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Literature summary extracted from

  • Oda, K.
    Scytalidopepsin B (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 219-221.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.32 DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae with propper processing prior to secretion Scytalidium lignicola

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.32 1,2-epoxy-3-(4-nitrophenoxy)propane modifies active site residue Glu53 Scytalidium lignicola
3.4.23.32 1-diazo-3-phenyl-2-propanone modifies active site residue Asp98 Scytalidium lignicola
3.4.23.32 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 Scytalidium lignicola

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.23.32 extracellular the enzyme is secreted Scytalidium lignicola
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.32 21969
-
1 * 21969, amino acid sequence calculation Scytalidium lignicola

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.32 additional information Scytalidium lignicola the enzyme is involved in protein degradation in wood destroying by the fungus ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.32 Scytalidium lignicola
-
strain ATCC 24568
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.23.32 Hydrolysis of proteins with broad specificity, cleaving Phe24-/-Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin catalytic residues are Glu53 and Asp98 Scytalidium lignicola

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.23.32 additional information
-
-
Scytalidium lignicola

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.32 angiotensin I + H2O cleavage of the Hi6-Pro7 bond Scytalidium lignicola ?
-
?
3.4.23.32 FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O i.e. insulin B chain, cleavage site specificity Scytalidium lignicola FVNQHLCGSHLVE + A + LYLVCGERGF + FY + TPKA
-
?
3.4.23.32 additional information the enzyme is involved in protein degradation in wood destroying by the fungus Scytalidium lignicola ?
-
?
3.4.23.32 Z-Phe-Xaa-Ala-Ala + H2O C-terminal cleavage site specificity, low activity Scytalidium lignicola Z-Phe + Xaa-Ala-Ala
-
?
3.4.23.32 Z-Xaa-Leu-Ala-Ala + H2O C-terminal cleavage site specificity, low activity Scytalidium lignicola Z-Xaa + Leu-Ala-Ala
-
?

Subunits

EC Number Subunits Comment Organism
3.4.23.32 monomer 1 * 21969, amino acid sequence calculation Scytalidium lignicola

Synonyms

EC Number Synonyms Comment Organism
3.4.23.32 More the enzyme belongs to the A4 peptidase family Scytalidium lignicola

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.32 2
-
substrate casein Scytalidium lignicola

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.23.32 Scytalidium lignicola
-
-
3.2