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Record 1 2011-01-05


Subject field(s)
  • Biological Sciences

Amino acid residue directly involved in the covalent bond changes during enzyme action.


Chymotrypsinogen has a single polypeptide chain of 245 residues held together by five intrachain disulfide bridges... It is converted into active [alpha] chymotrypsin by the enzymatic hydrolysis of four peptide linkages, by sequential action of trypsin and chymotrypsin, with the release of two dipeptides. The active [alpha] chymotrypsin produced this way consists of three polypeptide chains held together by two -S-S bonds. Thus the two specific residues essential for catalytic activity, histidine 57 and serine 195, are present in two different chains. However, it has been directly established by x-ray analysis of the tertiary structure of chymotrypsin that these ... catalytic residues ... are actually very close to each other in the conformation of the native enzyme.


  • Sciences biologiques

Le chymotrypsinogène est composé d'une chaîne polypeptidique unique contenant 245 acides aminés et comportant cinq liaisons disulfure intracaténaires. Il est transformé en [alpha]-chymotrypsine active par l'hydrolyse enzymatique de quatre liaisons peptidiques sous l'influence séquentielle de la trypsine et de la chymotrypsine, avec libération de deux dipeptides. L'[alpha]-chymotrypsine active ainsi produite est constituée de trois chaînes polypeptidiques maintenues par deux liaisons -S-S. Ainsi, les deux acides aminés spécifiques essentiels à l'activité catalytique, l'histidine en position 57 et la sérine 195, se trouvent dans deux chaînes différentes. Néanmoins, des analyses aux rayons X de la structure tertiaire de la chymotrypsine ont établi directement que ces [...] résidus catalytiques [...] se trouvent en fait très proches l'un de l'autre dans la conformation de l'enzyme natif.


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