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
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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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Inhibitors
Inhibitors on EC 3.4.23.26 - Rhodotorulapepsin
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pepstatin Ac
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60% inhibition at 0.031 mM, addition to cell culture enhances the cell growth and changes the optimal growth temperature
Diazoacetyl-DL-norleucine methyl ester
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5.4; active-site directed irreversible inhibitor; in presence of Cu2+
Diazoacetyl-DL-norleucine methyl ester
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in presence of Cu2+; pH optimum of inactivation: 5.5-6
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most resistant towards Streptomyces-pepsin inhibitor among the acid proteases tested
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