Abstract
RENNIN (EC 3.4.4.3) is a proteolytic enzyme1 that is of considerable industrial importance because of its ability to clot milk. Evidence has been presented that its clotting action on milk depends on the splitting of an ester bond2. If this is so, the active centre of rennin could be expected to be similar to those of other enzymes with esteraso activity such as chyrnotrypsin (EC 3.4.4.5) in which catalytic activity is associated with reactive serine3 and histidine4 side-chains. We have shown that rennin may be inactivated by photo-oxidation with methylene blue and that the loss of activity is probably due to destruction of histidine as there is no loss of activity when photo-oxidizable side-chains other than histidine are modified5.
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HILL, R., LAING, R. Inactivation of Rennin by Dansyl. Nature 210, 1160–1161 (1966). https://doi.org/10.1038/2101160a0
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DOI: https://doi.org/10.1038/2101160a0
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