3.4.23.26: Rhodotorulapepsin
This is an abbreviated version!
For detailed information about Rhodotorulapepsin, go to the full flat file.
Word Map on EC 3.4.23.26
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3.4.23.26
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3.4.23.6
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proteinases
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pepstatin
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endothiapepsin
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renin
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r-factors
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rhizopuspepsin
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rhizopus
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diazoacetyl-dl-norleucine
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trypsinogen
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beta-hairpins
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penicillopepsin
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statine-containing
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non-hydrogen
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hydroxyethylene
- 3.4.23.26
-
3.4.23.6
- proteinases
- pepstatin
- endothiapepsin
- renin
-
r-factors
- rhizopuspepsin
- rhizopus
- diazoacetyl-dl-norleucine
- trypsinogen
-
beta-hairpins
- penicillopepsin
-
statine-containing
-
non-hydrogen
-
hydroxyethylene
Reaction
Specificity similar to that of pepsin A. Cleaves Z-Lys-/-Ala-Ala-Ala and activates trypsinogen =
Synonyms
Cladosporium acid protease, Cladosporium acid proteinase, EC 3.4.23.6, EC 3.4.4.17, EC 3.4.99.15, extracellular acid protease, Paecilomyces proteinase, Proteinase, Cladosporium aspartic, Proteinase, Paecilomyces, Proteinase, Rhodotorula glutinis aspartic, Proteinase, Rhodotorula glutinis aspartic, II, Rhodotorula acid proteinase, Rhodotorula aspartic proteinase, Rhodotorula glutinis acid proteinase
ECTree
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Temperature Stability
Temperature Stability on EC 3.4.23.26 - Rhodotorulapepsin
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50 - 60
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the enzyme is highly stable at temperature below 50°C. After 30 min of incubation at 55°C, the residual proteolytic activity is 24% lower than its initial value, and at 60°C the activity loss is 88%
70