Regulation
Since the discovery and characterization of sucrose phosphorylase, few documented experiments discuss mechanisms of regulation for the enzyme. The known methods of regulation are transcriptional, affecting the amount of enzyme present at any given time.
Global regulation of DNA molecules containing the gene for sucrose phosphorylase is performed by catabolite repression. First discovered in Gram-negative bacteria, both Cyclic AMP (cAMP) and cAMP Receptor Protein (CRP) function in sucrose phosphorylase regulation (Reid and Abratt 2005). The cAMP-CRP complex formed when both molecules combine acts as a positive regulator for transcription of the sucrose phosphorylase gene. The complex binds to the promoter region to activate transcription, enhancing the creation of sucrose phosphorylase (Nelson and Cox 2005).
Genetic regulation of sucrose phosphorylase is also performed by metabolites. Through experimentation it is known that genes encoding for the sucrose phosphorylase enzyme can be induced by sucrose and raffinose (Trindade, Abratt, and Reid 2003). Glucose, on the other hand, represses the transcription of the sucrose phosphorylase gene (Trindade, Abratt, and Reid 2003). These metabolites undoubtedly function in this way because of their implications in cellular metabolism.
There has been little research on methods of the allosteric regulation of sucrose phosphorylase, so at this point the function of allosteric molecules can only be hypothesized. Due to the nature of its function in metabolic pathways, it is likely that sucrose phosphorylase is additionally regulated by other common metabolites. For example, the presence of ATP would probably inhibit sucrose phosphorylase since ATP is a product of the catabolic pathway. Conversely, ADP would likely stimulate sucrose phosphorylase to increase levels of ATP. Further research on the subject would be required to support or refute these ideas.
Read more about this topic: Sucrose Phosphorylase
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