlorophenyl)-2-[(1-methylethyl)sulfanyl]-1,3-thiazole-5-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.0000075
4-(4-chlorophenyl)-5-(hydroxyacetyl)-2-[(1-methylethyl)sulfanyl]thiophene-3-carbonitrile
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.0057
4-(4-chlorophenyl)-5-(methoxyacetyl)-2-[(1-methylethyl)sulfanyl]thiophene-3-carbonitrile
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00046
4-cyano-3-(3-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.00027
4-cyano-3-(4-fluorophenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.00025
4-cyano-3-(4-methoxyphenyl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.001
4-cyano-3-(dibenzo[b,d]furan-1-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.00032
4-cyano-3-(naphthalen-2-yl)-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.00062
4-cyano-3-[3-(methoxycarbonyl)phenyl]-5-(propan-2-ylsulfanyl)thiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
pH 7.5, 30°C
0.1
4-oxo-4-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]butanoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00124
5-(butylsulfanyl)-3-(4-chlorophenyl)-4-cyanothiophene-2-carboxylic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.00079
5-acetyl-4-(4-chlorophenyl)-2-[(1-methylethyl)sulfanyl]thiophene-3-carbonitrile
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.035
5-oxo-5-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]pentanoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.0038
ethyl 3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophene-2-carboxylate
Saccharomyces cerevisiae
-
30°C, pH 7.5
1
methyl N-([2-[4-ethoxy-2-(ethoxycarbonyl)-4-oxobutyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methioninate
Saccharomyces cerevisiae
-
IC50 above 1 mM, in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
1
methyl N-([2-[5-ethoxy-3-(methoxycarbonyl)-5-oxopentyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-isoleucyl-L-alaninate
Saccharomyces cerevisiae
-
IC50 above 1 mM, in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.19
methyl N-([2-[5-ethoxy-3-(methoxycarbonyl)-5-oxopentyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methioninate
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.34
methyl N-([2-[6-ethoxy-4-(ethoxycarbonyl)-6-oxohexyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-isoleucyl-L-alaninate
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.035
methyl N-([2-[6-ethoxy-4-(ethoxycarbonyl)-6-oxohexyl]-1-methyl-1H-imidazol-5-yl]methyl)-L-valyl-L-phenylalanyl-L-methioninate
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.27
N-[[2-(2,3-dicarboxypropyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-isoleucyl-L-alanine
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.15
N-[[2-(2,3-dicarboxypropyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-phenylalanyl-L-methionine
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.08
N-[[2-(3,4-dicarboxybutyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-isoleucyl-L-alanine
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.4
N-[[2-(3,4-dicarboxybutyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-phenylalanyl-L-methionine
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.08
N-[[2-(4,5-dicarboxypentyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-L-phenylalanyl-L-methionine
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.18
N-[[2-(4,5-dicarboxypentyl)-1-methyl-1H-imidazol-5-yl]methyl]-L-valyl-Lisoleucyl-L-alanine
Saccharomyces cerevisiae
-
in 5.8 mM dithiothreitol, 12 mM MgCl2, 0.012 mM ZnCl2 and 0.09% (w/v) CHAPS, 53 mM Tris-HCl, at pH 7.5 and 30°C
0.6
tert-butyl (2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.004
[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]propanedioic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.2
[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]sulfamic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.045
[3-(4-chlorophenyl)-4-cyano-5-[(1-methylethyl)sulfanyl]thiophen-2-yl]methyl acetate
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.005
[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]propanedioic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.2
[[(4E,8E)-5,9,13-trimethyltetradeca-4,8,12-trienoyl]amino]propanedioic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.028
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
0.13
(2Z,4E,8E)-5,9,13-trimethyl-3-(1-methyl-1H-imidazol-2-yl)tetradeca-2,4,8,12-tetraenoic acid
Saccharomyces cerevisiae
-
30°C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62000
about, alpha-subunit dimer, multi-angle laser light scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 37300, 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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of enzyme with (E,E)-[alpha,beta(n)-32P]-8-O-(3-benzoylbenzyl)-3,7-dimethyl-2,6-octadiene 1-diphosphate and of the enzyme with geranylgeranyl diphosphate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
procedure for labeling designed ankyrin repeat proteins (DARPins) engineered with a C-terminal CVIA sequence using an azide-containing FPP analog by yeast PFTase and procedures to subsequently conjugate the labeled DARPins to a TAMRA fluorophore
medicine
medicine
-
evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Casey, P.J.; Seabra, M.C.
Protein prenyltransferases
J. Biol. Chem.
271
5289-5292
1996
Saccharomyces cerevisiae
Park, H.W.; Beese, L.S.
Protein farnesyltransferase
Curr. Opin. Struct. Biol.
7
873-880
1997
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
Caplin, B.E.; Hettich, L.A.; Marshall, M.S.
Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase
Biochim. Biophys. Acta
1205
39-48
1994
Saccharomyces cerevisiae
Gomez, R.; Goodman, L.E.; Tripathy, S.K.; O'Rourke, E.; Manne, V.; Tamanoi, F.
Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart
Biochem. J.
289
25-31
1993
Saccharomyces cerevisiae
Turek-Etienne, T.C.; Strickland, C.L.; Distefano, M.D.
Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase
Biochemistry
42
3716-3724
2003
Saccharomyces cerevisiae
Duckworth, B.P.; Zhang, Z.; Hosokawa, A.; Distefano, M.D.
Selective labeling of proteins by using protein farnesyltransferase
ChemBioChem
8
98-105
2007
Saccharomyces cerevisiae
Hosokawa, A.; Wollack, J.W.; Zhang, Z.; Chen, L.; Barany, G.; Distefano, M.D.
Evaluation of an alkyne-containing analogue of farnesyl diphosphate as a dual substrate for protein-prenyltransferases
Int. J. Pept. Res. Ther.
13
345-354
2007
Saccharomyces cerevisiae
-
Labadie, G.R.; Viswanathan, R.; Poulter, C.D.
Farnesyl diphosphate analogues with omega-bioorthogonal azide and alkyne functional groups for protein farnesyl transferase-catalyzed ligation reactions
J. Org. Chem.
72
9291-9297
2007
Saccharomyces cerevisiae
de Figueiredo, R.M.; Coudray, L.; Dubois, J.
Synthesis and biological evaluation of potential bisubstrate inhibitors of protein farnesyltransferase. Design and synthesis of functionalized imidazoles
Org. Biomol. Chem.
5
3299-3309
2007
Saccharomyces cerevisiae
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
DeGraw, A.J.; Hast, M.A.; Xu, J.; Mullen, D.; Beese, L.S.; Barany, G.; Distefano, M.D.
Caged protein prenyltransferase substrates: tools for understanding protein prenylation
Chem. Biol. Drug Des.
72
171-181
2008
Saccharomyces cerevisiae
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
Pinel, B.; Dubois, J.; Seraphin, D.; Richomme, P.
Semisynthesis of alpha-methyl-gamma-lactones and in vitro evaluation of their activity on protein farnesyltransferase
J. Enzyme Inhib. Med. Chem.
25
172-179
2010
Saccharomyces cerevisiae
Lethu, S.; Ginisty, M.; Bosc, D.; Dubois, J.
Discovery of a new class of protein farnesyltransferase inhibitors in the arylthiophene series
J. Med. Chem.
52
6205-6208
2009
Saccharomyces cerevisiae
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
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)
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