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Literature summary for 3.4.23.4 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
Search for more literature for 3.4.23.4

Activating Compound

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Bos taurus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Substrates and Products (Substrate)

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