Prostaglandin H synthase Inactivation of the enzyme in the course of catalysis is accompanied by fast and dramatic changes in protein structure


AbstractProstaglandin H synthase (PGHS) as apo-PGHS, holo-PGHS, and holo-PGHS, inactivated in the course of catalysis was studied using chemical modification with diethyl pyrocarbonate (DEPC). The exhausted reaction with DEPC corresponded to the modification of 7 histidine residues in apo-PGHS and 4 in holo-PGHS. All 18 histidine residues became accessible for modification with DEPC in the enzyme, inactivated in the course of catalysis. The velocities of tryptic cleavage of all the three forms into two fragments were fairly different but independent of modification. Based on the results we hypothesize fast and dramatic changes in the protein structure in the course of the substrate conversion

Similar works

Full text


Elsevier - Publisher Connector

Provided a free PDF
Last time updated on 5/6/2017View original full text link

This paper was published in Elsevier - Publisher Connector .

Having an issue?

Is data on this page outdated, violates copyrights or anything else? Report the problem now and we will take corresponding actions after reviewing your request.