3.4.23.41: yapsin 1
This is an abbreviated version!
For detailed information about yapsin 1, go to the full flat file.
Word Map on EC 3.4.23.41
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3.4.23.41
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prohormone
-
granules
-
monobasic
-
propeptide
-
aspartyl
-
pituitary
-
cholecystokinin
-
non-anchored
-
tetrabasic
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parathyroid
-
pepstatin
-
endoglycosidase
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acth
-
zymogen
-
pheromone
-
dibasic
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pro-opiomelanocortin
-
proproteins
-
residue-specific
-
prohormone-processing
-
synthesis
-
medicine
- 3.4.23.41
-
prohormone
- granules
-
monobasic
- propeptide
-
aspartyl
-
pituitary
- cholecystokinin
-
non-anchored
-
tetrabasic
- parathyroid
- pepstatin
-
endoglycosidase
- acth
- zymogen
- pheromone
-
dibasic
- pro-opiomelanocortin
- proproteins
-
residue-specific
-
prohormone-processing
- synthesis
- medicine
Reaction
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions =
Synonyms
aspartic protease yapsin I, aspartic proteinase 3, Kex2, More, opsA, Yap3 gene product, yeast aspartic protease, yeast aspartic protease 3, YPS1, YPS7
ECTree
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Reaction
Reaction on EC 3.4.23.41 - yapsin 1
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hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
cleavage is enhanced in substrates having additional basic residues flanking the P1 site
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hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
cleaves at mono-, di-, and multi-basic cleavage sites
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