Information on EC 3.4.24.84 - Ste24 endopeptidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
3.4.24.84
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RECOMMENDED NAME
GeneOntology No.
Ste24 endopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The peptide bond hydrolysed can be designated -C-/-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Terpenoid backbone biosynthesis
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CAS REGISTRY NUMBER
COMMENTARY hide
316364-97-3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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defective prelamin A processing induces accelerated features of age-related bone loss including lower osteoblast and osteocyte numbers and higher levels of marrow adipogenesis
physiological function
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Zmpste24-null progeroid mice exhibit nuclear lamina defects and accumulate unprocessed prelamin A. Defective prelamin A processing induces accelerated features of age-related bone loss including lower osteoblast and osteocyte numbers and higher levels of marrow adipogenesis. There is a significant loss in trabecular and cortical bone between the Zmpste24 -/- mice compared with the wild-type controls. At 3 months of age, Zmpste24 -/- mice show a significant decrease in bone volume/tissue volume, trabecular thickness, and trabecular number compared with their wild-type littermates
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a-factor + H2O
?
show the reaction diagram
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the enzyme has CAAX endopeptidase activity towards a-factor substrate
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-
?
a-factor + H2O
fragments of a-factor
show the reaction diagram
a-factor-CaaX + H2O
a-factor + aaX
show the reaction diagram
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
a-factor-CAMQ + H2O
a-factor-C + AMQ
show the reaction diagram
-
-
?
a-factor-CVIA + H2O
a-factor-C + VIA
show the reaction diagram
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-
?
CaM53 + H2O
fragments of CaM53
show the reaction diagram
CaM53 is a prenylated C2+-calmodulin from petunia
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?
N-(Ac)-Cys-(farnesyl)-Ser-Ile-Met + H2O
?
show the reaction diagram
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the enzyme can process the prelaminA-specific CAAX sequence
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-
?
prelamin A + H2O
?
show the reaction diagram
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the enzyme removes the farnesylated tail of prelamin A
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?
prelamin A + H2O
lamin A
show the reaction diagram
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cleavage is dependent on processing at the CAAX-box
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-
?
prelamin A + H2O
lamin A + ?
show the reaction diagram
RACU88402 + H2O
fragments of RACU88402
show the reaction diagram
RACU88402 is a Rac-like GTPase
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?
YIIKGVFWDPA(farnesyl)CVIA + H2O
fragments of YIIKGVFWDPA(farnesyl)C + Val-Ile-Ala
show the reaction diagram
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farnesylated 15-mer peptide containing the mature a-factor sequence and the native a-factor CAAX motif
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?
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 + aaX
show the reaction diagram
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removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A,V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position
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?
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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restores Ste24 CAAX proteolytic activity after 1,10-phenanthroline treatment, reactivation with 0.25 mM Co2+ is 25% of that seen with 0.25 mM Zn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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Zn2+ chelator
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
lopinavir
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HIV protease inhibitors inhibit ZMPSTE24, leading to an accumulation of farnesyl-prelamin A. The inhibition of ZMPSTE24 by HIV protease inhibitors could play a role in the side effects of these drugs
lovastatin
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abolishes the conversion of prelamin A into lamin A
o-phenanthroline
tipranavir
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HIV protease inhibitors inhibit ZMPSTE24, leading to an accumulation of farnesyl-prelamin A. The inhibition of ZMPSTE24 by HIV protease inhibitors could play a role in the side effects of these drugs
additional information
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HIV protease inhibitors inhibit ZMPSTE24
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0184
lopinavir
Mus musculus
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0.0012
tipranavir
Mus musculus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
173
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wild-type, pH 7.5, 30°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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SDS-PAGE or immunoblot analyis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-bead-purified
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recombinant His-tagged Ste24, nickel chelate chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
complementation of a ste24 mutant
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expressed in Sf-21 insect cells; expression in CHO-K1 cells; Zmpste24, fused N-terminally to a His6 tag, cloned into the (5')-NheI-(3')-BamHI site of the pcDNA3.1 construct using reverse transcriptase-PCR on HeLa RNA, when cloned into pBacpak8
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expression of AtSte24 in Sacchromyces cerevisiae ste24DELTA mutant
expression of Ste24 in Sacchromyces cerevisiae ste24DELTA mutant
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H335A
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0.4% of wild-type activity
L438F
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1.0% of wild-type activity
L647R
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prelaminaAct mutant, cannot be cleaved by Zmpste24
L94P
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2.8% of wild-type activity
N265S
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4.3% of wild-type activity
P248L
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4.6% of wild-type activity
T159/L209del
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no residual activity
W302X
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the mutation is associated with restrictive dermopathy
W340R
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13.7% of wild-type activity
W450X
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0.3% of wild-type activity
E298A
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ability to complement the mating-defective phenotype of ste24-1 is lost
E298D
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ability to complement the mating-defective phenotype of ste24-1 is lost
H297A
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ability to complement the mating-defective phenotype of ste24-1 is lost
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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