Sandbox Reserved 1564

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

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

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.