Information on EC 3.4.23.28 - Acrocylindropepsin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.28
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RECOMMENDED NAME
GeneOntology No.
Acrocylindropepsin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6-/-Cys(SO3H), Glu21-/-Arg and Asn3-/-Gln, although not Gln4-His
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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aspartic proteinase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-84-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acrocylindrium sp.
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
Acrocylindrium sp.
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high activity
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-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 6 H2O
FVNQHL + CGSHL + VEAL + L-Tyr + LVCGERGF + L-Phe + YTPKA
show the reaction diagram
Acrocylindrium sp.
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i.e. insulin B chain, cleavage site specificity
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-
?
Glucagon + H2O
?
show the reaction diagram
insulin A chain + H2O
?
show the reaction diagram
Acrocylindrium sp.
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cleavage site specificity
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?
Oxidized insulin A-chain + H2O
?
show the reaction diagram
Acrocylindrium sp.
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complete hydrolysis of Leu13-Tyr14, partial hydrolysis of Leu16-Glu17 and Glu17-Asn18, some hydrolysis of Tyr14-Glu15 and Tyr19-Cys*SO3H2O
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Oxidized insulin B-chain + H2O
?
show the reaction diagram
Acrocylindrium sp.
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complete hydrolysis of: Leu6-Cys*SO3H7, Leu11-Val12, Leu15-Tyr16, Tyr16-Leu17, Phe24-Phe25, partial hydrolysis of: Asn3-Gln4, Ala14-Leu15, Gly20-Glu21, Glu21-Arg22, Tyr26-Thr27
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additional information
?
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Acrocylindrium sp.
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the enzyme prefers Tyr, Phe, or Leu at P1 or P1' positions
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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
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 6 H2O
FVNQHL + CGSHL + VEAL + L-Tyr + LVCGERGF + L-Phe + YTPKA
show the reaction diagram
Acrocylindrium sp.
-
i.e. insulin B chain, cleavage site specificity
-
-
?
Glucagon + H2O
?
show the reaction diagram
Acrocylindrium sp.
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-
-
-
?
insulin A chain + H2O
?
show the reaction diagram
Acrocylindrium sp.
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cleavage site specificity
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
Diazoacetyl-DL-norleucine methyl ester
Pepstatin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Acrocylindrium sp.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
Acrocylindrium sp.
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substrate casein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Acrocylindrium sp.
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Acrocylindrium sp.
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the enzyme is secreted
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Manually annotated by BRENDA team
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Acrocylindrium sp.
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purified enzyme, repeated crystallization
Acrocylindrium sp.
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 5
Acrocylindrium sp.
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highly stable, unstable below pH 0.7 and above pH 5.6
668811
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
Acrocylindrium sp.
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stable below
70
Acrocylindrium sp.
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inactivation above
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from cell culture medium by successive acetone precipitation, ammonium sulfate fractionation, and adsorption chromatography, to homogeneity
Acrocylindrium sp.
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