BRENDA - Enzyme Database
show all sequences of 3.4.24.84

Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis

Schmidt, W.K.; Tam, A.; Michaelis, S.; J. Biol. Chem. 275, 6227-6233 (2000)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
o-phenanthroline
-
Saccharomyces cerevisiae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
-
Saccharomyces cerevisiae
5783
-
integral to membrane
-
Saccharomyces cerevisiae
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
-
Homo sapiens
additional information
C-terminal proteolytic activity of Ste24 requires metall ions
Saccharomyces cerevisiae
Zn2+
the in vitro N-terminal proteolysis of a-factor requires Zn2+ as metal cofactor, inhibition at higher Zn2+ concentrations e.g. 2 mM
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a-factor + H2O
complements yeast ste24DELTA mutant
638976
Homo sapiens
fragments of a-factor
-
638976
Homo sapiens
-
a-factor + H2O
Ste24 participates in both N- and C-terminal processing steps of a-factor
638976
Homo sapiens
fragments of a-factor
-
638976
Homo sapiens
-
a-factor + H2O
Ste24 participates in both N- and C-terminal processing steps of a-factor
638976
Saccharomyces cerevisiae
fragments of a-factor
-
638976
Saccharomyces cerevisiae
-
a-factor + H2O
mutant a-factor, containing a A8G point mutation is not cleaved suggesting that Ste24 N-terminal protease activity is highly discriminating
638976
Saccharomyces cerevisiae
fragments of a-factor
-
638976
Saccharomyces cerevisiae
-
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
o-phenanthroline
-
Saccharomyces cerevisiae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
-
Saccharomyces cerevisiae
5783
-
integral to membrane
-
Saccharomyces cerevisiae
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
-
Homo sapiens
additional information
C-terminal proteolytic activity of Ste24 requires metall ions
Saccharomyces cerevisiae
Zn2+
the in vitro N-terminal proteolysis of a-factor requires Zn2+ as metal cofactor, inhibition at higher Zn2+ concentrations e.g. 2 mM
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a-factor + H2O
complements yeast ste24DELTA mutant
638976
Homo sapiens
fragments of a-factor
-
638976
Homo sapiens
-
a-factor + H2O
Ste24 participates in both N- and C-terminal processing steps of a-factor
638976
Homo sapiens
fragments of a-factor
-
638976
Homo sapiens
-
a-factor + H2O
Ste24 participates in both N- and C-terminal processing steps of a-factor
638976
Saccharomyces cerevisiae
fragments of a-factor
-
638976
Saccharomyces cerevisiae
-
a-factor + H2O
mutant a-factor, containing a A8G point mutation is not cleaved suggesting that Ste24 N-terminal protease activity is highly discriminating
638976
Saccharomyces cerevisiae
fragments of a-factor
-
638976
Saccharomyces cerevisiae
-
Other publictions for EC 3.4.24.84
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
719313
Ahmad
Homozygous null mutations in Z ...
Homo sapiens
Clin. Genet.
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158-164
2012
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735044
Barrowman
Requirements for efficient pro ...
Homo sapiens
PLoS ONE
7
e32120
2012
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9
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710803
Smigiel
Novel frameshifting mutations ...
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Am. J. Med. Genet. A
152A
447-452
2010
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718809
Goulbourne
HIV protease inhibitors inhibi ...
Homo sapiens
Biochem. Soc. Trans.
38
292-296
2010
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1
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5
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1
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712629
Rivas
Accelerated features of age-re ...
Mus musculus
J. Gerontol. A Biol. Sci. Med. Sci.
64
1015-1024
2009
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2
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678447
Porter
Inhibition of the CaaX proteas ...
Arabidopsis thaliana, Homo sapiens, Saccharomyces cerevisiae
Biochim. Biophys. Acta
1773
853-862
2007
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6
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682549
Coffinier
HIV protease inhibitors block ...
Mus musculus
Proc. Natl. Acad. Sci. USA
104
13432-13437
2007
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2
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4
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667497
Corrigan
Prelamin A endoproteolytic pro ...
Homo sapiens
Biochem. J.
387
129-138
2005
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1
-
1
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2
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3
1
1
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1
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1
1
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669751
Moulson
Homozygous and compound hetero ...
Homo sapiens
J. Invest. Dermatol.
125
913-919
2005
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1
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2
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2
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670378
Varela
Accelerated ageing in mice def ...
Mus musculus
Nature
437
564-568
2005
-
1
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1
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638978
Bracha
The Arabidopsis AtSTE24 is a C ...
Arabidopsis thaliana, Homo sapiens, Saccharomyces cerevisiae
J. Biol. Chem.
277
29856-29864
2002
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1
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2
1
1
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9
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3
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1
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1
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638977
Tam
The multispanning membrane pro ...
Saccharomyces cerevisiae
J. Biol. Chem.
276
46798-46806
2001
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1
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2
2
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2
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1
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1
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652151
Leung
Biochemical studies of Zmpste2 ...
Mus musculus
J. Biol. Chem.
276
29051-29058
2001
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1
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1
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4
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654005
Pei
Type II CAAX prenyl endopeptid ...
Saccharomyces cerevisiae
Trends Biochem. Sci.
26
275-277
2001
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638976
Schmidt
Reconstitution of the Ste24p-d ...
Homo sapiens, Saccharomyces cerevisiae
J. Biol. Chem.
275
6227-6233
2000
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653214
Trueblood
The CaaX proteases, Afc1p and ...
Saccharomyces cerevisiae
Mol. Cell. Biol.
20
4381-4392
2000
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638974
Tam
Dual roles for Ste24p in yeast ...
Homo sapiens, Saccharomyces cerevisiae
J. Cell Biol.
142
635-649
1998
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638975
Schmidt
Endoplasmic reticulum membrane ...
Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
95
11175-11180
1998
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651423
Boyartchuk
Roles pf prenyl protein protea ...
Saccharomyces cerevisiae
Genetics
150
95-1001
1998
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638973
Fujimura-Kamada
A novel membrane-associated me ...
Saccharomyces cerevisiae
J. Cell Biol.
136
271-285
1997
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3
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6
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653884
Boyartchuk.V.L.; Ashby
Modulation of Ras and a-factor ...
Saccharomyces cerevisiae
Science
275
1796-1800
1997
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