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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pH Stability
pH Stability on EC 3.4.23.26 - Rhodotorulapepsin
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5 - 8
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the enzyme is stable at pH up to 5.0 and retains on average, 50% of its maximal activity at pH 7.3, but no more than 5% after a 4-h incubation at pH 8.0
753717