Information on EC 3.4.23.29 - Polyporopepsin

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The expected taxonomic range for this enzyme is: Irpex lacteus

EC NUMBER
COMMENTARY hide
3.4.23.29
-
RECOMMENDED NAME
GeneOntology No.
Polyporopepsin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
61573-73-7
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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
Ala-Phe-Gly-Ala + H2O
Ala-Phe + Gly-Ala
show the reaction diagram
-
-
-
-
Ala-Phe-Leu-Ala + H2O
Ala-Phe + Leu-Ala
show the reaction diagram
-
-
-
-
alpha1-casein + H2O
?
show the reaction diagram
-
cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0
-
-
?
Angiotensin I + H2O
Proteolytically cleaved angiotensin
show the reaction diagram
-
hydrolyzes Tyr4-Ile5 bond much more rapidly than the Val3-Tyr4 bond
-
-
-
beta-casein + H2O
?
show the reaction diagram
-
cleavage of Leu165-Ser166, Ala189-Phe190, and Leu192-Tyr193 bonds, no cleavage of Leu139-Leu140 and Ser142-Trp143 bonds
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHL + VEA + LYLVCGERGF + FYT + PKA
show the reaction diagram
-
i.e. insulin B chain, cleavage site specificity at pH 3.0.the Ala14-Leu15 bond is preferred
-
-
?
Gly-Phe-Leu-Ala + H2O
Gly-Phe + Leu-Ala
show the reaction diagram
-
-
-
-
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
Proteolytically cleaved hemogobin
show the reaction diagram
-
-
-
-
-
kappa-casein + H2O
?
show the reaction diagram
-
cleavage of Phe105-Met106 bond
-
-
?
Oxidized B-chain of insulin + H2O
Proteolytically cleaved insulin B-chain
show the reaction diagram
-
peptide bonds mainly susceptible to the enzyme: Leu11-Val12, Ala14-Leu15, Phe24-Phe25, Thr27-Pro28
-
-
-
Phe-Ala-Ala-Ala + H2O
Phe-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
Phe-Glu-Ala-Ala + H2O
Phe-Glu + Ala-Ala
show the reaction diagram
-
-
-
-
Phe-Gly-Ala-Ala + H2O
Phe-Gly + Ala-Ala
show the reaction diagram
-
-
-
-
Phe-Leu-Ala-Ala + H2O
Phe-Leu + Ala-Ala
show the reaction diagram
-
-
-
-
Phe-Lys-Ala-Ala + H2O
Phe-Lys + Ala-Ala
show the reaction diagram
-
-
-
-
Phe-Tyr-Ala-Ala + H2O
Phe-Tyr + Ala-Ala
show the reaction diagram
-
-
-
-
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
chymostatin
-
-
Diazoacetyl-D,L-norleucine methyl ester
Diazoacetyl-DL-norleucine methyl ester
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inactivation, active site-directed inhibitor
Fe3+
-
-
Hg2+
-
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N-p-toluene sulfonyl-L-Phe chloromethyl ketone
-
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Pepstatin
sodium lauryl sulfate
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8 - 2.9
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substrates casein and hemoglobin
2.8
-
hemoglobin
3
-
hemoglobin
4
-
Phe-Leu-Ala-Ala
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
Polyporus tulipiferae, 3U-39, gel filtration
33500
-
Polyporus tulipiferae 2U-148, gel filtration
34000
-
Polyporus tulipiferae KY 2901 and U-212, gel filtration
35000
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Polyporus tulipiferae, calculation from nucleotide sequence
39000
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1 * 39000, Polyporus tulipiferae, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 36000, SDS-PAGE
monomer
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1 * 39000, Polyporus tulipiferae, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
two possible N-glycosylation sites at Asn192 and Asn228, the enzyme shows affinity for concanavalin A, wheat germ agglutinin, and Ricinus communis agglutinin
additional information
-
2 putative N-glycosylation sites, sugar chains can be attached to Asn192 and/or Asn238
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization by hanging drop method with ammonium sulfate as precipitant, X-ray diffraction structure determination and analysis at 1.9 A resolution
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enzyme from Fr. KY 2901 and mutant enzymes produced by irradiation with UV-light
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purified enzyme in complex with inhibitor pepstatin, hanging drop vapour diffusion method, 0.005 ml of 10 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 50% ammonium sulfate in 10 mM sodium citrate-sulfate buffer, pH 5.4, 20°C, X-ray diffraction structure determination and analysis at 1.3 A resolution, structure modeling
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
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stable
30731
4.6
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15 min, complete inactivation at 45°C, stable at 30°C
30730
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
pH 4.6, 15 min, stable
45
-
pH 4.6, 15 min, complete inactivation
50
-
pH 4.5, 15 min, stable up to
60
-
pH 4.5, 15 min, complete inactivation
additional information
-
the enzyme is the least heat-stable among the milk-clotting enzymes
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by dehydroacetylpepstatin affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
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