Information on EC 3.4.99.B1 - RCE1

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.99.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
RCE1
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins
show the reaction diagram
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
148463-92-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the deubiquitinating enzyme USP17 negatively regulates the activity of RCE1
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM + H2O
?
show the reaction diagram
2-aminobenzoyl-KSKTKC(farnesyl)dinitrophenyldiaminopropionic acid-IM + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + dinitrophenyldiaminopropionic acid-IM
show the reaction diagram
-
34% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl-IM + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + lysine-epsilon-dinitrophenyl-IM
show the reaction diagram
-
50% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)QLIM + H2O
?
show the reaction diagram
-
cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
-
-
-
2-aminobenzoyl-KSKTKC(farnesyl)VI-dinitrophenyldiaminopropionic acid + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + VI-dinitrophenyldiaminopropionic acid
show the reaction diagram
-
4.8% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + VI-lysine-epsilon-dinitrophenyl
show the reaction diagram
-
25% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)VIM + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + VIM
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-dinitrophenyldiaminopropionic acid-IM + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + dinitrophenyldiaminopropionic acid-IM
show the reaction diagram
-
2.5% of activity with KSKTKC(farnesyl)VIM
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-VI-dinitrophenyldiaminopropionic acid + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VI-dinitrophenyldiaminopropionic acid
show the reaction diagram
-
1% of activity with KSKTKC(farnesyl)VIM
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + lysine-epsilon-dinitrophenyl-IM
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VI-lysine-epsilon-dinitrophenyl
show the reaction diagram
-
2% of activity with KSKTKC(farnesyl)VIM
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VIM + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VIM
show the reaction diagram
-
35% of activity with KSKTKC(farnesyl)VIM
-
?
a-factor + H2O
fragments of a-factor
show the reaction diagram
-
-
-
?
a-factor derived synthetic farnesylated pentadecapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met + H2O
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys + N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
show the reaction diagram
-
i.e. 2-aminobenzoyl-KSKTKC(3-methylbenzophenone prenyl ether)K(dinitrophenyl)IM, an aryl ketone-containing peptide photophore, incorporating a benzophenone-modified isoprenoid, synthesis and structure, mass spectrometrical analysis, overview
mass spectrometrical product analysis
-
?
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met + H2O
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys + N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
show the reaction diagram
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the isoprenylated peptide substrate is derived from the C-terminal sequence of mammalian K-Ras4B, synthesized from 2-aminobenzoyl-KSKTKCK(dinitrophenyl)IM, synthesis and structure, mass spectrometrical analysis, overview
mass spectrometrical product analysis
-
?
CALM + H2O
?
show the reaction diagram
CALQ + H2O
?
show the reaction diagram
CAMQ + H2O
?
show the reaction diagram
CASQ + H2O
?
show the reaction diagram
CSVM + H2O
?
show the reaction diagram
CTLM + H2O
?
show the reaction diagram
CTSM + H2O
?
show the reaction diagram
CTVM + H2O
?
show the reaction diagram
CVIA + H2O
?
show the reaction diagram
dansyl-G(farnesyl)CIIS + H2O
dansyl-G(farnesyl)C + IIS
show the reaction diagram
-
-
-
?
dansyl-GLP(farnesyl)CVVM + H2O
dansyl-GLP(farnesyl)C + VVM
show the reaction diagram
-
-
-
?
dansyl-KTK(farnesyl)CVIM + H2O
dansyl-KTK(farnesyl)C + VIM
show the reaction diagram
-
-
-
?
dansyl-SAK(farnesyl)CVLS + H2O
dansyl-SAK(farnesyl)C + VLS
show the reaction diagram
-
-
-
?
dansyl-WDPA(farnesyl)CVIA + H2O
dansyl-WDPA(farnesyl)C + VIA
show the reaction diagram
-
-
-
?
dansyl-WDPA(geranylgeranyl)CVIA + H2O
dansyl-WDPA(geranylgeranyl)C + VIA
show the reaction diagram
-
-
-
?
farnesyl-Ha-Ras-CaaX + H2O
farnesyl-Ha-Ras-C + aaX
show the reaction diagram
-
-
?
farnesyl-Ki-Ras-CaaX + H2O
farnesyl-Ki-Ras-C + aaX
show the reaction diagram
specific for prenylated proteins containing a C-terminal CaaX motif
-
?
farnesyl-N-Ras-CaaX + H2O
farnesyl-N-Ras-C + aaX
show the reaction diagram
-
-
?
G-gamma1-CaaX + H2O
G-gamma1-C + aaX
show the reaction diagram
-
-
?
geranylgeranyl-Ki-Ras-CaaX + H2O
geranylgeranyl-Ki-Ras-C + aaX
show the reaction diagram
-
-
?
geranylgeranyl-Rab1b-CaaX + H2O
geranylgeranyl-Rab1b-C + aaX
show the reaction diagram
-
-
?
K-Ras(farnesyl)VIM + H2O
K-Ras(farnesyl) + VIM
show the reaction diagram
-
-
-
?
KSKTKC(farnesyl)VI + H2O
?
show the reaction diagram
-
a better substrate for hRCE1 than a KSKTKC(f)VIM
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-
?
KSKTKC(farnesyl)VIM + H2O
KSKTKC(farnesyl) + VIM
show the reaction diagram
-
no activity with unfarnesylated peptides
-
?
KWDPA(farnesyl)CVIA + H2O
KWDPA(farnesyl)C + VIA
show the reaction diagram
-
-
-
?
KWDPAC(S-trans,trans-farnesyl)VIA + H2O
KWDPAC(S-trans,trans-farnesyl) + VIA
show the reaction diagram
-
-
-
?
N-acetyl-S-farnesyl-Cys-Val-Ile-Ser + H2O
N-acetyl-S-farnesyl-Cys + Val-Ile-Ser
show the reaction diagram
-
-
-
-
?
N-Boc-S-farnesyl-L-Cys-Val-Ile-Met + H2O
N-Boc-S-farnesyl-L-Cys + Val-Ile-Met
show the reaction diagram
-
-
-
-
?
phosphodiesterase 6 + H2O
?
show the reaction diagram
-
-
-
?
Ras + H2O
fragments of Ras
show the reaction diagram
-
-
-
?
Ras-CaaX + H2O
Ras-C + aaX
show the reaction diagram
-
a stands for aliphatic amino acid, X is any amino acid
-
?
Ras2 + H2O
Ras2-C + aaX
show the reaction diagram
-
a stands for aliphatic amino acid, X is any amino acid
-
?
YIIKGVFWDPAC(farnesyl)-VIA + H2O
a-factor + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a-factor + H2O
fragments of a-factor
show the reaction diagram
-
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
K-Ras(farnesyl)VIM + H2O
K-Ras(farnesyl) + VIM
show the reaction diagram
-
-
-
?
Ras + H2O
fragments of Ras
show the reaction diagram
-
-
-
?
Ras-CaaX + H2O
Ras-C + aaX
show the reaction diagram
-
a stands for aliphatic amino acid, X is any amino acid
-
?
Ras2 + H2O
Ras2-C + aaX
show the reaction diagram
-
a stands for aliphatic amino acid, X is any amino acid
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
probably a metallo-dependent enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
beta-(2-naphthyl)-Ala-CH2Cl
-
affinity labeling agent of the enzyme
Ca2+
-
0.087 mM, 97% inhibition
Co2+
-
0.087 mM, 48% inhibition
Cu+
-
0.087 mM, 97% inhibition
Mersalyl acid
-
0.022 mM, 99% inhibition
methyl methanothiosulfonate
-
0.05 mM, 40% inhibition
N-Boc-Cys(farnesyl)-methylenamin-VIM-OH
N-Boc-S-farnesyl-L-cys-CH2Cl
-
-
N-Boc-S-farnesyl-L-cysteine aldehyde
-
potent competetive inhibitor
N6-[1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl]-N2-{4,15-dioxo-19-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-8,11,14-trioxa-5-azanonadecan-1-oyl}-L-lysyl-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-{(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl}-L-cysteinyl-N6-{3-[hydroxy(oxo)ammonio]-5-nitrophenyl}-L-lysyl-L-isoleucyl-L-methionine
-
labels the active site by crosslinking to the biotinylated probe, competitive to Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
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Nalpha-tosyl-L-lysine chloromethyl ketone
-
0.3 mM, 32% inhibition
Nalpha-tosyl-L-phenylalanine chloromethyl ketone
-
0.3 mM, 94% inhibition
Ni2+
-
0.087 mM, 48% inhibition
p-chloromercuribenzoate
-
inactivates the partially purified enzyme, with 0.005 mM substantial inhibition
p-hydroxymercuribenzoic acid
-
0.022 mM, 99% inhibition
p-Hydroxymercuriphenylsulfonic acid
-
0.022 mM, 99% inhibition
pseudo peptide R (CH2-NH)
-
-
-
RPI
farnesyl-peptide analogue, 0.000005 mM, 50% inhibition
Tos-Phe-CH2Cl
-
affinity labeling agent of the enzyme
tosyl-L-lysyl-chloromethylketone
tosyl-L-phenylalanyl-chloromethylketone
USP17
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USP17 deubiquitinates RCE1 and negatively regulates the activity of RCE1. Constitutive expression of USP17 blocks cell growth and decreases Ras activation, knockdown of USP17 expression results in a marked elevation in the level of GTP-bound Ras. USP17 and RCE1 co-localize at the endoplasmic reticulum
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additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
2-aminobenzoyl-KSKTKC(farnesyl)
-
-
0.003
2-aminobenzoyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl-IM
-
-
0.004
2-aminobenzoyl-KSKTKC(farnesyl)VI
-
-
0.004
2-aminobenzoyl-KSKTKC(farnesyl)VI-dinitrophenyldiaminopropionic acid
-
-
0.005
2-aminobenzoyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl
-
-
0.004
2-aminobenzoyl-KSKTKC(farnesyl)VIM
-
-
0.004
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-dinitrophenyldiaminopropionic acid-IM
-
-
0.005
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-VI-dinitrophenyldiaminopropionic acid
-
-
0.006
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl
-
-
0.004
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl
-
-
0.004
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VIM
-
-
0.00144 - 0.00326
a-factor derived synthetic farnesylated pentadecapeptide
0.0019
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
-
pH 7.5, 30°C
0.0064
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
-
pH 7.5, 30°C
0.002
K-Ras(farnesyl)VIM
-
-
-
0.0005
Ki-Ras
farnesylated or geranylgeranylated
-
0.004
KSKTKC(farnesyl)VIM
-
-
0.0028
KWDPA(farnesyl)CVIA
-
37°C
0.0057
N-acetyl-S-farnesyl-L-cysteinyl-L-valyl-L-isoleucyl-L-serine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
N-Boc-S-farnesyl-L-cys-CH2Cl
-
-
0.002
N-Boc-S-farnesyl-L-cysteine aldehyde
-
-
0.000085
pseudo peptide R (CH2-NH)
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000251
-
with N-acetyl-S-farnesyl-Cys+Val-Ile-Ser as substrate
0.00974
-
in extract of membrane preparation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
pH 6.0: 65% of maximal activity, pH 7.5: optimal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the inactivation of Rce1 actually increases peripheral leukocytosis, increases the release of immature hematopoietic cells into the circulation and the infiltration of cells into liver and spleen, and causes mice to die more rapidly
Manually annotated by BRENDA team
additional information
-
Sf9 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
RCE1 colocalizes with USP17 in the endoplasmic reticulum
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
-
fibroblast
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
RCE1 is regulated by ubiquination, deubiquitinating enzyme USP17 negatively regulates the activity of RCE1, overview
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
-
expression in Sf9 cells
-
expression in Sf9 insect cells
into the retroviral transfer vector pREX
-
membranes from Sf9 cells expressing the RCE1 ortholog of Leishmania major show proteolytic activity against farnesylated RAS-CVIM
-
membranes from Sf9 cells expressing the RCE1 ortholog of Trypanosoma brucei show proteolytic activity against farnesylated RAS-CVIM
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C139A
-
Yersinia enterocolitca outer protein T mutant, catalytically inactive
E139K
-
increase in proteolysis of a-factor-CAMQ
E156D
-
marginal activity, overexpression significantly boosts the activity
F189L
-
increase in proteolysis of a-factor-CAMQ
H184A
-
inactivation
H186A
-
no inactivation
H187A
-
no inactivation
H284A
-
inactivation
Q201R
-
increase in proteolysis of a-factor-CAMQ
Y160A
-
diminished but significant activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
-
Rce1-mediated removal of of the last three amino acids from isoprenylated Rho GTPases is required for the proteolytic activity of Yersinia enterocolitca outer protein T in living cells