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Function(s) and Biological Relevance
The protein being studied is Tetrahydroprotoberberine N-methyltransferase. This protein is found in yellow horned poppy (Glaucium flavium) and gives insights into substrate recognition and catalysis for the rational engineering of enzymes for chemoenzymatic synthesis and metabolic engineering. The substrate specificity of Tetrahydroprotoberberine N-methyltransferase arises from the arrangement of subgroup-specific stereospecific recognition elements relative to catalytic elements that are more widely-conserved among all Benzylisoquinoline alkaloids (BIA) N-methyltransferases (NMT).
Broader Implications
It is relevant because of the importance and utility of BIA compounds such as the use of metabolic engineering and synthetic biology approaches to reconstitute portions of the BIA biosynthetic pathways. However, most experiments have not provided substantial proof and explanations. In order to address this central problem in metabolic engineering, fundamental molecular, structural, and functional studies of BIA enzymes are needed. Overall, a deeper understanding of the enzyme structure and function will lead to an improved understanding of how BIA diversity is generated.
Structural highlights and structure-function relationships
Energy Transformation
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