We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 3.4.23.29 - Polyporopepsin for references in articles please use BRENDA:EC3.4.23.29
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The expected taxonomic range for this enzyme is: Irpex lacteus
Reaction Schemes
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain
Synonyms
Aspartic proteinase, ILAP, Irpex lacteus aspartic protease, Irpex lacteus aspartic proteinase, Irpex lacteus carboxyl proteinase B, milk-clotting enzyme, More, Polyporus aspartic proteinase, Proteinase, Irpex lacteus aspartic,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Aspartic proteinase
-
-
-
-
Irpex lacteus aspartic protease
-
-
Irpex lacteus aspartic proteinase
-
-
Irpex lacteus carboxyl proteinase B
-
-
Polyporus aspartic proteinase
-
-
-
-
Proteinase, Irpex lacteus aspartic
-
-
-
-
additional information
-
the enzyme belongs to the A1 peptidase family
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain
-
-
-
-
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain
catalytic mechanism, transition state model, substrate binding structure and mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of peptide bond
-
-
aspartic endopeptidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ala-Phe-Gly-Ala + H2O
Ala-Phe + Gly-Ala
-
-
-
-
Ala-Phe-Leu-Ala + H2O
Ala-Phe + Leu-Ala
-
-
-
-
alpha1-casein + H2O
?
-
cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0
-
-
?
Angiotensin I + H2O
Proteolytically cleaved angiotensin
-
hydrolyzes Tyr4-Ile5 bond much more rapidly than the Val3-Tyr4 bond
-
-
-
beta-casein + H2O
?
-
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
-
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
-
-
-
-
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
Proteolytically cleaved hemogobin
-
-
-
-
-
kappa-casein + H2O
?
-
cleavage of Phe105-Met106 bond
-
-
?
Oxidized B-chain of insulin + H2O
Proteolytically cleaved insulin B-chain
-
peptide bonds mainly susceptible to the enzyme: Leu11-Val12, Ala14-Leu15, Phe24-Phe25, Thr27-Pro28
-
-
-
Phe-Ala-Ala-Ala + H2O
Phe-Ala + Ala-Ala
-
-
-
-
Phe-Glu-Ala-Ala + H2O
Phe-Glu + Ala-Ala
-
-
-
-
Phe-Gly-Ala-Ala + H2O
Phe-Gly + Ala-Ala
-
-
-
-
Phe-Leu-Ala-Ala + H2O
Phe-Leu + Ala-Ala
-
-
-
-
Phe-Lys-Ala-Ala + H2O
Phe-Lys + Ala-Ala
-
-
-
-
Phe-Tyr-Ala-Ala + H2O
Phe-Tyr + Ala-Ala
-
-
-
-
additional information
?
-
additional information
?
-
-
milk clotting activity
-
-
-
additional information
?
-
-
milk clotting activity
-
-
-
additional information
?
-
-
milk clotting activity
-
-
-
additional information
?
-
-
the enzyme requires hydrophobic amino acids at P1 and/or P1' positions and at P3 and/or P4 positions, the enzyme shows high milk-clotting activity
-
-
-
additional information
?
-
-
the enzyme requires hydrophobic amino acids at P3 and/or P4 positions, the enzyme shows high milk-clotting activity, no activity with trypsinogen, pig pepsin, and mucorpepsins
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-epoxy-3-(4-nitrophenoxy)propane
Diazoacetyl-D,L-norleucine methyl ester
Diazoacetyl-DL-norleucine methyl ester
-
inactivation, active site-directed inhibitor
N-p-toluene sulfonyl-L-Phe chloromethyl ketone
-
-
sodium lauryl sulfate
-
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
not
1,2-epoxy-3-(4-nitrophenoxy)propane
-
inactivation, active site-directed inhibitor
Diazoacetyl-D,L-norleucine methyl ester
-
-
Diazoacetyl-D,L-norleucine methyl ester
-
not
pepstatin
-
-
pepstatin
-
binding structure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.8 - 2.9
-
substrates casein and hemoglobin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
formerly Irpex lacteus
-
-
brenda
formerly Irpex lacteus; Fr. KY 2901 and mutant enzymes U-212, 2U-148 and 3U-39 produced by irradiation with UV-light
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CARP_IRPLA
340
0
35051
Swiss-Prot
V5NCU0_LEUGO
412
0
43130
TrEMBL
B0DVH0_LACBS
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686)
410
1
43505
TrEMBL
B0DRF1_LACBS
Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686)
409
1
43113
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Polyporus tulipiferae, calculation from nucleotide sequence
39000
-
1 * 39000, Polyporus tulipiferae, SDS-PAGE
36000
-
Polyporus tulipiferae
36000
-
x * 36000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
-
1 * 39000, Polyporus tulipiferae, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
crystallization by hanging drop method with ammonium sulfate as precipitant, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
enzyme from Fr. KY 2901 and mutant enzymes produced by irradiation with UV-light
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.6
-
15 min, complete inactivation at 45°C, stable at 30°C
30730
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
native enzyme by dehydroacetylpepstatin affinity chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA and amino acid sequence determination and analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kobayashi, H.; Kusakabe, I.; Murakami, K.
Substrate specificity of a carboxyl proteinase from Irpex lacteus
Agric. Biol. Chem.
47
1921-1923
1983
Irpex lacteus
-
brenda
Kobayashi, H.; Sekibata, S.; Shibuya, H.; Yoshida, S.; Kusakabe, I.; Murakami, K.
Cloning and sequence analysis of cDNA for Irpex lacteus aspartic proteinase
Agric. Biol. Chem.
53
1927-1933
1989
Irpex lacteus
-
brenda
Kobayashi, H.; Kusakabe, I.; Murakami, K.
Purification and characterization of a pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus)
Agric. Biol. Chem.
49
2393-2397
1985
Irpex lacteus
-
brenda
Kawai, M.; Terada, O.
Studies on the milk-clotting enzymes produced by basidiomycetes. Part IV. Comparisons of some properties of crystalline acid proteinases produced by the parent and mutant strains of Irpex lacteus Fr
Agric. Biol. Chem.
40
1463-1469
1976
Irpex lacteus
-
brenda
Kobayashi, H.
Polyporopepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
113-115
2004
Irpex lacteus
-
brenda
Fujimoto, Z.; Fujii, Y.; Kaneko, S.; Kobayashi, H.; Mizuno, H.
Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin
J. Mol. Biol.
341
1227-1235
2004
Irpex lacteus
brenda
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
3.4.23.29 Polyporopepsin
more
top
Information
