Peptide substrates for chymosin (rennin). Interaction sites in k-casein-related sequences located outside the (103-108)-hexapeptide region that fits into the enzyme's active-site cleft
The role of individual amino acid residues in the 98-102 and 111-112 regions of bovine k-casein in its interaction with the milk-clotting enzyme chymosin (rennin) was investigated. A model of the enzyme-substrate complex is proposed. Herein the 103-108 fragment of the substrate, to be accommodated w...
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Veröffentlicht in: | Biochemical journal 1987-01, Vol.244 (3), p.553-558 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The role of individual amino acid residues in the 98-102 and 111-112 regions of bovine k-casein in its interaction with the milk-clotting enzyme chymosin (rennin) was investigated. A model of the enzyme-substrate complex is proposed. Herein the 103-108 fragment of the substrate, to be accommodated within the enzyme's active-site cleft, is brought into position by electrostatic binding (via His-98, His-100, His-102 and Lys-111) near the entrance of the cleft. |
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ISSN: | 0264-6021 |