3.4.21.99: spermosin
This is an abbreviated version!
For detailed information about spermosin, go to the full flat file.
Word Map on EC 3.4.21.99
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3.4.21.99
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ascidian
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acrosin
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halocynthia
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trypsin-like
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roretzi
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eggs
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vitelline
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proteasome
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self-sterile
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leupeptin
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gamete
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ubiquitin-proteasome
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hermaphrodite
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peptidyl-argininals
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egf-like
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nonself
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urochordata
- 3.4.21.99
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ascidian
- acrosin
- halocynthia
-
trypsin-like
- roretzi
- eggs
-
vitelline
- proteasome
-
self-sterile
- leupeptin
- gamete
-
ubiquitin-proteasome
-
hermaphrodite
-
peptidyl-argininals
-
egf-like
-
nonself
-
urochordata
Reaction
hydrolyses arginyl bonds, preferably with Pro in the P2 position =
ECTree
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Substrates Products on EC 3.4.21.99 - spermosin
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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
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
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-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
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-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
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-
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
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-
?
additional information
?
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the enzyme binds to the vitelline coat plays a key role in sperm penetration through the vitelline coat during ascidian fertilization
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?
additional information
?
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the enzyme binds to the vitelline coat plays a key role in sperm penetration through the vitelline coat during ascidian fertilization
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?
additional information
?
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the enzyme plays an essential role in fertilization of Halocynthia roretzi
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?
additional information
?
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the enzyme preferentially or specifically splits the Val-Pro-/-Arg bond in synthetic fluorogenic substrates. The enzyme prefers the Pro residue to Leu, Ser and Gly in the P2 position and prefers the Val residue to Leu, Phe and Gly in the p3 position
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?
