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3,7,11-trimethyl-12-(7-nitro-benzo[1,2,5]-oxadiazo-4-ylamino)-dodeca-2,6,10-trien-1-diphosphate + GST-RhoA
diphosphate + ?
-
-
-
-
?
3,7-dimethyl-8-(7-nitro-benzo[1,2,5]oxadiazol-4-ylamino)-octa-2,6-diene-1-diphosphate + GST-RhoA
diphosphate + ?
-
-
-
-
?
farnesyl diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFFCAI-Leu
diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFF-S-farnesyl-CAI-Leu
farnesyl diphosphate + Ki-Ras4B
diphosphate + S-geranylgeranyl-Ki-Ras4B
-
-
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-ALEPPETEPKRKCCIF
diphosphate + (biotin-CONH-(CH2)5-CO-)-ALEPPETEPKRK-S-geranylgeranyl-CCIF
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-GTPRASNRSCAIS
diphosphate + (biotin-CONH-(CH2)5-CO-)-GTPRASNRS-S-geranylgeranyl-CAIS
-
ECB-laminB(S), 5% activity in comparison of protein substrate motif: CAA-leucine
-
-
?
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFFCAI-Leu
diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFF-S-geranylgeranyl-CAI-Leu
geranylgeranyl diphosphate + Arg-Arg-Cys-Val-Leu-Leu
diphosphate + Arg-Arg-S-geranylgeranyl-Cys-Val-Leu-Leu
-
-
-
-
?
geranylgeranyl diphosphate + Asp-Asp-Pro-Thr-Ala-Ser-Ala-Cys-Val-Leu-Leu
Asp-Asp-Pro-Thr-Ala-Ser-Ala-(S-geranylgeranyl)-Cys-Val-Leu-Leu + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
geranylgeranyl diphosphate + Cdc420-cysteine
S-geranylgeranyl-Cdc420 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cys-Val-Leu-Leu
S-geranylgeranyl-Cys-Val-Leu-Leu + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Cys-Val-Leu-Ser
S-geranylgeranyl-Cys-Val-Leu-Ser + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + dansyl-Cys-Ile-Ile-Leu
diphosphate + dansyl-S-geranylgeranyl-Cys-Ile-Ile-Leu
-
-
-
-
?
geranylgeranyl diphosphate + dansyl-GCFT
diphosphate + S-geranylgeranyl dansyl-GCFT
-
-
-
?
geranylgeranyl diphosphate + dansyl-GCII
diphosphate + S-geranylgeranyl dansyl-GCII
-
-
-
?
geranylgeranyl diphosphate + dansyl-GCLL
diphosphate + S-geranylgeranyl dansyl-GCLL
-
-
-
?
geranylgeranyl diphosphate + dansyl-GCYL
diphosphate + S-geranylgeranyl dansyl-GCYL
-
-
-
?
geranylgeranyl diphosphate + dansyl-Gly-Cys-Ile-Ile-Leu
dansyl-Gly-(S-geranylgeranyl)-Cys-Ile-Ile-Leu + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + dansyl-Thr-Lys-Cys-Val-Ile-Met
diphosphate + dansyl-Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Met
-
-
-
-
?
geranylgeranyl diphosphate + GST-CDC42
diphosphate + GST-S-geranylgeranyl-CDC42
-
recombinant glutathione S-transferase fusion protein of CDC42Hs with a C-terminal Cys-Cys-Ile-Phe sequence
-
-
?
geranylgeranyl diphosphate + GST-RhoA
diphosphate + GST-S-geranylgeranyl-RhoA
-
-
-
-
?
geranylgeranyl diphosphate + H-Ras-CVLL
S-geranylgeranyl-protein + ?
-
-
-
-
?
geranylgeranyl diphosphate + K Ras-cysteine
S-geranylgeranyl-K Ras + diphosphate
geranylgeranyl diphosphate + Ki-Ras4A
diphosphate + S-geranylgeranyl-Ki-Ras4A
-
-
-
-
?
geranylgeranyl diphosphate + Ki-Ras4B
diphosphate + S-geranylgeranyl-Ki-Ras4B
geranylgeranyl diphosphate + Leu-Pro-Cys-Val-Val-Met
diphosphate + Leu-Pro-S-geranylgeranyl-Cys-Val-Val-Met
-
-
-
-
?
geranylgeranyl diphosphate + Lys-Lys-Cys-Ile-Ile-Met
diphosphate + Lys-Lys-S-geranylgeranyl-Cys-Ile-Ile-Met
-
-
-
-
?
geranylgeranyl diphosphate + Lys-Pro-Cys-Val-Val-Met
Lys-Pro-(S-geranylgeranyl)-Cys-Val-Val-Met + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + N-dansyl-Gly-Cys-Val-Ile-Leu-OH
?
-
-
-
-
?
geranylgeranyl diphosphate + N-Ras
diphosphate + S-geranylgeranyl-N-Ras
-
-
-
-
?
geranylgeranyl diphosphate + N-Ras-cysteine
S-geranylgeranyl-N-Ras + diphosphate
geranylgeranyl diphosphate + Phe-Phe-Cys-Ala-Ile-Leu
diphosphate + Phe-Phe-S-geranylgeranyl-Cys-Ala-Ile-Leu
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl 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
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
geranylgeranyl diphosphate + Rac GTPase-cysteine
S-geranylgeranyl-Rac GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
geranylgeranyl diphosphate + Rap-cysteine
S-geranylgeranyl-Rap + diphosphate
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
geranylgeranyl diphosphate + Ras protein
S-geranylgeranyl-Ras protein + diphosphate
geranylgeranyl diphosphate + Ras-CVLL
S-geranylgeranyl-Ras-CVLL + diphosphate
-
tritium labelled geranylgeranyl diphosphate for enzyme assay, His-tagged geranylgeranyl diphosphate
-
-
?
geranylgeranyl diphosphate + Ras-Cys-Val-Leu-Leu
diphosphate + Ras-S-geranylgeranyl-Cys-Val-Leu-Leu
geranylgeranyl diphosphate + Rho GTPase-cysteine
S-geranylgeranyl-Rho GTPase + diphosphate
geranylgeranyl diphosphate + Rho-cysteine
S-geranylgeranyl-Rho + diphosphate
geranylgeranyl diphosphate + Rho10-cysteine
S-geranylgeranyl-Rho10 + diphosphate
geranylgeranyl diphosphate + RhoA
diphosphate + S-geranylgeranyl-RhoA
-
-
-
-
?
geranylgeranyl diphosphate + RhoA GTPase-cysteine
S-geranylgeranyl-RhoA GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + rhoC protein
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + S-geranylgeranyl-Ki-Ras4B
diphosphate + S-geranylgeranyl-Ki-Ras4B
-
both the polylysine and the carboxy-terminal methionine are important for geranylgeranylation of this substrate
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Ala
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Ala
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Arg
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Arg
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Asn
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Asn
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Asp
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Asp
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Cys
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Cys
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Gln
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Gln
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Ile
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Ile
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Leu
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Leu
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Met
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Met
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Phe
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Phe
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Ser
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Ser
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Thr
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Thr
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Tyr
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Tyr
-
-
-
-
?
geranylgeranyl diphosphate + Thr-Lys-Cys-Val-Ile-Val
diphosphate + Thr-Lys-(S-geranylgeranyl)-Cys-Val-Ile-Val
-
-
-
-
?
geranylgeranyl diphosphate + [glutathione S-transferase]-GCVKIKKCVIL
diphosphate + ?
Ser-Ser-Cys-Ile-Leu-Leu + geranylgeranyl diphosphate
diphosphate + Ser-Ser-S-geranylgeranyl-Cys-Ile-Leu-Leu
-
-
-
-
?
additional information
?
-
farnesyl diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFFCAI-Leu
diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFF-S-farnesyl-CAI-Leu
-
biotin-gamma6
-
-
?
farnesyl diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFFCAI-Leu
diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFF-S-farnesyl-CAI-Leu
-
ECB-gamma6
-
-
?
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
the enzyme catalyzes postttranslational 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
-
-
?
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-ALEPPETEPKRKCCIF
diphosphate + (biotin-CONH-(CH2)5-CO-)-ALEPPETEPKRK-S-geranylgeranyl-CCIF
-
-
-
-
?
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-ALEPPETEPKRKCCIF
diphosphate + (biotin-CONH-(CH2)5-CO-)-ALEPPETEPKRK-S-geranylgeranyl-CCIF
-
ECB-G25K, 42% activity in comparison of protein substrate motif: CAA-leucine
-
-
?
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFFCAI-Leu
diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFF-S-geranylgeranyl-CAI-Leu
-
biotin-gamma6, preferred substrate
-
-
?
geranylgeranyl diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFFCAI-Leu
diphosphate + (biotin-CONH-(CH2)5-CO-)-NPFREKKFF-S-geranylgeranyl-CAI-Leu
-
ECB-gamma6, preferred substrate
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + K Ras-cysteine
S-geranylgeranyl-K Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + K Ras-cysteine
S-geranylgeranyl-K Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Ki-Ras4B
diphosphate + S-geranylgeranyl-Ki-Ras4B
-
-
-
-
?
geranylgeranyl diphosphate + Ki-Ras4B
diphosphate + S-geranylgeranyl-Ki-Ras4B
-
-
-
-
?
geranylgeranyl diphosphate + N-Ras-cysteine
S-geranylgeranyl-N-Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + N-Ras-cysteine
S-geranylgeranyl-N-Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the enzyme negatively regulates abscisic acid signaling in guard cells. The enzyme is specifically involved in negative regulation of auxin-induced lateral root initiation
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X is Leu, Phe or Ser, preferred substrate: Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X is Leu, Phe or Ser, preferred substrate: Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X may be Leu, Phe, or Ser, with high concentrations of peptide substrates this specificity is lost
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme catalyses the transfer of the 20-carbon prenyl group from geranylgeranyl diphosphate to the cysteine residue near the C-termini of a variety of eukaryotic proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
substrate motif: carboxy-terminal -Ca1a2X box
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
the enzyme adds a C20 geranylgeranyl group to proteins such as RhoA, RhoC, Rap1 and Ral at the cysteine within the carboxy-terminal tetrapeptide consensus sequence CAAL (C is cysteine, A is an aliphatic amino acid, and the C-terminal residue is leucine or phenylalanine)
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the Rab protein Rab8-GTPase, which ends with a Cys-Val-Leu-Leu motif is able to serve as a substrate for either geranylgeranyl transferase I and II, but modified predominantly by geranylgeranyl transferase II, Y78D mutation selective prevents prenylation of Rab8 by geranylgeranyl transferase II, but not geranylgeranyltransferaseI
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X is Leu, Phe or Ser, preferred substrate: Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
GGTase-I catalyzes C-terminal lipidation of more than 100 proteins, including many GTP-binding regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-Leu
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X is Leu or Phe
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X is Leu or Phe
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
yeast enzyme is essential for yeast cell growth
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap-cysteine
S-geranylgeranyl-Rap + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap-cysteine
S-geranylgeranyl-Rap + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Ras protein
S-geranylgeranyl-Ras protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Ras protein
S-geranylgeranyl-Ras protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Ras-Cys-Val-Leu-Leu
diphosphate + Ras-S-geranylgeranyl-Cys-Val-Leu-Leu
-
-
-
-
?
geranylgeranyl diphosphate + Ras-Cys-Val-Leu-Leu
diphosphate + Ras-S-geranylgeranyl-Cys-Val-Leu-Leu
-
-
-
-
?
geranylgeranyl diphosphate + Rho GTPase-cysteine
S-geranylgeranyl-Rho GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho GTPase-cysteine
S-geranylgeranyl-Rho GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho-cysteine
S-geranylgeranyl-Rho + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho-cysteine
S-geranylgeranyl-Rho + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho10-cysteine
S-geranylgeranyl-Rho10 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho10-cysteine
S-geranylgeranyl-Rho10 + diphosphate
while Rho10 has benn previously predicted to lack a CaaX motif, analysis of the Rho10 transcript sequence using RNA sequencing data reveals that one splice site is misannotated, the corrected sequence contains a CLIL C-terminal motif
-
-
?
geranylgeranyl diphosphate + [glutathione S-transferase]-GCVKIKKCVIL
diphosphate + ?
-
-
-
-
?
geranylgeranyl diphosphate + [glutathione S-transferase]-GCVKIKKCVIL
diphosphate + ?
-
-
-
-
?
additional information
?
-
the enzyme has a restricted substrate specificity. Ggtase-I substrates often contain CaaL motifs, overview. Of the three Rho paralogues, only GFP-Rho10 localizes to cellular membranes in wild-type cells. This membrane localization is slightly disrupted in the cdc43DELTA mutant, indicating that the Rho10 protein is likely a Ggtase-I substrate
-
-
?
additional information
?
-
-
the enzyme has a restricted substrate specificity. Ggtase-I substrates often contain CaaL motifs, overview. Of the three Rho paralogues, only GFP-Rho10 localizes to cellular membranes in wild-type cells. This membrane localization is slightly disrupted in the cdc43DELTA mutant, indicating that the Rho10 protein is likely a Ggtase-I substrate
-
-
?
additional information
?
-
-
not: N-Ras
-
-
?
additional information
?
-
GGTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 20-carbon isoprenoid geranylgeranyl from its donor geranylgeranyl diphosphate (GGPP) is specific to GGTase-I. No activity with H-Ras
-
-
?
additional information
?
-
GGTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 20-carbon isoprenoid geranylgeranyl from its donor geranylgeranyl diphosphate (GGPP) is specific to GGTase-I. No activity with H-Ras
-
-
?
additional information
?
-
-
some of the 18 analysed hexapeptides effieciently farnsylated by enzyme
-
-
?
additional information
?
-
the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition
-
-
?
additional information
?
-
the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition
-
-
?
additional information
?
-
GGTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 20-carbon isoprenoid geranylgeranyl from its donor geranylgeranyl diphosphate (GGPP) is specific to GGTase-I. Residues Lysalpha164, Hisbeta219, Argbeta263, Lysbeta266 and Tyrbeta272 in GGTase-I can form hydrogen bonds with GGPP. No activity with H-Ras
-
-
?
additional information
?
-
GGTase-I can transfer isoprenoids to intracellular proteins that contain CAAX motifs. The isoprenoid groups can be selectively recognized by GGTase-I. The 20-carbon isoprenoid geranylgeranyl from its donor geranylgeranyl diphosphate (GGPP) is specific to GGTase-I. Residues Lysalpha164, Hisbeta219, Argbeta263, Lysbeta266 and Tyrbeta272 in GGTase-I can form hydrogen bonds with GGPP. No activity with H-Ras
-
-
?
additional information
?
-
enzyme prefers farnesyl diphosphate over geranylgeranyl diphosphate, but catalyzes the reactions of both substrates, i.e. reactions of EC 2.5.1.58 and EC 2.5.1.59, respectively
-
-
-
additional information
?
-
-
requires geranylgeranylation of rho1p for the correct function of enzyme
-
-
?
additional information
?
-
most of the CaaX-containing proteins with X= Leu and X= Met are good substrates of PGGT-I, whereas those with X= Phe are poor substrates for PGGT-I, Trypanosma cruzi j2 DNAJ protein, Trypanosoma cruzi PRL-1 protein tyrosine phosphatase, CHFM (a small GTPase like protein), and Trypanosoma cruzi Rho1 GTPase are no substrates for PGGT-I
-
-
?
additional information
?
-
-
most of the CaaX-containing proteins with X= Leu and X= Met are good substrates of PGGT-I, whereas those with X= Phe are poor substrates for PGGT-I, Trypanosma cruzi j2 DNAJ protein, Trypanosoma cruzi PRL-1 protein tyrosine phosphatase, CHFM (a small GTPase like protein), and Trypanosoma cruzi Rho1 GTPase are no substrates for PGGT-I
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
farnesyl diphosphate + protein-cysteine
S-farnesyl protein + diphosphate
-
the enzyme catalyzes postttranslational modification of proteins, the farnesyl moieties attached to the substrates are direcly involved in protein-protein interactions as well as in protein-membrane interactions
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
geranylgeranyl diphosphate + Cdc420-cysteine
S-geranylgeranyl-Cdc420 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + K Ras-cysteine
S-geranylgeranyl-K Ras + diphosphate
geranylgeranyl diphosphate + N-Ras-cysteine
S-geranylgeranyl-N-Ras + diphosphate
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl 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
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
geranylgeranyl diphosphate + Rac GTPase-cysteine
S-geranylgeranyl-Rac GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
geranylgeranyl diphosphate + Rap-cysteine
S-geranylgeranyl-Rap + diphosphate
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
geranylgeranyl diphosphate + Ras protein
S-geranylgeranyl-Ras protein + diphosphate
geranylgeranyl diphosphate + Ras-CVLL
S-geranylgeranyl-Ras-CVLL + diphosphate
-
tritium labelled geranylgeranyl diphosphate for enzyme assay, His-tagged geranylgeranyl diphosphate
-
-
?
geranylgeranyl diphosphate + Rho GTPase-cysteine
S-geranylgeranyl-Rho GTPase + diphosphate
geranylgeranyl diphosphate + Rho-cysteine
S-geranylgeranyl-Rho + diphosphate
geranylgeranyl diphosphate + Rho10-cysteine
S-geranylgeranyl-Rho10 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + RhoA GTPase-cysteine
S-geranylgeranyl-RhoA GTPase + diphosphate
-
-
-
?
additional information
?
-
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Cdc42-cysteine
S-geranylgeranyl-Cdc42 + diphosphate
-
-
-
?
geranylgeranyl diphosphate + K Ras-cysteine
S-geranylgeranyl-K Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + K Ras-cysteine
S-geranylgeranyl-K Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + N-Ras-cysteine
S-geranylgeranyl-N-Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + N-Ras-cysteine
S-geranylgeranyl-N-Ras + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
the enzyme negatively regulates abscisic acid signaling in guard cells. The enzyme is specifically involved in negative regulation of auxin-induced lateral root initiation
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
enzyme catalyses the transfer of the 20-carbon prenyl group from geranylgeranyl diphosphate to the cysteine residue near the C-termini of a variety of eukaryotic proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
the enzyme adds a C20 geranylgeranyl group to proteins such as RhoA, RhoC, Rap1 and Ral at the cysteine within the carboxy-terminal tetrapeptide consensus sequence CAAL (C is cysteine, A is an aliphatic amino acid, and the C-terminal residue is leucine or phenylalanine)
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
GGTase-I catalyzes C-terminal lipidation of more than 100 proteins, including many GTP-binding regulatory proteins
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
yeast enzyme is essential for yeast cell growth
-
-
?
geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
-
this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rac-cysteine
S-geranylgeranyl-Rac + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap-cysteine
S-geranylgeranyl-Rap + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap-cysteine
S-geranylgeranyl-Rap + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rap1A-cysteine
S-geranylgeranyl-Rap1A + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Ras protein
S-geranylgeranyl-Ras protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Ras protein
S-geranylgeranyl-Ras protein + diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + Rho GTPase-cysteine
S-geranylgeranyl-Rho GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho GTPase-cysteine
S-geranylgeranyl-Rho GTPase + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho-cysteine
S-geranylgeranyl-Rho + diphosphate
-
-
-
?
geranylgeranyl diphosphate + Rho-cysteine
S-geranylgeranyl-Rho + diphosphate
-
-
-
?
additional information
?
-
the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition
-
-
?
additional information
?
-
the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3R,4S,5R)-2-(3,4-dichlorophenyl)-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-1-[(4-methylphenyl)sulfonyl]-4-(pentylsulfanyl)-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-4-[(4-methoxyphenyl)sulfanyl]-1-[(4-methylphenyl)sulfonyl]-5-propylpyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-5-ethyl-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-2-(4-bromophenyl)-5-hexyl-4-(hexylsulfanyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(3-chlorophenyl)-5-(cyclopentylmethyl)-1-[(4-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(4-chlorophenyl)-1-[(4-chlorophenyl)sulfonyl]-5-(cyclopentylmethyl)pyrrolidine-3-carboxylic acid
-
-
(2R,3R,4S,5R)-4-[(3-tert-butoxy-3-oxopropyl)sulfanyl]-2-(4-chlorophenyl)-5-(cyclopentylmethyl)-1-(phenylsulfonyl)pyrrolidine-3-carboxylic acid
-
-
(2R,3R,5S)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]pyrrolidine-3-carboxylic acid
compete with the substrate protein rather than GGPP; compete with the substrate protein rather than GGPP
(2S,5R)-5-ethyl-2-(4-fluorophenyl)-1-tosyl-2,5-dihydro-1H-pyrrole-3-carboxylic acid
-
IC50: 0.2 mM using RhoA as a substrate, IC50: 0.25 mM using Ki-Ras4B as a substrate
(2S,5S)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-2,5-dihydro-1H-pyrrole-3-carboxylic acid
(2S,6S)-2,6-bis(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-1,2,5,6-tetrahydropyridine-3-carboxylic acid
-
IC50: 0.0003 mM using RhoA as a substrate, IC50: 0.002 mM using Ki-Ras4B as a substrate
(2S,6S)-6-(4-fluorophenyl)-1-[(4-methylphenyl)sulfonyl]-2-phenyl-1,2,5,6-tetrahydropyridine-3-carboxylic acid
-
IC50: 0.12 mM using RhoA as a substrate, IC50: 0.08 mM using Ki-Ras4B as a substrate
(S)-N-(1-amino-3-(4-fluorophenyl)-1-oxopropan-2-yl)-4-((1-(3,4-dichlorophenyl)-4-(2-(methylthio)ethyl)-3-(pyridin-3-yl)-1H-pyrazol-5-yl)oxy)butanamide
potent GGT1 inhibitor, anti-proliferative efficacy against MDA-MB-231 cells has an IC50 value of 0.0076 mM
(S)-N-(1-amino-3-(4-methoxyphenyl)-1-oxopropan-2-yl)-4-((1-(3,4-dichlorophenyl)-4-(2-(methylthio)ethyl)-3-(pyridin-3-yl)-1H-pyrazol-5-yl)oxy)butanamide
potent GGT1 inhibitor
(S)-N-(4-(3,4-dichlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
-
dual inhibitor for both farnesyl transferase and geranygeranyltransferase-I. Compound occupies both isoprenoid and peptide substrate binding sites
(S)-N-(4-(3-chlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
-
dual inhibitor for both farnesyl transferase and geranygeranyltransferase-I
1-phosphono-(E,E,E)-geranylgeraniol
1-[2-[(Z)-[[4-(8-chloro-10,11-dihydrodibenzo[b,f]thiepin-10-yl)piperazin-1-yl]imino]methyl]phenoxy]-N,N-dimethylmethanamine
i.e L-269289, selective chemical inhibition of GGTase I by L-269289 potentiates echinocandin activity and renders echinocandin-resistant Candida albicans responsive to treatment in vitro and in animal models for disseminated infection
1-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-cyclohexanecarboxylic acid
-
IC50: 6525 nM
1-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-cyclohexanecarboxylic acid methyl ester
-
IC50: above 0.01 mM
11-aminoundecylcarbonyl-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
-
competitive. bivalent inhibitor for simultaneous recognition of both exteriorand interior protein surface. Not inhibitory against farnesyltransferase
2-(3-chlorophenyl)-6-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-1,2,5,6-tetrahydropyridine-3-carboxylic acid
compete with the substrate protein rather than GGPP; compete with the substrate protein rather than GGPP
2-aryl-4-aminobenzoic acid
-
IC50: 21 nM
2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-N-(3-methyl-butyl)-acetamide
-
IC50: above 0.01 mM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl] acetylamino}-4-methyl-pentanoic acid methyl ester
-
IC50: above 0.01 mM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid
-
IC50: 0.0063 mM; IC50: 170 nM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid methyl ester
-
IC50: 4500 nM; IC50: above 0.01 mM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methyl-pentanoic acid
-
IC50: 2700 nM; IC50: 580 nM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methyl-pentanoic acid methyl ester
-
IC50: above 0.01 mM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methylsulfanyl-butyric acid
-
IC50: 3350 nM
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methylsulfanyl-butyric acid methyl ester
-
IC50: above 0.01 mM
3-(4'-farnesyloxy-3'-methoxyphenyl)-2-trans propenoic acid
-
0.1 mM, 83.9% inhibition
3-(4'-farnesyloxy-3'-OH-phenyl)-2-trans propenoic acid
-
0.1 mM, 93.5% inhibition
3-(4'-geranyloxy-3'-methoxyphenyl)-2-trans propenoic acid
-
0.1 mM, 78.6% inhibition
3-(4'-geranyloxy-3'-methoxyphenyl)-2-trans propenoic acid ethyl ester
-
0.1 mM, 3% inhibition
3-(4'-geranyloxy-3'-OH-phenyl)-2-trans propenoic acid
-
0.1 mM, 72.4% inhibition
3-(4'-geranyloxy-3'-OH-phenyl)-2-trans propenoic acid ethyl ester
-
0.1 mM, 7.5% inhibition
3-(4'-isopentenyloxy-3'-OH-phenyl)-2-trans propenoic acid
-
0.1 mM, 46.4% inhibition
3-aza-geranylgeranyl-diphosphate
-
competitive inhibitor with respect to geranylgeranyl diphosphate, non-competitive to Cys-Val-Phe-Leu
3-chloro-N-[2-oxo-2-[2-[[1-phenyl-3-(4-propoxyphenyl)pyrazol-4-yl]methylidene]hydrazinyl]ethyl]benzamide
-
GGTI-DU.Sig1, PubChem CID 3311883, inhibitor of protein geranylgeranyltransferase type I
4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile
is bound to the peptide-binding site by competing with the CAAX substrate in the 4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile-FTase complex, cf. EC 2.5.1.58, but is bound in the lipid-binding pocket together with a portion of the peptide-binding site in the 4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile-GGTase-I complex; is bound to the peptide-binding site by competing with the CAAX substrate in the 4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrileFTase complex, cf. EC 2.5.1.58, but is bound in the lipid-binding pocket together with a portion of the peptide-binding site in the L-4-[2-[4-(3-chlorophenyl)-3-oxopiperazin-1-yl]-2-(1H-imidazol-5-yl)ethyl]benzonitrile-GGTase-I complex
4-[[([5-[(4-ethylphenoxy)methyl]-4-(1-phenylethyl)-4H-pyrazol-3-yl]sulfanyl)acetyl]amino]benzamide
-
inhibitor identified using quantitative structure-activity realtionship models and virtual screening of chemicals. confirmation of predicted data by experiment
4-[[2-[[5-(2-methoxyphenyl)-4-phenethyl-1,2,4-triazol-3-yl]sulfanyl]acetyl]amino]benzamide
-
GGTI-DU.En1, PubChem CID 2118978, inhibitor of protein geranylgeranyltransferase type I
4-[[2-[[5-[(4-ethylphenoxy)methyl]-4-(1-phenylethyl)-1,2,4-triazol-3-yl]sulfanyl]acetyl]amino]benzamide
-
GGTI-DU.En2, PubChem CID 3455185, inhibitor of protein geranylgeranyltransferase type I, no or little activity against protein farnesyltransferase
auraptene
-
0.1 mM, 18.6% inhibition
boropinic acid
-
0.1 mM, 31% inhibition
collinin
-
0.1 mM, 34.2% inhibition
Cys-3-(aminomethyl)benzoic acid-Leu
-
noncompetitive to geranylgeranyl diphosphate, competitive to dansyl-Gly-Cys-Ile-Ile-Leu
Cys-Val-Phe-Leu
-
noncompetitive inhibitor with respect to geranylgeranyl diphosphate, 50% inhibition at 0.0001 mM, competitive to Cys-Val-Phe-Leu
diethyl dicarbonate
-
80% loss of activity at 5 mM
GGTI-2151
16.3% inhibition at 50 nM
GGTI-2154
14.7% inhibition at 50 nM
GGTI-2418
a GGTI inhibitor, in clinical trials as potential anti-tumor agent in breast cancer; a GGTI inhibitor, in clinical trials as potential anti-tumor agent in breast cancer
L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
-
-
manumycin A
the cdc43DELTA mutant is 2fold more susceptible to this farnesyltransferase inhibitor than the wild-type
methyl N-([2-(3-chlorophenyl)-6-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-1,2,5,6-tetrahydropyridin-3-yl]carbonyl)leucinate
with anti-tumor activity; with anti-tumor activity
N-(12-ammoniododecanoyl)-D-cysteinyl-L-valyl-L-isoleucyl-L-leucine trifluoroacetate
-
-
N-(12-[[(3-[[(3R)-3-ammonio-4-phenylbutyl]oxy]-4,5-bis[[(3S)-3-ammonio-4-phenylbutyl]oxy]phenyl)carbonyl]amino]dodecanoyl)-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine tris(trifluoroacetate)
-
-
N-(2,5-dichlorophenyl)-N'-[[3-(4-methylphenyl)-1-phenylpyrazol-4-yl]methylideneamino]oxamide
-
GGTI-DU.Sig2, PubChem CID 4277701, inhibitor of protein geranylgeranyltransferase type I
N-(4-[[(3-[[(3R)-3-ammonio-4-phenylbutyl]oxy]-4,5-bis[[(3S)-3-ammonio-4-phenylbutyl]oxy]phenyl)carbonyl]amino]butanoyl)-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine tris(trifluoroacetate)
-
-
N-([(2S)-2-benzyl-4-[(4-methyl-1H-imidazol-5-yl)methyl]-3-oxopiperazin-1-yl]carbonyl)-L-leucine
-
N-([5-[(1H-imidazol-5-ylamino)methyl]-2'-methylbiphenyl-2-yl]carbonyl)-L-leucine
a non-thiol-containing peptidomi-metic, it can inhibit human tumor growth in mice and the combination therapy with cytotoxic agents is more beneficial than monotherapy. N-([5-[(1H-imidazol-5-ylamino)methyl]-2'-methylbiphenyl-2-yl]carbonyl)-L-leucine is able to induce breast carcinoma apoptosis and tumor regression in H-Ras transgenic mice; a non-thiol-containing peptidomi-metic, it can inhibit human tumor growth in mice and the combination therapy with cytotoxic agents is more beneficial than monotherapy. N-([5-[(1H-imidazol-5-ylamino)methyl]-2'-methylbiphenyl-2-yl]carbonyl)-L-leucine is able to induce breast carcinoma apoptosis and tumor regression in H-Ras transgenic mice
N-benzyl-2-[(2-chlorobenzyl)[[5-(4-methylphenyl)-2H-tetrazol-2-yl]acetyl]amino]butanamide
-
inhibitor identified using quantitative structure-activity realtionship models and virtual screening of chemicals. confirmation of predicted data by experiment
N-benzyl-2-[(2-chlorophenyl)methyl-[2-[5-(4-methylphenyl)tetrazol-2-yl]acetyl]amino]butanamide
-
GGTI-DU.As2, PubChem CID 3180738, inhibitor of protein geranylgeranyltransferase type I, no or little activity against protein farnesyltransferase
N-[(5-[[(2R)-2-amino-3-sulfanylpropyl]amino]biphenyl-2-yl)carbonyl]-L-leucine
-
N-[(E)-1-(benzylcarbamoyl)-2-[5-(3,4-dichlorophenyl)furan-2-yl]ethenyl]-4-methylbenzamide
-
inhibitor identified using quantitative structure-activity realtionship models and virtual screening of chemicals. confirmation of predicted data by experiment
N-[12-([[3,4,5-tris(3-ammoniopropoxy)phenyl]carbonyl]amino)dodecanoyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine tris(trifluoroacetate)
-
-
N-[2-(benzylamino)-2-oxoethyl]-2-[5-(4-chlorophenyl)tetrazol-2-yl]-N-(4-propan-2-ylphenyl)acetamide
-
GGTI-DU.As1, PubChem CID 3180720, inhibitor of protein geranylgeranyltransferase type I
N-[3-(benzylamino)-1-[5-(3,4-dichlorophenyl)furan-2-yl]-3-oxoprop-1-en-2-yl]-4-methylbenzamide
-
GGTI-DU.Sig3, PubChem CID 5143450, inhibitor of protein geranylgeranyltransferase type I, no or little activity against protein farnesyltransferase
N-[6-(3,4,5-tris(3-amino-1-propoxy)benzoylamino)-undecylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
-
competitive, bivalent inhibitor for simultaneous recognition of both exterior and interior protein surface. Not inhibitory against farnesyltransferase
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-hexylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine trifluoroacetate
-
-
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-propylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
-
bivalent inhibitor for simultaneous recognition of both exterior and interior protein surface. Not inhibitory against farnesyltransferase
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-undecylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
-
competitive, bivalent inhibitor for simultaneous recognition of both exterior and interior protein surface. Not inhibitory against farnesyltransferase
N-[[4-(imidazol-4-yl)methylamino]-2-(1-naphthyl)benzoyl]leucine
-
Na-(4-[[1-(3,4-dichlorophenyl)-4-[2-(methylsulfanyl)ethyl]-3-(pyridin-3-yl)-1H-pyrazol-5-yl]oxy]butanoyl)-L-phenylalaninamide
-
Na-([(5R)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-2,5-dihydro-1H-pyrrol-3-yl]carbonyl)-L-phenylalaninamide
with anti-tumor activity; with anti-tumor activity
NPFREKKFFCAIL
-
biotin-gamma6, substrate inhibition at high peptide concentration
P61A6
derived from an allenoate-derived compound library, shows efficiency of the enzyme inhibitor to inhibit tumor growth demonstrated using human pancreatic cancer xenograft; derived from an allenoate-derived compound library, shows efficiency of the enzyme inhibitor to inhibit tumor growth demonstrated using human pancreatic cancer xenograft
PD-083176
-
noncompetitive to geranylgeranyl diphosphate, competitive to GST-CDC42, modest inhibitor
Phenylglyoxal
-
80% loss of activity, inactivation of inhibition in the presence of geranylgeranyl diphosphate
tetrapeptide CVIL
superposition of the crystal structures of the CVIL-GGTase-I complex; superposition of the crystal structures of the CVIL-GGTase-I complex
Thr-Lys-Cys-Val-Ile-Leu
-
potent competitor, 50% inhibition at 0.001 mM
Thr-Lys-Cys-Val-Ile-Met
-
potent competitor, 50% inhibition at 0.008 mM
tipifarnib
the cdc43DELTA mutant is 4fold more susceptible to this farnesyltransferase inhibitor than the wild-type
umbelliprenine
-
0.1 mM, 13.4% inhibition
[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetic acid benzyl ester
-
IC50: above 0.01 mM
{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-acetic acid
-
IC50: above 0.01 mM
{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-acetic acid methyl ester
-
IC50: above 0.01 mM
(2S,5S)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-2,5-dihydro-1H-pyrrole-3-carboxylic acid
-
IC50: 0.0005 mM using RhoA as a substrate, IC50: 0.0009 mM using Ki-Ras4B as a substrate
(2S,5S)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-2,5-dihydro-1H-pyrrole-3-carboxylic acid
-
-
1-phosphono-(E,E,E)-geranylgeraniol
-
competitive to geranylgeranyl diphosphate, noncompetitive to GST-CDC42
1-phosphono-(E,E,E)-geranylgeraniol
-
competitive to geranylgeranyl diphosphate, potent substrate inhibition to dansyl-Gly-Cys-Ile-Ile-Leu
GGTi-2147
specific GGTIbeta enzyme inhibitor; specific GGTIbeta enzyme inhibitor
GGTi-2147
specific GGTIbeta enzyme inhibitor; specific GGTIbeta enzyme inhibitor
GGTi-2147
a potent and selective inhibitor of GGT; potent and selective inhibitor of GGT
GGTi-2147
specific GGTIbeta enzyme inhibitor; specific GGTIbeta enzyme inhibitor
GGTI-298
-
induces apoptosis and augments tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in human lung cancer cells. GGTI-298 induces DR4 and DR5 expression and reduces c-FLIP levels. Enforced c-FLIP expression or DR5 knockdown attenuates apoptosis induced by GGTI-298 and TRAIL combination. DR4 knockdown sensitizes cancer cells to GGTI298/TRAIL-induced apoptosis. The combination of GGTI-298 and TRAIL is more effective than each single agent in decreasing the levels of IkappaBalpha and p-Akt
GGTI-298
-
treatment of airway smooth muscle cells induces expression of p53-dependent proteins, p53 upregulated modulator of apoptosis Noxa, and damage-regulated autophagy modulator DRAM, this is inhibited by the p53 transcriptional activation inhibitor cyclic-pifithrin-alpha. Inhibition of autophagy with bafilomycin-A1 or short-hairpin RNA silencing of Atg7 substantially augments GGTI-298-induced apoptosis
GGTI-DU40
-
1-40 microM dissolved in dimethyl sulfoxide, affects actin cytoskeletal integrity, cell adhesion, cell-cell junctions, myosin II phosphorylation, and membrane localization of GTP-binding proteins in trabecular meshwork cells is tested using immunofluorescence detection and immunoblotting analysis and the effect on aqueous humor outflow
GGTI-DU40
-
5-40 microM dissolved in dimethyl sulfoxide influence cell morphology in a dose and time dependent manner, affects actin cytoskeletal integrity, cell adhesion, cell-cell junctions, myosin II phosphorylation, and membrane localization of GTP-binding proteins in trabecular meshwork cells is tested using immunofluorescence detection and immunoblotting analysis and the effect on aqueous humor outflow (25 and 40 microM)
GGTI-DU40
16.3% inhibition at 50 nM
L-269289
-
inhibitor L-269289 and echinocandins act in a synergistic manner for the treatment of Candida parapilosis
L-269289
-
inhibitor L-269289 and echinocandins act in a synergistic manner for the treatment of Candida tropicalis
L-269289
-
inhibitor L-269289 is active on its own to kill Candida glabrata, and its fungicidal activity is enhanced when combined with caspofungin
additional information
-
not inhibited by valencic acid, 4'-geranyloxybenzoic acid, 4-isopentenyloxy-3-methoxy benzoic acid, and 4-geranyloxy-3-methoxy benzoic acid
-
additional information
-
not inhibited by 3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoic acid methyl ester trifluoroacetate and mono(3,3',3''-(5-(methoxycarbonyl)benzene-1,2,3-triyl)tris(oxy)tripropan-1-aminium) mono(2,2,2-trifluoroacetate)
-
additional information
most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors. Inhibition mechanisms for FTase, EC 2.5.1.58, and GGTase-I are different. Molecular modeling studies of GGTase-I and protein-inhibitor interactions, overview; most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors. Inhibition mechanisms for FTase, EC 2.5.1.58, and GGTase-I are different. Molecular modeling studies of GGTase-I and protein-inhibitor interactions, overview
-
additional information
most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors. Inhibition mechanisms for FTase, EC 2.5.1.58, and GGTase-I are different. Molecular modeling studies of GGTase-I and protein-inhibitor interactions, overview; most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors. Inhibition mechanisms for FTase, EC 2.5.1.58, and GGTase-I are different. Molecular modeling studies of GGTase-I and protein-inhibitor interactions, overview
-
additional information
nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy, liposomal encapsulation and pH-dependent delivery to cancer cells, scheme of synthesis of pH-responsive liposome and the proposed intracellular drug release pathway, method, overview. Liposomal GGTI inhibits protein geranylgeranylation inside the cell and this effect is dependent on the low pH of lysosomes; nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy, liposomal encapsulation and pH-dependent delivery to cancer cells, scheme of synthesis of pH-responsive liposome and the proposed intracellular drug release pathway, method, overview. Liposomal GGTI inhibits protein geranylgeranylation inside the cell and this effect is dependent on the low pH of lysosomes
-
additional information
nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy, liposomal encapsulation and pH-dependent delivery to cancer cells, scheme of synthesis of pH-responsive liposome and the proposed intracellular drug release pathway, method, overview. Liposomal GGTI inhibits protein geranylgeranylation inside the cell and this effect is dependent on the low pH of lysosomes; nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy, liposomal encapsulation and pH-dependent delivery to cancer cells, scheme of synthesis of pH-responsive liposome and the proposed intracellular drug release pathway, method, overview. Liposomal GGTI inhibits protein geranylgeranylation inside the cell and this effect is dependent on the low pH of lysosomes
-
additional information
-
nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy, liposomal encapsulation and pH-dependent delivery to cancer cells, scheme of synthesis of pH-responsive liposome and the proposed intracellular drug release pathway, method, overview. Liposomal GGTI inhibits protein geranylgeranylation inside the cell and this effect is dependent on the low pH of lysosomes; nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy, liposomal encapsulation and pH-dependent delivery to cancer cells, scheme of synthesis of pH-responsive liposome and the proposed intracellular drug release pathway, method, overview. Liposomal GGTI inhibits protein geranylgeranylation inside the cell and this effect is dependent on the low pH of lysosomes
-
additional information
-
inhibitors pose a potential treatment for inflammation, multiple sclerosis, atherosclerosis, and other diseases, 47 potential inhibitors with a predicted IC50 greater than 5.50 microM are identified by the use of quantitative structure-activity relationship models and in vitro tests with 7 of them
-
additional information
-
TKSer-Val-Ile-Leu inactive as competitor
-
additional information
most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors; most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors
-
additional information
most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors; most GGT inhibitors are CAAX-competitive inhibitors, except for a few GGPP-competitive inhibitors
-
additional information
the mammalian PGGT-I inhibitors GGTI-297 and FTI-276 have little effect on Trypanosoma cruzi PGGT-I activity
-
additional information
-
the mammalian PGGT-I inhibitors GGTI-297 and FTI-276 have little effect on Trypanosoma cruzi PGGT-I activity
-
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0.25 - 4
(2S,5R)-5-ethyl-2-(4-fluorophenyl)-1-tosyl-2,5-dihydro-1H-pyrrole-3-carboxylic acid
Homo sapiens
-
IC50: 0.2 mM using RhoA as a substrate, IC50: 0.25 mM using Ki-Ras4B as a substrate
0.0009 - 4
(2S,5S)-5-tert-butyl-2-(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-2,5-dihydro-1H-pyrrole-3-carboxylic acid
Homo sapiens
-
IC50: 0.0005 mM using RhoA as a substrate, IC50: 0.0009 mM using Ki-Ras4B as a substrate
0.002 - 4
(2S,6S)-2,6-bis(4-chlorophenyl)-1-[(2-methylphenyl)sulfonyl]-1,2,5,6-tetrahydropyridine-3-carboxylic acid
Homo sapiens
-
IC50: 0.0003 mM using RhoA as a substrate, IC50: 0.002 mM using Ki-Ras4B as a substrate
0.08 - 4
(2S,6S)-6-(4-fluorophenyl)-1-[(4-methylphenyl)sulfonyl]-2-phenyl-1,2,5,6-tetrahydropyridine-3-carboxylic acid
Homo sapiens
-
IC50: 0.12 mM using RhoA as a substrate, IC50: 0.08 mM using Ki-Ras4B as a substrate
0.0024
(S)-N-(1-amino-3-(4-fluorophenyl)-1-oxopropan-2-yl)-4-((1-(3,4-dichlorophenyl)-4-(2-(methylthio)ethyl)-3-(pyridin-3-yl)-1H-pyrazol-5-yl)oxy)butanamide
Homo sapiens
pH 7.4, 30°C
0.0031
(S)-N-(1-amino-3-(4-methoxyphenyl)-1-oxopropan-2-yl)-4-((1-(3,4-dichlorophenyl)-4-(2-(methylthio)ethyl)-3-(pyridin-3-yl)-1H-pyrazol-5-yl)oxy)butanamide
Homo sapiens
pH 7.4, 30°C
0.021
(S)-N-(4-(3,4-dichlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
Rattus norvegicus
-
pH 7.4, 30°C
0.0323
(S)-N-(4-(3-chlorophenoxy)benzyl)-6-(1H-indol-3-yl)piperazine-2,5-dione
Rattus norvegicus
-
pH 7.4, 30°C
0.006525
1-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-cyclohexanecarboxylic acid
Homo sapiens
-
IC50: 6525 nM
0.01
1-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-cyclohexanecarboxylic acid methyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.0014
11-aminoundecylcarbonyl-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
Rattus norvegicus
-
-
0.000021
2-aryl-4-aminobenzoic acid
Homo sapiens
-
IC50: 21 nM
0.01
2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-N-(3-methyl-butyl)-acetamide
Homo sapiens
-
IC50: above 0.01 mM
0.01
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl] acetylamino}-4-methyl-pentanoic acid methyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.00017 - 0.0063
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid
0.0045 - 0.01
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid methyl ester
0.00058 - 0.0027
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methyl-pentanoic acid
0.01
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methyl-pentanoic acid methyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.00335
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methylsulfanyl-butyric acid
Homo sapiens
-
IC50: 3350 nM
0.01
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methylsulfanyl-butyric acid methyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.008
4-[[([5-[(4-ethylphenoxy)methyl]-4-(1-phenylethyl)-4H-pyrazol-3-yl]sulfanyl)acetyl]amino]benzamide
Rattus norvegicus
-
30°C
0.00007
GGTI-DU40
Sus scrofa
-
complete inhibition at 5 microM, tritium-labelled geranylgeranyl diphosphate for activity assay with lysate of trabecular mesh cells, 30°C
0.0048
L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
Homo sapiens
-
-
0.0014
N-(12-ammoniododecanoyl)-D-cysteinyl-L-valyl-L-isoleucyl-L-leucine trifluoroacetate
Homo sapiens
-
-
0.00098
N-(12-[[(3-[[(3R)-3-ammonio-4-phenylbutyl]oxy]-4,5-bis[[(3S)-3-ammonio-4-phenylbutyl]oxy]phenyl)carbonyl]amino]dodecanoyl)-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine tris(trifluoroacetate)
Homo sapiens
-
-
0.00066
N-(4-[[(3-[[(3R)-3-ammonio-4-phenylbutyl]oxy]-4,5-bis[[(3S)-3-ammonio-4-phenylbutyl]oxy]phenyl)carbonyl]amino]butanoyl)-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine tris(trifluoroacetate)
Homo sapiens
-
-
0.000466
N-([(2S)-2-benzyl-4-[(4-methyl-1H-imidazol-5-yl)methyl]-3-oxopiperazin-1-yl]carbonyl)-L-leucine
Homo sapiens
pH and temperature not specified in the publication
0.035
N-benzyl-2-[(2-chlorobenzyl)[[5-(4-methylphenyl)-2H-tetrazol-2-yl]acetyl]amino]butanamide
Rattus norvegicus
-
30°C
0.043
N-[(E)-1-(benzylcarbamoyl)-2-[5-(3,4-dichlorophenyl)furan-2-yl]ethenyl]-4-methylbenzamide
Rattus norvegicus
-
30°C
0.0006
N-[12-([[3,4,5-tris(3-ammoniopropoxy)phenyl]carbonyl]amino)dodecanoyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine tris(trifluoroacetate)
Homo sapiens
-
-
0.0006
N-[6-(3,4,5-tris(3-amino-1-propoxy)benzoylamino)-undecylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
Rattus norvegicus
-
-
0.00066
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-propylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
Rattus norvegicus
-
-
0.00064 - 0.00098
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-undecylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
0.000313
Na-(4-[[1-(3,4-dichlorophenyl)-4-[2-(methylsulfanyl)ethyl]-3-(pyridin-3-yl)-1H-pyrazol-5-yl]oxy]butanoyl)-L-phenylalaninamide
Homo sapiens
pH and temperature not specified in the publication
0.01
[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetic acid benzyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.01
{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-acetic acid
Homo sapiens
-
IC50: above 0.01 mM
0.01
{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-acetic acid methyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.00017
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid
Homo sapiens
-
IC50: 170 nM
0.0063
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid
Homo sapiens
-
IC50: 0.0063 mM
0.0045
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid methyl ester
Homo sapiens
-
IC50: 4500 nM
0.01
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-3-phenyl-propionic acid methyl ester
Homo sapiens
-
IC50: above 0.01 mM
0.00058
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methyl-pentanoic acid
Homo sapiens
-
IC50: 580 nM
0.0027
2-{2-[3-(1H-imidazol-4-ylmethyl)-2,4-dioxo-3,4-dihydro-2H-quinazolin-1-yl]-acetylamino}-4-methyl-pentanoic acid
Homo sapiens
-
IC50: 2700 nM
0.00064
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-undecylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
Rattus norvegicus
-
-
0.00098
N-[6-(3,4,5-tris(3-amino-4-phenyl-1-butoxy)benzoylamino)-undecylcarbonyl]-L-cysteinyl-L-valyl-L-isoleucyl-L-leucine
Rattus norvegicus
-
-
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evolution
tunable selectivity may be a general phenomenon among multispecific enzymes involved in posttranslational modification and raises the possibility of variable substrate selectivity among GGTase-I orthologues from different organisms
malfunction
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity
malfunction
combined FTase/GGTase-I deficiency significantly reduces K-Ras-induced lung tumors and improves survival without obvious pulmonary toxicity
malfunction
downregulation or inhibition of GGT decreases synaptogenesis
malfunction
GGTase-I inhibition results in proliferation inhibition associated with G1 arrest and accumulation of cell cycle regulators such as p21CIP1/WAF1
malfunction
high K+ or bicuculline-induced increases in dendritic spine density are significantly abolished by enzyme inhibition. GGTI not only regulates the basal neuronal dendritic growth but also mediates neuronal activity and BDNF-induced dendritogenesis. Dendrite development of Purkinje cells is dramatically impeded by downregulation of GGTIbeta expression or inhibiting GGTI activity in cultured cerebellar slices
malfunction
-
loss of enzyme activity results in colonies of round, single-celled organisms that resemble unicellular algae. Enzyme mutants fail to respond to polarized light. Ppggb mutants appear to remain in an undifferentiated state, with no sign of polarity
malfunction
mice with lateral ventricular injection of GGTi-2147, a specific GGTI inhibitor, have significant reduction in the membrane association of Rac1 and in the dendritic spine densities in the hippocampus, the cerebellum, and the frontal cortex
malfunction
overexpression of GGTbeta promotes the linear density of post-synaptic density protein 95 (PSD 95) and synapsin 1, two major molecular markers of synaptogenesis, while downregulation or inhibition of GGT decreases synaptogenesis
malfunction
the related Rac and Ras proteins are not mislocalized in the cdc43DELTA mutant even though they contain similar CaaL motifs, the membrane localization of each of these GTPases is dependent on the prenylation of the CaaX cysteine. The cdc43DELTA mutant has a growth defect at 37°C and 39°C. The cdc43dELTA mutant does not exhibit cell wall defects. The cdc43DELTA mutant is more susceptible to farnesyltransferase inhibitors
malfunction
-
overexpression of GGTbeta promotes the linear density of post-synaptic density protein 95 (PSD 95) and synapsin 1, two major molecular markers of synaptogenesis, while downregulation or inhibition of GGT decreases synaptogenesis
-
malfunction
-
downregulation or inhibition of GGT decreases synaptogenesis
-
physiological function
-
enzyme GGTase-I is abundantly expressed in human primary glioma tissues. Inhibition or downregulation of GGTase-I markedly decreases the proliferation of glioma cells and induces their apoptosis, while overexpression of GGTase-I promotes cell growth in vitro. Inactivation of GGTase-I eliminates geranylgeranylation of RhoA and Rac1, prevents them from targeting to the plasma membrane, and inhibits Rac1 activity. Overexpressing wild type or constitutively active Rac1 stimulates glioma cell growth, similar to the effect of GGTase-I overexpression. Overexpressing dominant-negative Rac1 or Rac1 with the prenylation site deleted or mutated abrogates GGTase-I-induced proliferation in glioma cells
physiological function
-
inhibition or down-regulation using small interference RNA inhibits dendritic development of Purkinje cells. In contrast, up-regulation of enzyme expression promotes dendritic arborization of Purkinje cells. Neuronal depolarization induced by high K+ or treatment with brain-derived neurotrophic factor BDNF promotes membrane association of Rac1 and dendritic development of Purkinje cells in cultured cerebellar slices. The effect of BDNF or high K+ is inhibited by inhibition or down-regulation of enzyme
physiological function
-
pharmacological inhibition of protein geranylgeranyltransferase-I induces simultaneous p53-dependent apoptosis and autophagy in airway smooth muscle cells, and autophagy regulates apoptosis induction
physiological function
Cryptococcus neoformans geranylgeranyltransferase-I is involved in high-temperature growth and morphogenesis. The enzyme belongs to the CaaX prenyltransferases (where CaaX indicates a cysteine followed by two aliphatic amino acids and a variable amino acid) that direct the subcellular localization of a large group of proteins by catalyzing the attachment of hydrophobic isoprenoid moieties onto C-terminal CaaX motifs, thus facilitating membrane association. The enzyme-mediated activity is not essential, but is important for thermotolerance, morphogenesis, and virulence. Ggtase-I function is required for full membrane localization of Rho10 and the two Cdc42 paralogues (Cdc42 and Cdc420). Ggtase-I activity are required for full growth in association with macrophages
physiological function
enzyme GGTase-I has a crucial role in the posttranslational modification of Ras proteins. The enzyme is involved in several diseases, e.g. glaucoma via Rho prenylation, and neurological diseases. GGTase-I catalyzes geranylgeranyl 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
physiological function
enzyme GGTase-I has a crucial role in the posttranslational modification of Ras proteins. The enzyme is involved in several diseases, e.g. glaucoma via Rho prenylation, and neurological diseases. GGTase-I catalyzes geranylgeranyl 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
physiological function
importance of GGTase-I in cell proliferation and cell cycle progression
physiological function
-
protein geranylgeranyltransferase type I is not required for viability, but is required for cell adhesion, polar cell elongation, and cell differentiation
physiological function
role of geranylgeranyltransferase I-mediated protein prenylation in the brain. GGTI and geranylgeranylation are involved in neurodegenerative diseases, e.g., aging, Alzheimer's disease, multiple sclerosis, and Niemann-Pick disease type C, mechanism of GGTI-mediated isoprenylation in the pathogenesis of neurodegenerative and neurodevelopmental disorders, overview. GGTI is localized at the neuromuscular junction and regulates agrin-induced clustering of acetylcholine receptors by interacting with muscle-specific receptor tyrosine kinase. Importance of prenylation in synaptic function. GGTI promotes neuronal dendritogenesis via increasing the membrane association of Rac1 in CNS neurons
physiological function
role of geranylgeranyltransferase I-mediated protein prenylation in the brain. GGTI and geranylgeranylation are involved in neurodegenerative diseases, e.g., aging, Alzheimer's disease, multiple sclerosis, and Niemann-Pick disease type C, mechanism of GGTI-mediated isoprenylation in the pathogenesis of neurodegenerative and neurodevelopmental disorders, overview. Importance of prenylation in synaptic function. GGTI not only regulates the basal neuronal dendritic growth but also mediates neuronal activity and BDNF-induced dendritogenesis. GGTI promotes neuronal dendritogenesis via increasing the membrane association of Rac1 in CNS neurons
physiological function
role of geranylgeranyltransferase I-mediated protein prenylation in the brain. GGTI and geranylgeranylation are involved in neurodegenerative diseases, e.g., aging, Alzheimer's disease, multiple sclerosis, and Niemann-Pick disease type C, mechanism of GGTI-mediated isoprenylation in the pathogenesis of neurodegenerative and neurodevelopmental disorders, overview. Importance of prenylation in synaptic function. GGTI not only regulates the basal neuronal dendritic growth but also mediates neuronal activity and BDNF-induced dendritogenesis. GGTI promotes neuronal dendritogenesis via increasing the membrane association of Rac1 in CNS neurons. Roles of the enzyme in aging, overview
physiological function
role of geranylgeranyltransferase I-mediated protein prenylation in the brain. GGTI and geranylgeranylation are involved in neurodegenerative diseases, e.g., aging, Alzheimer's disease, multiple sclerosis, and Niemann-Pick disease type C, mechanism of GGTI-mediated isoprenylation in the pathogenesis of neurodegenerative and neurodevelopmental disorders, overview. neuromuscular junction. GGTI is localized at the neuromuscular junction and regulates agrin-induced clustering of acetylcholine receptors by interacting with muscle-specific receptor tyrosine kinase. Importance of prenylation in synaptic function. GGTI promotes neuronal dendritogenesis via increasing the membrane association of Rac1 in CNS neurons
physiological function
the enzyme mediates lipid modification of Rho small GTPases, such as Rho, Rac, and Cdc42, which are important for neuronal synaptogenesis. It promotes the basal and neuronal activity and brain-derived neurotrophic factor (BDNF)-induced dendritic morphogenesis of cultured hippocampal neurons and cerebellar slices. Function and mechanism of geranylgeranyltransferase I in neuronal synaptogenesis, enzyme regulation by factors that promote synaptogenesis, overview. The activities of GGT and Rac are regulated by BDNF
physiological function
deleting beta-subunit CDC43 of geranylgeranyltransferase type I confers hypersensitivity to echinocandins. The membrane localization of Rho is disrupted in the CDC43 mutant, resulting in decreased amounts of glucans in the cell wall, thereby exacerbating the cell wall stress upon caspofungin addition
physiological function
-
deletion of CDC43 is lethal in Candida glabrata
physiological function
-
the enzyme mediates lipid modification of Rho small GTPases, such as Rho, Rac, and Cdc42, which are important for neuronal synaptogenesis. It promotes the basal and neuronal activity and brain-derived neurotrophic factor (BDNF)-induced dendritic morphogenesis of cultured hippocampal neurons and cerebellar slices. Function and mechanism of geranylgeranyltransferase I in neuronal synaptogenesis, enzyme regulation by factors that promote synaptogenesis, overview. The activities of GGT and Rac are regulated by BDNF
-
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
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
additional information
the enzyme includes two subunits: an alpha subunit (GGTalpha), the catalytic subunit, that is shared with farnesyltransferase, EC 2.5.1.58, and a distinct beta subunit (GGTbeta), which is responsible for substrate binding
additional information
the enzyme includes two subunits: an alpha subunit (GGTalpha), the catalytic subunit, that is shared with farnesyltransferase, EC 2.5.1.58, and a distinct beta subunit (GGTbeta), which is responsible for substrate binding
additional information
-
the enzyme includes two subunits: an alpha subunit (GGTalpha), the catalytic subunit, that is shared with farnesyltransferase, EC 2.5.1.58, and a distinct beta subunit (GGTbeta), which is responsible for substrate binding
-
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brenda
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Rattus norvegicus
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Rattus norvegicus
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Rattus norvegicus
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Schizosaccharomyces pombe
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1998
Rattus norvegicus
-
brenda
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2004
Rattus norvegicus
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Homo sapiens
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Rattus norvegicus
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Arabidopsis thaliana
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Homo sapiens
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Homo sapiens
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Homo sapiens, Rattus norvegicus
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Mol. Cancer
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2010
Homo sapiens
brenda
Rao, P.V.; Peterson, Y.K.; Inoue, T.; Casey, P.J.
Effects of pharmacologic inhibition of protein geranylgeranyltransferase type I on aqueous humor outflow through the trabecular meshwork
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2008
Homo sapiens, Sus scrofa
brenda
Ghavami, S.; Mutawe, M.; Schaafsma, D.; Yeganeh, B.; Unruh, H.; Klonisch, T.; Halayko, A.
Geranylgeranyl transferase 1 modulates autophagy and apoptosis in human airway smooth muscle
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Homo sapiens
brenda
Qiao, Y.; Gao, J.; Qiu, Y.; Wu, L.; Guo, F.; Lo, K.K.; Li, D.
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2011
Rattus norvegicus
brenda
Zhou, X.; Qian, J.; Hua, L.; Shi, Q.; Liu, Z.; Xu, Y.; Sang, B.; Mo, J.; Yu, R.
Geranylgeranyltransferase I promotes human glioma cell growth through Rac1 membrane association and activation
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2013
Homo sapiens
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Wu, K.; Zhou, X.; Luo, Z.
Geranylgeranyltransferase I is essential for dendritic development of cerebellar Purkinje cells
Mol. Brain
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18
2010
Rattus norvegicus
brenda
Gangopadhyay, S.A.; Losito, E.L.; Hougland, J.L.
Targeted reengineering of protein geranylgeranyltransferase type I selectivity functionally implicates active-site residues in protein-substrate recognition
Biochemistry
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2014
Rattus norvegicus (P53610), Rattus norvegicus (Q04631)
brenda
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
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267-276
2015
Homo sapiens (P49354), Homo sapiens (P53609), Rattus norvegicus (P53610), Rattus norvegicus (Q04631)
brenda
Selvig, K.; Ballou, E.R.; Nichols, C.B.; Alspaugh, J.A.
Restricted substrate specificity for the geranylgeranyltransferase-I enzyme in Cryptococcus neoformans: implications for virulence
Eukaryot. Cell
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2013
Cryptococcus neoformans (J9VNV2), Cryptococcus neoformans
brenda
Li, Z.; Sun, C.; Zhang, T.; Mo, J.; Shi, Q.; Zhang, X.; Yuan, M.; Chen, L.; Mao, X.; Yu, R.; Zhou, X.
Geranylgeranyltransferase I mediates BDNF-induced synaptogenesis
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Rattus norvegicus (P53610), Rattus norvegicus (Q04631), Rattus norvegicus Sprague-Dawley (P53610), Rattus norvegicus Sprague-Dawley (Q04631)
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Gao, S.; Yu, R.; Zhou, X.
The role of geranylgeranyltransferase I-mediated protein prenylation in the brain
Mol. Neurobiol.
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6925-6937
2015
Homo sapiens (P49354), Homo sapiens (P53609), Rattus norvegicus (P53610), Rattus norvegicus (Q04631), Mus musculus (Q61239), Mus musculus (Q8BUY9)
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Thole, J.M.; Perroud, P.F.; Quatrano, R.S.; Running, M.P.
Prenylation is required for polar cell elongation, cell adhesion, and differentiation in Physcomitrella patens
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2014
Physcomitrium patens
brenda
Lu, J.; Yoshimura, K.; Goto, K.; Lee, C.; Hamura, K.; Kwon, O.; Tamanoi, F.
Nanoformulation of geranylgeranyltransferase-I inhibitors for cancer therapy: liposomal encapsulation and pH-dependent delivery to cancer cells
PLoS ONE
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e0137595
2015
Homo sapiens (P49354), Homo sapiens (P53609), Homo sapiens
brenda
Sun, Q.; Xiong, K.; Yuan, Y.; Yu, J.; Yang, L.; Shen, C.; Su, C.; Lu, Y.
Inhibiting fungal echinocandin resistance by small-molecule disruption of geranylgeranyltransferase type i activity
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2020
[Candida] glabrata, Candida parapsilosis, Candida tropicalis, Candida albicans (Q9Y764), Candida albicans
brenda
Ashok, S.; Hildebrandt, E.R.; Ruiz, C.S.; Hardgrove, D.S.; Coreno, D.W.; Schmidt, W.K.; Hougland, J.L.
Protein farnesyltransferase catalyzes unanticipated farnesylation and geranylgeranylation of shortened target sequences
Biochemistry
59
1149-1162
2020
Rattus norvegicus (Q04631 AND Q02293)
brenda
Mansha, M.; Kumari, U.U.; Cournia, Z.; Ullah, N.
Pyrazole-based potent inhibitors of GGT1 Synthesis, biological evaluation, and molecular docking studies
Eur. J. Med. Chem.
124
666-676
2016
Homo sapiens (P49354 and P49356)
brenda