3.4.23.29: Polyporopepsin
This is an abbreviated version!
For detailed information about Polyporopepsin, go to the full flat file.
Word Map on EC 3.4.23.29
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3.4.23.29
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cheese
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rennet
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chymosin
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pusillus
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mucor
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bran
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kappa-casein
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curd
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skim
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miehei
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rhizomucor
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argentino
- 3.4.23.29
-
cheese
-
rennet
- chymosin
- pusillus
- mucor
- bran
- kappa-casein
-
curd
-
skim
- miehei
- rhizomucor
-
argentino
Reaction
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain =
Synonyms
Acid protease, aspartic protease, Aspartic proteinase, EC 3.4.4.17, 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
ECTree
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Substrates Products
Substrates Products on EC 3.4.23.29 - Polyporopepsin
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REACTION DIAGRAM
alpha1-casein + H2O
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cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0
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angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
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hydrolyzes Tyr4-Ile5 bond much more rapidly than the Val3-Tyr4 bond
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beta-casein + H2O
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cleavage of Leu165-Ser166, Ala189-Phe190, and Leu192-Tyr193 bonds, no cleavage of Leu139-Leu140 and Ser142-Trp143 bonds
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FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHL + VEA + LYLVCGERGF + FYT + PKA
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i.e. insulin B chain, cleavage site specificity at pH 3.0.the Ala14-Leu15 bond is preferred
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Oxidized B-chain of insulin + H2O
Proteolytically cleaved insulin B-chain
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peptide bonds mainly susceptible to the enzyme: Leu11-Val12, Ala14-Leu15, Phe24-Phe25, Thr27-Pro28
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additional information
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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
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additional information
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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
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