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Cladosporium acid protease
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Cladosporium acid proteinase
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EC 3.4.23.6
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formerly
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EC 3.4.4.17
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formerly, part transferred
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EC 3.4.99.15
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formerly
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extracellular acid protease
Paecilomyces proteinase
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Proteinase, Cladosporium aspartic
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Proteinase, Paecilomyces
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Proteinase, Rhodotorula glutinis aspartic
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Proteinase, Rhodotorula glutinis aspartic, II
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Rhodotorula acid proteinase
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Rhodotorula aspartic proteinase
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Rhodotorula glutinis acid proteinase
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extracellular acid protease
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extracellular acid protease
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Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
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Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
Copoly-L-Leu-L-Lys*HBr + H2O
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Copoly-L-Leu-L-Orn-NH2*HBr + H2O
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DRVYIHPFHLLVYS + H2O
DRVY + IHPFHLL + VYS
Gly-Leu-Tyr + H2O
Gly-Leu + Tyr
Z-Lys-Ala-Ala-Ala + H2O
Z-Lys + Ala-Ala-Ala
Z-Lys-Leu-Ala-Ala + H2O
Z-Lys + Leu-Ala-Ala
additional information
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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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?
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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azocasein + H2O
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azocasein + H2O
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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-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-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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Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
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casein + H2O
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casein + H2O
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high activity
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casein + H2O
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high activity
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Copoly-L-Leu-L-Lys*HBr + H2O
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1:1, DPn: 50
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Copoly-L-Leu-L-Lys*HBr + H2O
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1:1, DPn: 50
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Copoly-L-Leu-L-Orn-NH2*HBr + H2O
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1:1, DPn: 50
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Copoly-L-Leu-L-Orn-NH2*HBr + H2O
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1:1, DPn: 50
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Copoly-L-Leu-L-Orn-NH2*HBr + H2O
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1:1, DPn: 50
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Copoly-L-Leu-L-Orn-NH2*HBr + H2O
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1:1, DPn: 50
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DRVYIHPFHLLVYS + H2O
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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Gly-Leu-Tyr + H2O
Gly-Leu + Tyr
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Gly-Leu-Tyr + H2O
Gly-Leu + Tyr
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Gly-Leu-Tyr + H2O
Gly-Leu + Tyr
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Gly-Leu-Tyr + H2O
Gly-Leu + Tyr
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Hemoglobin + H2O
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Hemoglobin + H2O
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Hemoglobin + H2O
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Hemoglobin + H2O
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Z-Lys-Ala-Ala-Ala + H2O
Z-Lys + Ala-Ala-Ala
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Z-Lys-Ala-Ala-Ala + H2O
Z-Lys + Ala-Ala-Ala
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Z-Lys-Leu-Ala-Ala + H2O
Z-Lys + Leu-Ala-Ala
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Z-Lys-Leu-Ala-Ala + H2O
Z-Lys + Leu-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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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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1,2-epoxy-3-(4-nitrophenoxy)propane
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4-bromo-phenacylbromide
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alpha-Diazo-p-bromo acetophenone
diazoacetyl glycine ethyl ester
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Diazoacetyl-DL-norleucine methyl ester
Diazoacetyl-Gly ethyl ester
N-Diazoacetyl-N'-2,4-dinitrophenylethylenediamine
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p-bromophenacyl bromide
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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
sodium lauryl sulfate
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Streptomyces-pepsin inhibitor
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alpha-Diazo-p-bromo acetophenone
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alpha-Diazo-p-bromo acetophenone
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weak
Diazoacetyl-DL-norleucine methyl ester
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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
Diazoacetyl-DL-norleucine methyl ester
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in presence of Cu2+
Diazoacetyl-DL-norleucine methyl ester
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i.e. DAN
Diazoacetyl-Gly ethyl ester
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Diazoacetyl-Gly ethyl ester
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in presence of cupric ions
Streptomyces-pepsin inhibitor
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most resistant towards Streptomyces-pepsin inhibitor among the acid proteases tested
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Streptomyces-pepsin inhibitor
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from Streptomyces naniwaensis
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Majima, E.; Oda, K.; Murao, S.; Ichishima, E.
Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate
Agric. Biol. Chem.
52
787-793
1988
Rhodotorula glutinis, Rhodotorula glutinis K-24
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brenda
Takahashi, K.; Chang, W.J.
The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin
J. Biochem.
80
497-506
1976
Paecilomyces variotii
brenda
Murao, S.; Funakoshi, S.; Oda, K.
Acid protease of Cladosporium species No. 45-2. I. Purification, crystallization, and some enzymic properties of acid protease of Cladosporium species No. 45-2
Agric. Biol. Chem.
36
1327-1333
1972
Cladosporium sp., Cladosporium sp. No. 45-2
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brenda
Oda, K.; Kamada, M.; Murao, S.
Extracellular acid protease of yeasts. IV. Physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24
Agric. Biol. Chem.
36
1103-1108
1972
Rhodotorula glutinis, Rhodotorula glutinis K-24
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brenda
Kamada, M.; Oda, K.; Murao, S.
Extracellular protease of yeasts. III. Purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties
Agric. Biol. Chem.
36
1095-1101
1972
Rhodotorula glutinis, Rhodotorula glutinis K-24
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brenda
Oda, K.; Funakoshi, S.; Murao, S.
Acid protease of Cladosporium species No. 45-2. II. Physicochemical properties and substrate specificity of acid protease isolated from Cladosporium species No. 45-2
Agric. Biol. Chem.
37
1723-1729
1973
Cladosporium sp., Cladosporium sp. No. 45-2
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brenda
Liu, C.L.; Ohtsuki, K.; Hatano, H.
Inactivation of Rhodotorula glutinis acid protease by diazoacetyl compounds
J. Biochem.
73
671-673
1973
Rhodotorula glutinis
brenda
Liu, C.L.; Hatano, H.
An aspartic acid residue at the active site of Rhodotorula glutinis acid protease
FEBS Lett.
42
352-354
1974
Rhodotorula glutinis
brenda
Kanazawa, H.
Acid proteases. I. Inactivation of Cladosporium acid protease by diazoacetyl-DL-norleucine methyl ester as an active-site-directed irreversible inhibitor
J. Biochem.
81
1739-1744
1977
Cladosporium sp.
brenda
Subramanian, E.; Cook, W.J.
Crystallization and preliminary X-ray investigation of acid protease from Cladosporium
J. Biol. Chem.
259
1251-1252
1984
Cladosporium sp.
brenda
Murao, S.
Rhodotorulapepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
139-140
2004
Rhodotorula glutinis, Rhodotorula glutinis K-24
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brenda
Lario, L.; Chaud, L.; Almeida, M.; Converti, A.; Duraes Sette, L.; Pessoa, A.
Production, purification, and characterization of an extracellular acid protease from the marine Antarctic yeast Rhodotorula mucilaginosa L7
Fungal Biol.
119
1129-1136
2015
Rhodotorula mucilaginosa, Rhodotorula mucilaginosa L7
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brenda