Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.

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

Nature

journal_title

Nature

authors

Biesecker G,Harris JI,Thierry JC,Walker JE,Wonacott AJ

doi

10.1038/266328a0

subject

Has Abstract

pub_date

1977-03-24 00:00:00

pages

328-33

issue

5600

eissn

0028-0836

issn

1476-4687

journal_volume

266

pub_type

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