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Information on EC 3.4.24.84 - Ste24 endopeptidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P47154

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.84 Ste24 endopeptidase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P47154 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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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
zmpste24, ste24p, face-1, atste24, afc1p, hs ste24p, a-factor converting enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Afc1
a-factor converting enzyme
a-factor converting enzyme
-
-
Ste24p
-
-
-
-
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
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
?
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
YIIKGVFWDPA(farnesyl)CVIA + H2O
YIIKGVFWDPA(farnesyl)C + Val-Ile-Ala
show the reaction diagram
-
farnesylated 15-mer peptide containing the mature a-factor sequence and the native a-factor CAAX motif
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
?
a-factor + H2O
fragments of a-factor
show the reaction diagram
a-factor-CaaX + H2O
a-factor + aaX
show the reaction diagram
-
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
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
show the reaction diagram
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
probably Zn2+-dependent metalloprotease
Co2+
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 22% inhibition, inhibition is not reversible
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 76% inhibition, inhibition is not reversible
o-phenanthroline
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52300
-
x * 52300, deduced from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52300, deduced from nucleotide sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E298A
-
ability to complement the mating-defective phenotype of ste24-1 is lost
E298D
-
ability to complement the mating-defective phenotype of ste24-1 is lost
H297A
-
ability to complement the mating-defective phenotype of ste24-1 is lost
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged Ste24, nickel chelate chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
complementation of a ste24 mutant
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujimura-Kamada, K.; Nouvet, F.J.; Michaelis, S.
A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor
J. Cell Biol.
136
271-285
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Schmidt, W.K.; Tam, A.; Fujimura-Kamada, K.; Michaelis, S.
Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
Proc. Natl. Acad. Sci. USA
95
11175-11180
1998
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
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Tam, A.; Schmidt, W.K.; Michaelis, S.
The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor
J. Biol. Chem.
276
46798-46806
2001
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
Homo sapiens (O75844), Saccharomyces cerevisiae (P47154), Saccharomyces cerevisiae, Arabidopsis thaliana (Q8RX88)
Manually annotated by BRENDA team
Boyartchuk, V.L.; Rine, J.
Roles pf prenyl protein proteases in maturation of Saccharomyces cerevisiae
Genetics
150
95-1001
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Trueblood, C.E.; Boyartchuk, V.L.; Picologlou, E.A.; Rozema, D.; Poulter, C.D.; Rine, J.
The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities
Mol. Cell. Biol.
20
4381-4392
2000
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Boyartchuk.V.L.; Ashby, M.N.; Rine, J.
Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
Science
275
1796-1800
1997
Saccharomyces cerevisiae (P47154)
Manually annotated by BRENDA team
Pei, J.; Grishin, N.V.
Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
Trends Biochem. Sci.
26
275-277
2001
Saccharomyces cerevisiae
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, Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team