Tetrahydroprotoberberine N-methyltransferase
From Proteopedia
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<StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine complex with SAM (PDB code [[6p3n]])' scene=''> | <StructureSection load='6P3N' size='340' side='right' caption='Tetrahydroprotoberbine complex with SAM (PDB code [[6p3n]])' scene=''> | ||
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'''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right. | '''Tetrahydroprotoberbine N-methyltransferase''' is a protein thats dimer interface includes six salt 6 salt bridges and 8 hydrogens bonds. It is expressed in E. ''coli'' and crystallized at a pH of 7.0. The crystals were grown in the presence of SAH,SAM, and SAH+SMS. Below are the two different substrates that were in the presence of the crystallized protein. The substrate SAM is shown to the right. | ||
[[Image:6p3o.pdb1-500.jpg]] | [[Image:6p3o.pdb1-500.jpg]] |
Revision as of 10:13, 19 January 2020
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References
- ↑ Takao, N., Kamigauchi, M., and Okada, M. (1983) Biosynthesis of benzo-[c]phenanthridine alkaloids sanguinarine, chelirubine and macarpine.Helv. Chim. Acta 66, 473–484 CrossRef
- ↑ Bennett, M. R., Thompson, M. L., Shepherd, S. A., Dunstan, M. S., Herbert, A. J., Smith, D. R. M., Cronin, V. A., Menon, B. R. K., Levy, C., and Micklefield, J. (2018) Structure and biocatalytic scope of coclaurine Nmethyltransferase.Angew. Chem. Int. Ed. Engl. 57, 10600–10604CrossRef Medline