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
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r-factors
- rhizopuspepsin
- rhizopus
- diazoacetyl-dl-norleucine
- trypsinogen
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beta-hairpins
- penicillopepsin
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statine-containing
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non-hydrogen
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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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Substrates Products
Substrates Products on EC 3.4.23.26 - Rhodotorulapepsin
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REACTION DIAGRAM
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preferential cleavage of: Tyr-Ile and Leu-Val, at a lower rate: Val-Tyr and Leu-Leu
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Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
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preferential cleavage of: Tyr-Ile and Leu-Val, at a lower rate: Val-Tyr and Leu-Leu
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Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
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Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
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Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
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Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
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Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
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Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
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Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
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Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
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Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
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DRVY + IHPFHLL + VYS
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tetradecapaptide renin substrate, cleavage pattern, overview
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DRVYIHPFHLLVYS + H2O
DRVY + IHPFHLL + VYS
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tetradecapaptide renin substrate, cleavage pattern, overview
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substrate specificity, overview, high activity with increasing chain length and Ala at the N-terminal side of the scissile bond, no activity with Z-Lys-Ala-Ala
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additional information
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substrate specificity, overview, high activity with increasing chain length and Ala at the N-terminal side of the scissile bond, no activity with Z-Lys-Ala-Ala
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