Nicking of the tryptophan synthase beta 2-subunit at Glu-296 prevents the conformational change undergone on binding the alpha-subunit.

Abstract:

:Using a monoclonal antibody as conformational probe it has been shown that the weakly active nicked-beta 2 dimer of tryptophan synthase generated by proteolytic cleavage at Glu-296, does not undergo on association with alpha subunit a conformational change known to occur in intact beta 2 subunit. This alpha induced conformational change is also prevented in intact beta 2 by the coenzyme pyridoxal-5'-phosphate when the substrate L-serine is absent.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Linkens HJ,Djavadi-Ohaniance L,Goldberg ME

doi

10.1016/0014-5793(93)80591-h

subject

Has Abstract

pub_date

1993-04-12 00:00:00

pages

224-8

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80591-H

journal_volume

320

pub_type

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