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Literature summary for 4.2.1.78 extracted from

  • Lichman, B.R.; Sula, A.; Pesnot, T.; Hailes, H.C.; Ward, J.M.; Keep, N.H.
    Structural evidence for the dopamine-first mechanism of norcoclaurine synthase (2017), Biochemistry, 56, 5274-5277 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis the enzyme has also shown great potential as a biocatalyst for the formation of chiral isoquinolines Thalictrum flavum

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution X-ray crystallography. The structure supports two features of the dopamine-first mechanism: the binding of dopamine catechol to Lys-122 and the position of the carbonyl substrate binding site at the active site entrance. The catalytically vital residue Glu-110 occupies a ligand-bound conformation that may be catalytically significant Thalictrum flavum

Organism

Organism UniProt Comment Textmining
Thalictrum flavum Q67A25
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General Information

General Information Comment Organism
metabolism the enzyme is a Pictet-Spenglerase that catalyzes a step in plant benzylisoquinoline alkaloid metabolism, a compound family that includes bioactive natural products such as morphine Thalictrum flavum