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Literature summary extracted from

  • Gustchina, E.; Rumsh, L.; Ginodman, L.; Majer, P.; Andreeva, N.
    Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of kappa-casein (1996), FEBS Lett., 379, 60-62.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.23.4 His-Pro-His-Pro-His-NH2 stimulation, part of kappa-casein Bos taurus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.4
-
 Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.4 kappa-casein + H2O Bos taurus cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.4 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.4 His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O part of the bovine kappa-casein sequence Bos taurus His-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
 ?
3.4.23.4 kappa-casein + H2O cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106 Bos taurus ?
-
 ?
3.4.23.4 Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O part of the bovine kappa-casein sequence Bos taurus Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
 ?