Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.
Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.
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DOI：
10.1016/j.abb.2011.10.005
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发表时间：
2012-03-15
影响因子：
3.9
通讯作者：
Grant GA
中科院分区：
文献类型：
--
作者：
Grant GA
D-3-Phosphoglycerate dehydrogenases (PGDH) exist with at least three different structural motifs and the enzymes from different species display distinctly different mechanisms. In many species, particularly bacteria, the catalytic activity is regulated allosterically through binding of L-serine to a distinct structural domain, termed the ACT domain. Some species, such as M. tuberculosis, contain an additional domain, called the "allosteric substrate binding" or ASB domain, that functions as a co-domain in the regulation of catalytic activity. That is, both substrate and effector function synergistically in the regulation of activity to give the enzyme some interesting properties that may have physiological relevance for the persistent state of tuberculosis. Both enzymes function through a V-type regulatory mechanism and, in the E. coli enzyme, it has been demonstrated that this results from a dead-end complex that decreases the concentration of active species rather than a decrease in the velocity of the active species. This review compares and contrasts what we know about these enzymes and provides additional insight into their mechanism of allosteric regulation.
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