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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

Reaction

farnesyl diphosphate
+
protein-cysteine
=
S-farnesyl protein
 +
diphosphate

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

Engineering

Engineering on EC 2.5.1.58 - protein farnesyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
G612A
-
decreased activity, mutant is resistant to the PFT inhibitors BMS-388891 and BMS-339941
Y837C
D297A
-
beta-subunit, 200fold decrease in kcat
D297N
-
beta-subunit, 200fold decrease in kcat
D352A
in the D352A mutant of the beta subunit Mg2+ binding motif, three water molecules and one oxygen atom from the alpha- and beta-phosphates of farnesyl diphosphate complete the octahedral coordination sphere of Mg2+. The absence of D352beta makes the transition of the substrates towards a conformational change harder
Dbeta352A
-
drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. The Km(Mg2+) increases 28-fold to 110 mM, and the farnesylation rate constant at saturating Mg2+ decreases 27-fold to 0.30 per s
Dbeta352K
-
drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. Mutation removes the magnesium activation of farnesylation catalyzed by FTase but does not significantly enhance the rate constant for farnesylation in the absence of Mg2+
H248A
-
beta-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 10fold decreased in comparison of wild-type, the rate constant by chemical step using farnesyl monophosphate 5fold decreased
H362A
-
beta-subunit, 50fold decrease in kcat
H362Q
K164A
-
alpha-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 30fold decreased in comparison of wild-type enzyme, the rate constant by chemical step using farnesyl monophosphate unaffected
K164N
-
mutation abolishes enzyme activity
K294A
-
slightly higher peptide affinity than wild-type enzyme, 7fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
K294Q
-
little alteration in peptide affinity, 2fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
N199D
-
mutation reduces enzyme activity
R172E
-
mutation reduces enzyme activity
R291A
-
2fold lower peptide affinity than wild-type enzyme, 3-4fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
R291G
-
little alteration in peptide affinity, 3-4fold decrease in affinity for farnesyl diphosphate, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type,decrease in rate constant for farnesylation in absence of Mg2+
R291K
-
slightly higher peptide affinity than wild-type enzyme, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
R291Q
-
little alteration in peptide affinity, mutation decreases the positive charge in the diphosphate binding pocket and also decrease the value of Km(Mg2+), compared to wild-type, decrease in rate constant for farnesylation in absence of Mg2+
W203H
-
mutation reduces enzyme activity
Y166F
-
mutation reduces enzyme activity
Y300F
-
beta-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 500fold decreased in comparison of wild-type enzyme, the rate constant by chemical step using farnesyl monophosphate 300fold decreased. Transition state for farnesylation is stabilized by interactions between the alpha-phosphate of the isoprenoid substrate and the side chains of Y300beta
C309A
-
lower kcat than the wild-type enzyme
D109N
-
loss of affinity of the enzyme for its protein substrate
D307A
-
lower kcat than the wild-type enzyme
E256A
-
130fold higher Km for the farnesyl diphosphate substrate
G259V
-
loss of affinity of the enzyme for its protein substrate
G328S
-
loss of affinity of the enzyme for its protein substrate
H363A
-
lower kcat than the wild-type enzyme
R211Q
-
lower kcat than the wild-type enzyme
Y310F
-
lower kcat than the wild-type enzyme
additional information