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Information on EC 3.4.23.31 - Scytalidopepsin A
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EC Tree
3.4.23.31 Scytalidopepsin ASpecify your search results
The expected taxonomic range for this enzyme is: Scytalidium lignicola
Reaction Schemes
Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves Cys(SO3H)7-/-Gly and Leu17-/-Val in the B chain of insulin
Synonyms
scytalidopepsin a, scytalidium lignicolum acid proteinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Proteinase, Scytalidium lignicolum aspartic
-
-
-
-
Proteinase, Scytalidium lignicolum aspartic, A-2
-
-
-
-
Proteinase, Scytalidium lignicolum aspartic, A-I
-
-
-
-
Proteinase, Scytalidium lignicolum aspartic, C-
-
-
-
-
Scytalidium aspartic proteinase A
-
-
-
-
Scytalidium lignicolum acid proteinase
-
-
-
-
Scytalidium lignicolum aspartic proteinase
-
-
-
-
Scytalidium lignicolum carboxyl proteinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves Cys(SO3H)7-/-Gly and Leu17-/-Val in the B chain of insulin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
42613-34-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + His-Leu + Leu-Val-Tyr-Ser
-
cleavage of Tyr-Ile, Phe-His and Leu-Leu bond
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
benzyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
benzyloxycarbonyl-Ala-Phe + Gly-Ala
-
-
-
-
?
benzyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
benzyloxycarbonyl-Ala-Phe + Leu-Ala
-
-
-
-
?
benzyloxycarbonyl-Gly-Phe-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Phe + Leu-Ala
-
-
-
-
?
Benzyloxycarbonyl-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Leu + Ala-Ala
-
slow hydrolysis
-
?
benzyloxycarbonyl-Lys-Ala-Ala-Ala + H2O
benzyloxycarbonyl-Lys-Ala + Ala-Ala
-
-
-
-
?
benzyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
benzyloxycarbonyl-Lys-Leu + Ala-Ala
-
-
-
-
?
benzyloxycarbonyl-Phe-Glu-Ala-Ala + H2O
benzyloxycarbonyl-Phe-Glu + Ala-Ala
-
-
-
-
?
benzyloxycarbonyl-Phe-Lys-Ala-Ala + H2O
benzyloxycarbonyl-Phe-Lys + Ala-Ala
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLC + GSHLVEALYLVCGERGF + FYTPKA
-
i.e. insulin B chain, cleavage site specificity
-
-
?
Oxidized insulin B-chain + H2O
?
-
specifically hydrolyzes Cys7-Gly8 bond
-
-
?
Phenyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
Phenyloxycarbonyl-Ala-Phe + Gly-Ala
-
-
-
-
?
Phenyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
Phenyloxycarbonyl-Ala-Phe + Leu-Ala
-
-
-
?
Phenyloxycarbonyl-Glu-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Glu-Leu + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Gly-Leu-Gly-Phe + H2O
Phenyloxycarbonyl-Gly-Leu + Gly-Phe
-
-
-
?
Phenyloxycarbonyl-Gly-Phe-Gly-Ala + H2O
Phenyloxycarbonyl-Gly-Phe + Gly-Ala
-
-
-
?
Phenyloxycarbonyl-Leu-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Leu-Leu + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Lys-Ala + Ala-Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Lys-Leu + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Phe-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Ala + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Phe-Glu-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Glu + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Leu + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Phe-Lys-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Lys + Ala-Ala
-
-
-
?
Phenyloxycarbonyl-Tyr-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Tyr-Leu + Ala-Ala
-
-
-
?
Proangiotensin + H2O
?
-
enzyme form A-1 hydrolyzes Tyr4-Ile5 and Phe8-His9
-
-
?
Z-Phe-Xaa-Ala-Ala + H2O
Z-Phe-Xaa + Ala-Ala
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cleavage site specificity
-
-
?
Z-Xaa-Leu-Ala-Ala + H2O
Z-Xaa-Leu + Ala-Ala
-
cleavage site specificity
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Ala-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Leu + Ala-Ala
-
-
-
-
?
Benzyloxycarbonyl-Ala-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Leu + Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Ala-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Leu + Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Gly-Leu + Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Gly-Leu + Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Ala + H2O
Benzyloxycarbonyl-Phe + Leu-Ala
-
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Ala + H2O
Benzyloxycarbonyl-Phe + Leu-Ala
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slow hydrolysis
-
?
Benzyloxycarbonyl-Phe-Leu-Ala + H2O
Benzyloxycarbonyl-Phe + Leu-Ala
-
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Phe-Leu + Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Phe-Leu + Ala-Ala
-
-
-
?
Benzyloxycarbonyl-Phe-Tyr-Ala + H2O
Benzyloxycarbonyl-Phe + Tyr-Ala
-
-
-
?
Benzyloxycarbonyl-Phe-Tyr-Ala + H2O
Benzyloxycarbonyl-Phe + Tyr-Ala
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slow
-
?
Benzyloxycarbonyl-Phe-Tyr-Ala + H2O
Benzyloxycarbonyl-Phe + Tyr-Ala
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-
-
?
Benzyloxycarbonyl-Phe-Tyr-Ala-Ala + H2O
Benzyloxycarbonyl-Phe-Tyr + Ala-Ala
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-
-
?
Benzyloxycarbonyl-Phe-Tyr-Ala-Ala + H2O
Benzyloxycarbonyl-Phe-Tyr + Ala-Ala
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-
-
-
?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Ala-Phe 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Ala-Phe 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Ala-Phe 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Gly-Phe 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Gly-Phe 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Gly-Phe 4-nitrophenyl ester + H2O
?
-
-
-
-
?
Succinyl-Phe-Arg-Ala-Phe 4-nitrophenyl ester + H2O
?
-
at high rate
-
-
?
Succinyl-Phe-Arg-Ala-Phe 4-nitrophenyl ester + H2O
?
-
at high rate
-
-
?
Succinyl-Phe-Arg-Ala-Phe 4-nitrophenyl ester + H2O
?
-
at high rate
-
-
?
additional information
?
-
-
trypsinogen activation, substrate specificity
-
-
?
additional information
?
-
-
the enzyme is involved in protein degradation in wood destroying by the fungus
-
-
?
additional information
?
-
-
no cleavage of the Hi6-Pro7 bond of angiotensin I
-
-
?
additional information
?
-
-
trypsinogen activation, substrate specificity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is involved in protein degradation in wood destroying by the fungus
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Benzyloxycarbonyl-Gly-Pro-Phe-Leu-Ala
-
benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe-D-Leu-Ala-Ala
-
benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe-Leu
-
benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe-Leu-Ala
-
benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
additional information
-
a related enzyme from the same organism, proteinase C is also insensitive to these inhibitors; diazoacetyl-DL-norleucine methyl ester; diisopropyl fluorophosphate; methyl 2-diazoacetamidohexanoate, 1,2-epoxy-3-(4-nitrophenyl)propane; not: EDTA; Streptomyces-pepsin inhibitor
-
additional information
-
a related enzyme from the same organism, proteinase C is also insensitive to these inhibitors; diazoacetyl-DL-norleucine methyl ester; methyl 2-diazoacetamidohexanoate, 1,2-epoxy-3-(4-nitrophenyl)propane; Streptomyces-pepsin inhibitor; talopeptin (MK-1, metal proteinase inhibitor); thiolstatin (thiol proteinase inhibitor)
-
additional information
-
a related enzyme from the same organism, proteinase C is also insensitive to these inhibitors; pepstatin
-
additional information
-
the enzyme is insensitive to pepstatin and inhibitor S-PI, i.e. Ac-VV-statine-A-statine, statine is 4-amino-3-hydroxy-6-methylheptanoic acid, no inhibition by diazoacetyl-DL-norleucine methyl ester or 1,2-epoxy-3-(4-nitrophenoxy)propane
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
Succinyl-Phe-Arg-Ala-Phe 4-nitrophenyl ester
-
benzyloxycarbonyl-Phe-Leu-Ala-Ala, benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala
additional information
additional information
-
kinetic studies with synthetic peptides
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 3.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 3.8
-
2: about 50% of activity maximum, 3.8: about 80% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39 - 63
-
39°C: about 40% of activity maximum, 63°C: 60% of activity maximum
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
glycopeptide is composed of mannose, glucosamine, asparagine, serine and glycine in an approximate molar ratio of 10:3:2:1:1, possible structure
glycoprotein
-
carbohydrate content: 8-12% (enzyme form A-1 and A-2)
glycoprotein
-
the enzyme contains 3 mol of glucosamine and 10 mol of mannose
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Scytalidium lignicola
-
brenda
Oda, K.; Murao, S.
New acid proteases from Scytalidium lignicolum M-133. II. Purification and some enzymatic properties of acid protease A and B of Scytalidium lignicolum ATCC 24568.
Agric. Biol. Chem.
38
2435-2444
1974
Scytalidium lignicola, Scytalidium lignicola A-2
-
brenda
Oda, K.; Murao, S.
Studies on new acid proteases from Scytalidium lignicolum M-133. Part V. Action of Scytalidium lignicolum acid proteases on the insulin B-chain
Agric. Biol. Chem.
40
1221-1225
1976
Scytalidium lignicola
-
brenda
Oda, K.; Torishima, H.; Murao, S.
Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568
Agric. Biol. Chem.
50
651-658
1986
Scytalidium lignicola, Scytalidium lignicola C, Scytalidium lignicola A-2
-
brenda
Oda, K.; Murao, S.
Studies on new acid proteases from Scytalidium lignicolum ATCC 24568. Part VIII. Kinetic studies on S-PI(pepstatin Ac)-insensitive acid proteinases of Scytalidium lignicolum ATCC 24568. Evidence identifying them with a carboxyl proteinase group
Agric. Biol. Chem.
50
659-663
1986
Scytalidium lignicola, Scytalidium lignicola A-2
-
brenda
Ichishima, E.; Majima, E.; Emi, M.; Hayashi, K.; Murao, S.
Enzymic cleavage of the histidyl-prolyl bond of proangiotensin by carboxyl proteinases from Aspergillus sojae and Scytalidium lignicolum
Agric. Biol. Chem.
45
2391-2393
1981
Scytalidium lignicola
-
brenda
Morihara, K.; Tsuzuki, H.; Murao, S.; Oda, K.
Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides
J. Biochem.
85
661-668
1979
Scytalidium lignicola, Scytalidium lignicola A-2
brenda
Oda, K.; Murao, S.; Oka, T.; Morihara, K.
Pepstatin-insensitive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides
Agric. Biol. Chem.
40
859-866
1976
Scytalidium lignicola, Scytalidium lignicola A-2
-
brenda
Oda, K.; Murao, S.
Studies on new acid proteases from Scytalidium lignicolum ATCC 24568. Part IX. Additional evidence for the identity of Scytalidium lignicolum acid proteinases with the carboxyl proteinase group: the interaction between angiotensin I and S-PI-insensitive acid proteinases by means of a zinc(II)-dye complex as a probe
Agric. Biol. Chem.
50
1995-2001
1986
Scytalidium lignicola, Scytalidium lignicola A-2
-
brenda
Murao, S.; Morita, N.; Yamamoto, Y.; Oda, K.
Studies on new acid proteases from Scytalidium lignicolum M-133. Part VI. Partial structure of glycopeptide obtained from Scytalidium lignicolum acid protease A
Agric. Biol. Chem.
42
1343-1349
1978
Scytalidium lignicola
-
brenda
Murao, S.
Scytalidopepsin A
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
224-225
2004
Scytalidium lignicola
-
brenda
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