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- Aspergillopepsin_I abstract "Aspergillopepsin I (EC 3.4.23.18, Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus awamori acid proteinase, Aspergillus carboxyl proteinase, carboxyl proteinase, Aspergillus kawachii aspartic proteinase, Aspergillus saitoi acid proteinase, pepsin-type aspartic proteinase, Aspergillus niger acid proteinase, sumizyme AP, proctase P, denapsin, denapsin XP 271, proctase) is an enzyme. This enzyme catalyses the following chemical reaction Hydrolysis of proteins with broad specificity. Generally favours hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milkThis enzyme is found in a variety of Aspergillus species.".
- Aspergillopepsin_I ecNumber "3.4.23.18".
- Aspergillopepsin_I wikiPageID "5573998".
- Aspergillopepsin_I wikiPageRevisionID "573529687".
- Aspergillopepsin_I casNumber "9025".
- Aspergillopepsin_I ecNumber "3.4".
- Aspergillopepsin_I iubmbEcNumber "3".
- Aspergillopepsin_I name "Aspergillopepsin I".
- Aspergillopepsin_I subject Category:EC_3.4.23.
- Aspergillopepsin_I type Biomolecule.
- Aspergillopepsin_I type Enzyme.
- Aspergillopepsin_I type BiologicalObject.
- Aspergillopepsin_I comment "Aspergillopepsin I (EC 3.4.23.18, Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus awamori acid proteinase, Aspergillus carboxyl proteinase, carboxyl proteinase, Aspergillus kawachii aspartic proteinase, Aspergillus saitoi acid proteinase, pepsin-type aspartic proteinase, Aspergillus niger acid proteinase, sumizyme AP, proctase P, denapsin, denapsin XP 271, proctase) is an enzyme.".
- Aspergillopepsin_I label "Aspergillopepsin I".
- Aspergillopepsin_I sameAs m.0v3cgkp.
- Aspergillopepsin_I sameAs Q12902879.
- Aspergillopepsin_I sameAs Q12902879.
- Aspergillopepsin_I wasDerivedFrom Aspergillopepsin_I?oldid=573529687.
- Aspergillopepsin_I isPrimaryTopicOf Aspergillopepsin_I.
- Aspergillopepsin_I name "Aspergillopepsin I".