| Literature DB >> 193030 |
G Biesecker, J I Harris, J C Thierry, J E Walker, A J Wonacott.
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.Entities:
Mesh:
Substances:
Year: 1977 PMID: 193030 DOI: 10.1038/266328a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962