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 Lettjournal_title
FEBS lettersauthors
Linkens HJ,Djavadi-Ohaniance L,Goldberg MEdoi
10.1016/0014-5793(93)80591-hsubject
Has Abstractpub_date
1993-04-12 00:00:00pages
224-8issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(93)80591-Hjournal_volume
320pub_type
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