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Information on EC 3.4.24.84 - Ste24 endopeptidase and Organism(s) Homo sapiens and UniProt Accession O75844

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.84 Ste24 endopeptidase
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: O75844 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
Synonyms
a-factor converting enzyme, Afc1, Afc1p, At Ste24p, AtSte24, CAAX prenyl protease 1 homolog, FACE-1, Hs Ste24p, Sc Ste24p, Ste24p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CAAX prenyl protease 1 homolog
268564
-
FACE-1
247
-
Hs Ste24p
247
-
Ste24p
-
-
-
-
Zmpste24
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
316364-97-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prelamin A + H2O
?
show the reaction diagram
-
the enzyme removes the farnesylated tail of prelamin A
-
-
?
prelamin A + H2O
lamin A + ?
show the reaction diagram
a-factor + H2O
?
show the reaction diagram
-
the enzyme has CAAX endopeptidase activity towards a-factor substrate
-
-
?
a-factor + H2O
fragments of a-factor
show the reaction diagram
N-(Ac)-Cys-(farnesyl)-Ser-Ile-Met + H2O
?
show the reaction diagram
-
the enzyme can process the prelaminA-specific CAAX sequence
-
-
?
prelamin A + H2O
lamin A
show the reaction diagram
-
cleavage is dependent on processing at the CAAX-box
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
Zn2+-dependent active site
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
Zn2+ chelator
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 41% inhibition, inhibition is not reversible
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 68% inhibition, inhibition is not reversible
lovastatin
-
abolishes the conversion of prelamin A into lamin A
additional information
-
HIV protease inhibitors inhibit ZMPSTE24
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
173
-
wild-type, pH 7.5, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
FACE1_HUMAN
475
7
54813
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
SDS-PAGE or immunoblot analyis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H335A
-
0.4% of wild-type activity
L362F
L438F
-
1.0% of wild-type activity
L94P
-
2.8% of wild-type activity
N265S
-
4.3% of wild-type activity
P248L
-
4.6% of wild-type activity
T159/L209del
-
no residual activity
W302X
-
the mutation is associated with restrictive dermopathy
W340R
-
13.7% of wild-type activity
W450X
-
0.3% of wild-type activity
L647R
-
prelaminaAct mutant, cannot be cleaved by Zmpste24
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Ni-bead-purified
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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
-
expression of Ste24 in Sacchromyces cerevisiae ste24DELTA mutant
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
mutations in the ZMPSTE24 gene lead to incomplete maturation of prelamin A and as a consequence to the premature aging disease Hutchinson-Gilford Progeria Syndrome. In general, the residual activity of ZMPSTE24 patient alleles correlates with disease severity. Complete loss-of-function alleles are associated with restrictive dermopathy, whereas retention of partial, measureable activity results in mandibuloacral dysplasia type B or severe progeria
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tam, A.; Nouvet, F.J.; Fujimura-Kamada, K.; Slunt, H.; Sisodia, S.S.; Michaelis, S.
Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing
J. Cell Biol.
142
635-649
1998
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schmidt, W.K.; Tam, A.; Michaelis, S.
Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
J. Biol. Chem.
275
6227-6233
2000
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bracha, K.; Lavy, M.; Yalovsky, S.
The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
J. Biol. Chem.
277
29856-29864
2002
Arabidopsis thaliana (Q8RX88), Homo sapiens (O75844), Saccharomyces cerevisiae (P47154), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Corrigan, D.P.; Kuszczak, D.; Rusinol, A.E.; Thewke, D.P.; Hrycyna, C.A.; Michaelis, S.; Sinensky, M.S.
Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24
Biochem. J.
387
129-138
2005
Homo sapiens
Manually annotated by BRENDA team
Moulson, C.L.; Go, G.; Gardner, J.M.; van der Wal, A.C.; Smitt, J.H.; van Hagen, J.M.; Miner, J.H.
Homozygous and compound heterozygous mutations in ZMPSTE24 cause the laminopathy restrictive dermopathy
J. Invest. Dermatol.
125
913-919
2005
Homo sapiens
Manually annotated by BRENDA team
Porter, S.B.; Hildebrandt, E.R.; Breevoort, S.R.; Mokry, D.Z.; Dore, T.M.; Schmidt, W.K.
Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones
Biochim. Biophys. Acta
1773
853-862
2007
Arabidopsis thaliana, Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Smigiel, R.; Jakubiak, A.; Esteves-Vieira, V.; Szela, K.; Halon, A.; Jurek, T.; Levy, N.; De Sandre-Giovannoli, A.
Novel frameshifting mutations of the ZMPSTE24 gene in two siblings affected with restrictive dermopathy and review of the mutations described in the literature
Am. J. Med. Genet. A
152A
447-452
2010
Homo sapiens
Manually annotated by BRENDA team
Goulbourne, C.N.; Vaux, D.J.
HIV protease inhibitors inhibit FACE1/ZMPSTE24: a mechanism for acquired lipodystrophy in patients on highly active antiretroviral therapy?
Biochem. Soc. Trans.
38
292-296
2010
Homo sapiens, Homo sapiens (O75844)
Manually annotated by BRENDA team
Ahmad, Z.; Phadke, S.R.; Arch, E.; Glass, J.; Agarwal, A.K.; Garg, A.
Homozygous null mutations in ZMPSTE24 in restrictive dermopathy: evidence of genetic heterogeneity
Clin. Genet.
81
158-164
2012
Homo sapiens (O75844)
Manually annotated by BRENDA team
Barrowman, J.; Hamblet, C.; Kane, M.; Michaelis, S.
Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24
PLoS ONE
7
e32120
2012
Homo sapiens, Homo sapiens (O75844)
Manually annotated by BRENDA team
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