Information on EC 3.4.23.31 - Scytalidopepsin A

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The expected taxonomic range for this enzyme is: Scytalidium lignicola

EC NUMBER
COMMENTARY hide
3.4.23.31
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RECOMMENDED NAME
GeneOntology No.
Scytalidopepsin A
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
42613-34-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
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cleavage of Tyr-Ile, Phe-His and Leu-Leu bond
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Benzyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
show the reaction diagram
Benzyloxycarbonyl-Ala-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Leu + Ala-Ala
show the reaction diagram
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
show the reaction diagram
Benzyloxycarbonyl-Gly-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Gly-Leu + Ala-Ala
show the reaction diagram
Benzyloxycarbonyl-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Leu + Ala-Ala
show the reaction diagram
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slow hydrolysis
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Benzyloxycarbonyl-Phe-Leu-Ala + H2O
Benzyloxycarbonyl-Phe + Leu-Ala
show the reaction diagram
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
?
show the reaction diagram
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
Benzyloxycarbonyl-Phe-Leu + Ala-Ala
show the reaction diagram
Benzyloxycarbonyl-Phe-Tyr-Ala + H2O
Benzyloxycarbonyl-Phe + Tyr-Ala
show the reaction diagram
Benzyloxycarbonyl-Phe-Tyr-Ala-Ala + H2O
Benzyloxycarbonyl-Phe-Tyr + Ala-Ala
show the reaction diagram
casein + H2O
?
show the reaction diagram
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLC + GSHLVEALYLVCGERGF + FYTPKA
show the reaction diagram
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i.e. insulin B chain, cleavage site specificity
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?
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Ala-Phe 4-nitrophenyl ester + H2O
?
show the reaction diagram
N-tert-Butoxycarbonyl-Phe-Arg(NO2)-Gly-Phe 4-nitrophenyl ester + H2O
?
show the reaction diagram
Oxidized insulin B-chain + H2O
?
show the reaction diagram
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specifically hydrolyzes Cys7-Gly8 bond
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Phenyloxycarbonyl-Ala-Ala-Lys-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Ala-Ala-Lys + Ala-Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Ala-Lys-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Ala-Lys + Ala-Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
Phenyloxycarbonyl-Ala-Phe + Gly-Ala
show the reaction diagram
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Phenyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
Phenyloxycarbonyl-Ala-Phe + Leu-Ala
show the reaction diagram
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Phenyloxycarbonyl-Glu-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Glu-Leu + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Gly-Leu-Gly-Phe + H2O
Phenyloxycarbonyl-Gly-Leu + Gly-Phe
show the reaction diagram
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Phenyloxycarbonyl-Gly-Phe-Gly-Ala + H2O
Phenyloxycarbonyl-Gly-Phe + Gly-Ala
show the reaction diagram
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Phenyloxycarbonyl-Leu-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Leu-Leu + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Lys-Ala-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Lys-Ala + Ala-Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Lys-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Lys-Leu + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Phe-Ala-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Ala + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Phe-Glu-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Glu + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Phe-Gly-Ala + H2O
?
show the reaction diagram
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Phenyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Leu + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Phe-Lys-Ala-Ala + H2O
Phenyloxycarbonyl-Phe-Lys + Ala-Ala
show the reaction diagram
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Phenyloxycarbonyl-Tyr-Leu-Ala-Ala + H2O
Phenyloxycarbonyl-Tyr-Leu + Ala-Ala
show the reaction diagram
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Proangiotensin + H2O
?
show the reaction diagram
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enzyme form A-1 hydrolyzes Tyr4-Ile5 and Phe8-His9
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Succinyl-Phe-Arg-Ala-Phe 4-nitrophenyl ester + H2O
?
show the reaction diagram
Z-Phe-Xaa-Ala-Ala + H2O
Z-Phe-Xaa + Ala-Ala
show the reaction diagram
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cleavage site specificity
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?
Z-Xaa-Leu-Ala-Ala + H2O
Z-Xaa-Leu + Ala-Ala
show the reaction diagram
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cleavage site specificity
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme is involved in protein degradation in wood destroying by the fungus
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CuCl2
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activates
MnCl2
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ac-pepstatin
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benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
alpha-Microbial alkaline proteinase inhibitor
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weak
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angiotensin I
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Benzyloxycarbonyl-Gly-Pro-Phe-Leu-Ala
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benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe
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benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe-D-Leu-Ala-Ala
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benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe-Leu
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benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
Benzyloxycarbonyl-Phe-Leu-Ala
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benzyloxycarbonyl-Gly-Leu-Ala-Ala as substrate
N-bromosuccinimide
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
Benzyloxycarbonyl-Ala-Leu-Ala-Ala
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3.1
Benzyloxycarbonyl-Ala-Lys-Ala-Ala-Ala
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1.5
Benzyloxycarbonyl-Ala-Phe-Gly-Ala
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0.6
Benzyloxycarbonyl-Ala-Phe-Leu-Ala
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1.3
Benzyloxycarbonyl-Gly-Phe-Leu-Ala
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2.5
Benzyloxycarbonyl-Lys-Ala-Ala-Ala
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2.1
Benzyloxycarbonyl-Lys-Leu-Ala-Ala
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3.7
benzyloxycarbonyl-Phe-Glu-Ala-Ala
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0.8
benzyloxycarbonyl-Phe-Lys-Ala-Ala
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1.6
Benzyloxycarbonyl-Phe-Tyr-Ala-Ala
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0.5 - 1
Succinyl-Phe-Arg-Ala-Phe 4-nitrophenyl ester
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.5
3.6
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benzyloxycarbonyl-Phe-Glu-Ala-Ala, enzyme form A-1 and A-2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 3.8
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2: about 50% of activity maximum, 3.8: about 80% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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enzyme form A-1 and A-2
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39 - 63
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39C: about 40% of activity maximum, 63C: 60% of activity maximum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
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isozyme A-1
3.8
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isozyme A-2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the enzyme is secreted
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
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Scytalidium lignicolum, gel filtration
40600
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Scytalidium lignicolum, sedimentation equilibrium analysis
43000
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Scytalidium lignicolum, enzyme form A-1 and A-2, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 5.5
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37C, 20 h, stable
30754
3 - 5
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37C, 20 h, stable
30756
4
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15 min, stable below 50C, about 60% loss of activity at 60C
30754
4.8
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15 min, stable below 55C, complete loss of activity at 68C
30756
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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pH 4.0, 15 min, stable below
55
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pH 4.8, 15 min, stable below
60
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pH 4.0, 15 min, 60% loss of activity
68
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pH 4.8, 15 min, complete loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme form: A-1 and A-2
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proteinase C
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