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.

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 Lett

journal_title

FEBS letters

authors

Gustchina E,Rumsh L,Ginodman L,Majer P,Andreeva N

doi

10.1016/0014-5793(95)01488-8

subject

Has Abstract

pub_date

1996-01-22 00:00:00

pages

60-2

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01488-8

journal_volume

379

pub_type

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