Abstract:
:Calf chymosin molecules exist in the two alternative structural forms: the first one has S1 and S3 binding pockets occluded by its own Tyr77 residue (the self-inhibited form); the second has these pockets free for a substrate binding (the active form). The preliminary incubation of the enzyme with a pentapeptide corresponding to the histidine-proline cluster of the specific substrate kappa-casein results in a 200-fold increase of the hydrolysis rate for the enzyme 'slow substrate'. The result suggests that the cluster is an allosteric effector that promotes the conversion of the enzyme into the active form. These data provide the experimental ground for the explanation of chymosin specificity towards kappa-casein.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gustchina E,Rumsh L,Ginodman L,Majer P,Andreeva Ndoi
10.1016/0014-5793(95)01488-8subject
Has Abstractpub_date
1996-01-22 00:00:00pages
60-2issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(95)01488-8journal_volume
379pub_type
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