Abstract:
:In this review, various experiments which establish the occurrence of covalent modification mechanisms, both in vivo and in vitro, in the control of acetyl-CoA carboxylase have been presented. It is interesting to note that phosphorylation of the carboxylase results in disaggregation of the active species. These studies indicate that aggregation and disaggregation of the enzyme are involved in the control of carboxylase activity. Our covalent modification mechanism and the allosteric control mechanism share a common ground in that both mechanisms affect the equilibrium between protomers and polymers of the enzyme. However, it is clear that the allosteric control mechanism cannot function alone under normal physiological conditions. Covalent modification of the carboxylase is prerequisite for efficient functioning of the allosteric mechanism. There are many aspects of the regulation of acetyl-CoA carboxylase which require further clarification. However, it is now established that short-term control of acetyl-CoA carboxylase involves the covalent modification mechanism.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Kim KHdoi
10.1007/BF00223358subject
Has Abstractpub_date
1979-12-14 00:00:00pages
27-43issue
1-3eissn
0300-8177issn
1573-4919journal_volume
28pub_type
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