3.4.24.84: Ste24 endopeptidase
This is an abbreviated version!
For detailed information about Ste24 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.84
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3.4.24.84
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lamins
-
prelamin
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progeroid
-
farnesylated
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hutchinson-gilford
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metalloprotease
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laminopathies
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dermopathy
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lipodystrophy
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mandibuloacral
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farnesyltransferase
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clavicles
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misshapen
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ste14p
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acro-osteolysis
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carboxylmethylation
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micrognathia
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medicine
- 3.4.24.84
- lamins
-
prelamin
-
progeroid
-
farnesylated
-
hutchinson-gilford
- metalloprotease
- laminopathies
-
dermopathy
- lipodystrophy
-
mandibuloacral
-
farnesyltransferase
-
clavicles
-
misshapen
-
ste14p
- acro-osteolysis
-
carboxylmethylation
- micrognathia
- medicine
Reaction
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, Zmpste24
ECTree
3.4.24.84 Ste24 endopeptidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.84 - Ste24 endopeptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abz-K-SKTKC(farnesyl)VI(-dinitrophenyl derivative of lysine) + H2O
?
-
-
-
?
CaM53 + H2O
fragments of CaM53
CaM53 is a prenylated C2+-calmodulin from petunia
-
?
METP-(639aa)-RSYLLGNSSPRTQSPQNC(farnesyl)-OCH3 + H2O
METP-(639aa)-RSY + LLGNSSPRTQSPQNC(farnesyl)-OCH3
-
-
-
?
N-(Ac)-Cys-(farnesyl)-Ser-Ile-Met + H2O
?
-
the enzyme can process the prelaminA-specific CAAX sequence
-
-
?
prelamin A + H2O
?
the enzyme removes the farnesylated tail of prelamin A
-
-
?
prelamin A + H2O
lamin A
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cleavage is dependent on processing at the CAAX-box
-
-
?
RACU88402 + H2O
fragments of RACU88402
RACU88402 is a Rac-like GTPase
-
?
YIIKGVFWDPA(farnesyl)CVIA + H2O
YIIKGVFWDPA(farnesyl)C + Val-Ile-Ala
-
farnesylated 15-mer peptide containing the mature a-factor sequence and the native a-factor CAAX motif
-
?
YIIKGVFWDPA[farnesyl-C]AMQ + H2O
YIIKGVFWDPA[farnesyl-C] + AMQ
-
-
?
YIIKGVFWDPA[farnesyl-C]VIA + H2O
YIIKGVFWDPA[farnesyl-C] + VIA
-
-
?
a-factor + H2O
?
-
the enzyme has CAAX endopeptidase activity towards a-factor substrate
-
-
?
a-factor + H2O
fragments of a-factor
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complements yeast ste24DELTA mutant
-
?
a-factor + H2O
fragments of a-factor
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complements yeast ste24DELTA mutant
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
?
a-factor + H2O
fragments of a-factor
-
mating pheromone a-factor
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 participates in both N- and C-terminal processing steps of a-factor
-
?
a-factor + H2O
fragments of a-factor
-
mutant a-factor, containing a A8G point mutation is not cleaved suggesting that Ste24 N-terminal protease activity is highly discriminating
-
?
a-factor + H2O
fragments of a-factor
-
Ste24 is required for the first of the two N-terminal processing steps of mating pheromone a-factor
-
-
?
a-factor-CaaX + H2O
a-factor + aaX
-
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 + aaX
-
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
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CAAX motif, enzyme may also play a role in amino-terminal proteolytic processing of a-factor
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
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endoproteolytic cleavage of a C-terminal tripeptide of prenylated proteins with a CaaX motif
-
?
prelamin A + H2O
lamin A + ?
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enzyme cleaves the prenylated and carboxylmethylated 15-amino acid tail from the C-terminus of prelamin A to yield mature lamin. Mutations in the lamin A gene that eliminate the ZMPSTE24 cleavage site lead to the premature aging disease Hutchinson-Gilford Progeria Syndrome
-
?
prelamin A + H2O
lamin A + ?
the C-terminal 41 amino acids of prelamin A contain sufficient context to allow cleavage of the tail by ZMPSTE24. Mutations in amino acids immediately surrounding the cleavage site (between Y646 and L647) interfere with efficient cleavage of the prelamin A tail, e,g R644C, L648A and N650A, in addition to L647R. 9 of the 15 residues within the cleaved tail that lie immediately upstream of the CAAX motif are not critical for ZMPSTE24-mediated cleavage, duplication of the same 9 amino acids impairs the ability of ZMPSTE24 to cleave prelamin A
-
-
?
prelamin A + H2O
lamin A + ?
-
cleavage occurs between the farnesylated cysteine and the A1 position of the CAAX motif, although the prelamin A peptide is predominantly cleaved between A1 and A2
-
-
?
additional information
?
-
the enzyme does not cleave mutant prelamin A (L647R)
-
-
?
additional information
?
-
-
the enzyme does not cleave mutant prelamin A (L647R)
-
-
?
