Abstract:
:The glyceraldehyde 3-phosphate dehydogenase holoenzyme of Bacillus stearothermophilus possesses precise 222 symmetry: in this respect it differs from the reported structure of the lobster muscle enzyme. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer.
journal_name
Naturejournal_title
Natureauthors
Biesecker G,Harris JI,Thierry JC,Walker JE,Wonacott AJdoi
10.1038/266328a0subject
Has Abstractpub_date
1977-03-24 00:00:00pages
328-33issue
5600eissn
0028-0836issn
1476-4687journal_volume
266pub_type
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