2.5.1.58: protein farnesyltransferase
This is an abbreviated version!
For detailed information about protein farnesyltransferase, go to the full flat file.
Word Map on EC 2.5.1.58
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2.5.1.58
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farnesylation
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prenylation
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geranylgeranylation
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isoprenoids
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beta-subunits
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isoprenylation
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15-carbon
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lamins
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manumycin
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geranylgeranyltransferase-i
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farnesyl-protein
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h-ras
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medicine
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peptidomimetic
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prelamin
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ggtase-i
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p21ras
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tetrapeptide
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farnesol
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tetrahydroquinoline
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ras-dependent
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pharmacology
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progerin
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3hmevalonate
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ras-induced
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lovastatin
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tipifarnib
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drug development
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ras-mediated
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ras-transformed
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lonafarnib
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hutchinson-gilford
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dimethylallyl
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geranylgeraniol
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isoprene
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analysis
- 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
Reaction
Synonyms
AfFTase, CAAX farnesyltransferase, EhFT, Era1, farnesyl protein transferase, farnesyltransferase, farnesyltransferase ternary complex part II, farnesyltransferase, farnesyl pyrophosphate-protein, farnesyltransferase, protein, FntA, FntB, FPT, fptase, FTase, hFTase, HIT5, Pf-PFT, PfPFT, PFT, PFTase, prenyl transferase, prenylprotein transferase, prenyltransferase, protein cysteine farnesyltransferase, protein farnesyl transferase, protein farnesyltransferase, protein prenyltransferase, protein-farnesyltransferase, R-PFT, Ram1, RAS farnesyltransferase, Ras protein farnesyltransferase, rFPTase, rFTase, rPFTase, TbFTase, yPFTase
ECTree
2.5.1.58 protein farnesyltransferaseAdvanced search results
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results (Application
Application on EC 2.5.1.58 - protein farnesyltransferase
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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
drug development
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the enzyme from Aspergillus fumigatus is a target for antifungal drug design
medicine
pharmacology
the enzyme is a promising therapeutic target for the treatment of various Ras-induced cancers and several other kinds of diseases
medicine
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evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers
medicine
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evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers
medicine
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evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers
medicine
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prime target for development of anticancer therapeutics
medicine
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prime target for development of anticancer therapeutics
medicine
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enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells
medicine
enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells
medicine
enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells
medicine
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possibility of development of specific inhibitors for parasitic protozoa
medicine
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inhibition of protein farnesyltransferase with influence for oncogenesis, potential target for treatment of cancer
medicine
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possible target of therapy of Hutchinson-Gilford progeria syndrome by inhibiting protein farnesylation
medicine
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analysis of reaction mechanism using catalytically active crystals and comparison with the human enzyme. In the CAAX binding site, a single residue substitution at the a2 site from tyrosine to asparagine results in a deeper cavity in this region compared with the human enzyme. The prenylated product exit groove is wider in the Cryptococcus neoformans enzyme relative to human enzyme and varies in amino acid composition. A substrate-induced conformational change observed for the 4alpha-5alpha loop of results in a molecular surface in the active site with two distinct states that can be individually exploited for inhibitor design
medicine
design of a protein farnesyltransferase-driven plasma membrane-targeted chimeric peptide, PpIX-C6-PEG8-KKKKKKSKTKC-OMe, for plasma membrane-targeted photodynamic therapy and enhanced immunotherapy. The plasma membrane targeting ability of the peptide originates from the cellular K-Ras signaling, which occurs exclusively to drive the corresponding proteins to plasma membrane by protein farnesyltransferase
medicine
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enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells
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medicine
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analysis of reaction mechanism using catalytically active crystals and comparison with the human enzyme. In the CAAX binding site, a single residue substitution at the a2 site from tyrosine to asparagine results in a deeper cavity in this region compared with the human enzyme. The prenylated product exit groove is wider in the Cryptococcus neoformans enzyme relative to human enzyme and varies in amino acid composition. A substrate-induced conformational change observed for the 4alpha-5alpha loop of results in a molecular surface in the active site with two distinct states that can be individually exploited for inhibitor design
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