2.5.1.58: protein farnesyltransferase

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For detailed information about protein farnesyltransferase, go to the full flat file.

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 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.58 protein farnesyltransferase

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Results	in table
2	Activating Compound
3673	AA Sequence
44	Application
1	CAS Registry Number
37	Cloned(Commentary)
17	Crystallization (Commentary)
412	Disease/ Diagnostics
25	General Information
2	General Stability
420	IC50 Value
974	Inhibitors
240	kcat/KM [mM/s]
26	Ki Value [mM]
114	KM Value [mM]
4	Localization
78	Metals/Ions
36	Molecular Weight [Da]
61	Natural Substrates/ Products (Substrates)
5	Organic Solvent Stability
151	Organism
2	Pathway
114	PDB ID
20	pH Optimum
2	pH Range
1	pH Stability
2	pI Value
59	Protein Variants
30	Purification (Commentary)
18	Reaction
145	Reference
39	Source Tissue
6	Specific Activity [micromol/min/mg]
486	Substrates and Products (Substrate)
30	Subunits
145	Synonyms
1	Systematic Name
18	Temperature Optimum [°C]
114	Turnover Number [1/s]

General Stability

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General Stability on EC 2.5.1.58 - protein farnesyltransferase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

all activity is lost, when the subunits are dissociated chemically

Rattus norvegicus

-

637517

the heterodimer cannot be dissociated unless it is denaturated, and each individual subunit appears to be unstable in solution, the number of hydrogen bonds found in the enzyme subunit interface may explain the unusual stability of the heterodimer

Rattus norvegicus

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637505