3.4.23.40: Phytepsin
This is an abbreviated version!
For detailed information about Phytepsin, go to the full flat file.
Word Map on EC 3.4.23.40
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3.4.23.40
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cardunculus
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cardoon
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proteinases
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pistil
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milk-clotting
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plant-specific
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rennet
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stigmatic
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artichoke
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chymosin
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cheeses
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food industry
- 3.4.23.40
- cardunculus
- cardoon
- proteinases
- pistil
-
milk-clotting
-
plant-specific
- rennet
-
stigmatic
- artichoke
- chymosin
-
cheeses
- food industry
Reaction
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-/-Asp- and -Asp-/-Asp- bonds in 2S albumin from plant seeds =
Synonyms
Acid protease, Ap1, Aspartic proteinase, Aspartyl endoproteinase, Barley grain aspartic proteinase, Carboxyl proteinase, CardA, cardB, Cardosin, cardosin A, cardosin B, Cynarase, cynarase A, cynarase B, cynarase C, Edestinase, HvAP, Nepenthesin, Oryzasin, PCB, procardosin B
ECTree
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Substrates Products
Substrates Products on EC 3.4.23.40 - Phytepsin
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REACTION DIAGRAM
((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl) + H2O
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alpha-casein + H2O
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formation of two cleavage products of about 30 and 23 kDa
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?
beta-casein + H2O
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formation of one single product of about 23 kDa
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kappa-casein + H2O
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digestion of kappa-casein results in the appearance of a product of about 16 kDa
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L-Pro-L-Thr-L-Glu-L-Phe(p-NO2)-L-Phe-L-Arg-L-Leu + H2O
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Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe-Phe + Phe(NO2)-Ala-Leu + H2O
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?
Gliadin + H2O
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gliadin subunits with MW of 66800-9500 and 31000 are processed to fragemnts of 57000-63000 and 24000-26600, respectively
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Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe + H2O
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substrate of cardosin B
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Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
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substrate of cardosin A
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modelling of enzyme-substrate complex
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Protein + H2O
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may participate in the processing of the C-terminus of barley prolectin
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Protein + H2O
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contribution to the digestion of trapped insects
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preference for phenylalanine, leucine or norleucine at P! site, for tyrosine or phenylalanine at P1 site
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additional information
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the enzyme shows a preference for accommodating large hydrophobic amino acids at position P1, such as phenylalanine, tyrosine, and leucine. In P1', the enzyme prefers rather small amino acids like valine, alanine, and serine
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additional information
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no hydrolysis of denatured alpha-hordothionin
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additional information
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endopeptidase activity, aliphatic or aromatic amino acids at P1 and P1' possible, e.g. Leu, Val, Phe, Thr
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