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Literature summary extracted from

  • Kobayashi, H.
    Polyporopepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 113-115.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.29 DNA and amino acid sequence determination and analysis Irpex lacteus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.29 crystallization by hanging drop method with ammonium sulfate as precipitant, X-ray diffraction structure determination and analysis at 1.9 A resolution Irpex lacteus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.29 1,2-epoxy-3-(4-nitrophenoxy)propane inactivation, active site-directed inhibitor Irpex lacteus
3.4.23.29 Diazoacetyl-DL-norleucine methyl ester inactivation, active site-directed inhibitor Irpex lacteus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.29 36000
-
 x * 36000, SDS-PAGE Irpex lacteus

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.29 Irpex lacteus
-
 formerly Irpex lacteus
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.29 glycoprotein two possible N-glycosylation sites at Asn192 and Asn228, the enzyme shows affinity for concanavalin A, wheat germ agglutinin, and Ricinus communis agglutinin Irpex lacteus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.29 native enzyme by dehydroacetylpepstatin affinity chromatography Irpex lacteus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.29 alpha1-casein + H2O cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0 Irpex lacteus ?
-
 ?
3.4.23.29 beta-casein + H2O cleavage of Leu165-Ser166, Ala189-Phe190, and Leu192-Tyr193 bonds, no cleavage of Leu139-Leu140 and Ser142-Trp143 bonds Irpex lacteus ?
-
 ?
3.4.23.29 FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O i.e. insulin B chain, cleavage site specificity at pH 3.0.the Ala14-Leu15 bond is preferred Irpex lacteus FVNQHLCGSHL + VEA + LYLVCGERGF + FYT + PKA
-
 ?
3.4.23.29 Hemoglobin + H2O
-
 Irpex lacteus ?
-
 ?
3.4.23.29 kappa-casein + H2O cleavage of Phe105-Met106 bond Irpex lacteus ?
-
 ?
3.4.23.29 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 Irpex lacteus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.23.29 ? x * 36000, SDS-PAGE Irpex lacteus

Synonyms

EC Number Synonyms Comment Organism
3.4.23.29 milk-clotting enzyme
-
 Irpex lacteus
3.4.23.29 More the enzyme belongs to the A1 peptidase family Irpex lacteus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.23.29 additional information
-
 the enzyme is the least heat-stable among the milk-clotting enzymes Irpex lacteus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.29 2.8 2.9 substrates casein and hemoglobin Irpex lacteus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.23.29 Irpex lacteus
-
-
 5.3