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Information on EC 3.4.24.84 - Ste24 endopeptidase and Organism(s) Mus musculus and UniProt Accession Q80W54

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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:
Mus musculus
UNIPROT: Q80W54 not found.
Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
FACE-1
244
-
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
YIIKGVFWDPA[farnesyl-C]AMQ + H2O
YIIKGVFWDPA[farnesyl-C] + AMQ
show the reaction diagram
-
-
?
YIIKGVFWDPA[farnesyl-C]VIA + H2O
YIIKGVFWDPA[farnesyl-C] + VIA
show the reaction diagram
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lopinavir
-
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
tipranavir
-
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0184
lopinavir
Mus musculus
-
-
0.0012
tipranavir
Mus musculus
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
FACE1_MOUSE
475
7
54735
Swiss-Prot
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Zmste24-deficient mice, Zmpste24 deficiency elicits a stress signaling pathway that is evidenced by a marked upregulation of p53 target genes, accompanied by a senescence phenotype at the cellular level and accelerated ageing at the organismal level
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
existence of a checkpoint response activated by the nuclear abnormalities caused by prelamin A accumulation, hyperactivation of the tumour suppressor p53 may cause accelerated ageing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leung, G.K.; Schmidt, W.K.; Bergo, M.O.; Gavino, B.; Wong, D.H.; Tam, A.; Ashby, M.N.; Michaelis, S.; Young, S.G.
Biochemical studies of Zmpste24-deficient mice
J. Biol. Chem.
276
29051-29058
2001
Mus musculus, Mus musculus (Q80W54)
Manually annotated by BRENDA team
Varela, I.; Cadinanos, J.; Pendas, A.M.; Gutierrez-Fernandez, A.; Folgueras, A.R.; Sanchez, L.M.; Zhou, Z.; Rodriguez, F.J.; Stewart, C.L.; Vega, J.A.; Tryggvason, K.; Freije, J.M.; Lopez-Otin, C.
Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation
Nature
437
564-568
2005
Mus musculus
Manually annotated by BRENDA team
Coffinier, C.; Hudson, S.E.; Farber, E.A.; Chang, S.Y.; Hrycyna, C.A.; Young, S.G.; Fong, L.G.
HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead to an accumulation of prelamin A in cells
Proc. Natl. Acad. Sci. USA
104
13432-13437
2007
Mus musculus
Manually annotated by BRENDA team
Rivas, D.; Li, W.; Akter, R.; Henderson, J.E.; Duque, G.
Accelerated features of age-related bone loss in zmpste24 metalloproteinase-deficient mice
J. Gerontol. A Biol. Sci. Med. Sci.
64
1015-1024
2009
Mus musculus
Manually annotated by BRENDA team
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