Berbamunine synthase

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In enzymology, berbamunine synthase (EC 1.14.19.66, Formerly EC 1.1.3.34 and EC 1.14.21.3) is an enzyme that catalyzes the combination of two benzylisoquinoline alkaloids

2D representation of the chemical structure of Q27102185.
(S)-N-methylcoclaurine
+
 
2D representation of the chemical structure of Q27101882.
(R)-N-methylcoclaurine
 
O2
2 H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27102072.
berbamunine

The enzyme has a cofactor, a reduced nicotinamide adenine dinucleotide phosphate in combination with a hemoprotein, which allows it to use molecular oxygen to oxidatively combine the alkaloid substrates.[1][2][3]

It can combine related alkaloids differing only in the degree of methylation of the phenolic oxygens. For example, (S)-coclaurine also reacts with (R)-N-methylcoclaurine to give 2'-norberbamunine and dimerisation of (R)-N-methylcoclaurine gives guattegaumerine.[1][3]

+
 
2D representation of the chemical structure of Q27101882.
(R)-N-methylcoclaurine
 
O2
2 H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27105368.
2'-norberbamunine

The enzyme belongs to the family of oxidoreductases and its systematic name is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O phenol-coupling). It is also called (S)-N-methylcoclaurine oxidase (C-O phenol-coupling). It was first isolated from Berberis stolonifera and participates in alkaloid biosynthesis.[2][3]

References

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