The Enzyme Database

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EC 1.14.19.65     
Accepted name: (S)-cheilanthifoline synthase
Reaction: (S)-scoulerine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-cheilanthifoline + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of stylopine biosynthesis, click here
Other name(s): CYP719A14 (gene name); (S)-scoulerine oxidase (methylenedioxy-bridge-forming) (ambiguous)
Systematic name: (S)-scoulerine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(S)-cheilanthifoline-forming]
Comments: A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline by the oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine. cf. EC 1.14.19.73, (S)-nandinine synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-nandinine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 138791-27-2
References:
1.  Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953–2961.
2.  Diaz Chavez, M.L., Rolf, M., Gesell, A. and Kutchan, T.M. Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana. Arch. Biochem. Biophys. 507 (2011) 186–193. [DOI] [PMID: 21094631]
[EC 1.14.19.65 created 1999 as EC 1.1.3.33, transferred 2002 to EC 1.14.21.2, modified 2016, transferred 2018 to EC 1.14.19.65]
 
 
EC 1.14.19.73     
Accepted name: (S)-nandinine synthase
Reaction: (S)-scoulerine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-nandinine + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of nandinine biosynthesis, click here
Glossary: (S)-scoulerine = (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol
(S)-cheilanthifoline = (6aS)-9-methoxy-6,11,12,14-tetrahydro-2H,6aH-[1,3]dioxolo[4,5-h]isoquino[2,1-b]isoquinolin-8-ol
Other name(s): CYP719A3
Systematic name: (S)-scoulerine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(S)-nandinine-forming]
Comments: A cytochrome P-450 (heme-thiolate) enzyme found in plants. The enzyme catalyses an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid (S)-nandinine by the oxidative ring closure of adjacent phenolic and methoxy groups of (S)-scoulerine. cf. EC 1.14.19.65, (S)-cheilanthifoline synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-cheilanthifoline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ikezawa, N., Iwasa, K. and Sato, F. Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia californica. FEBS J. 274 (2007) 1019–1035. [DOI] [PMID: 17250743]
2.  Diaz Chavez, M.L., Rolf, M., Gesell, A. and Kutchan, T.M. Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana. Arch. Biochem. Biophys. 507 (2011) 186–193. [DOI] [PMID: 21094631]
[EC 1.14.19.73 created 2016 as EC 1.14.21.12, transferred 2018 to EC 1.14.19.73]
 
 
EC 1.14.21.2      
Transferred entry: (S)-cheilanthifoline synthase. Now EC 1.14.19.65, (S)-cheilanthifoline synthase
[EC 1.14.21.2 created 2002, modified 2016, deleted 2018]
 
 
EC 1.14.21.12      
Transferred entry: (S)-nandinine synthase. Now EC 1.14.19.73, (S)-nandinine synthase
[EC 1.14.21.12 created 2016, deleted 2018]
 
 
EC 1.21.3.3     
Accepted name: reticuline oxidase
Reaction: (S)-reticuline + O2 = (S)-scoulerine + H2O2
For diagram of stylopine biosynthesis, click here
Other name(s): BBE; berberine bridge enzyme; berberine-bridge-forming enzyme; tetrahydroprotoberberine synthase
Systematic name: (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming)
Comments: Contains FAD. The enzyme from the plant Eschscholtzia californica binds the cofactor covalently [3]. Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge (’berberine bridge’) of (S)-tetrahydroprotoberberines. The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 152232-28-5
References:
1.  Steffens, P., Nagakura, N. and Zenk, M.H. The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis. Tetrahedron Lett. 25 (1984) 951–952.
2.  Dittrich, H. and Kutchan, T.M. Molecular cloning, expression and induction of the berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc. Natl. Acad. Sci. USA 88 (1991) 9969–9973. [DOI] [PMID: 1946465]
3.  Kutchan, T.M. and Dittrich, H. Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in higher plants. J. Biol. Chem. 270 (1995) 24475–24481. [DOI] [PMID: 7592663]
[EC 1.21.3.3 created 1989 as EC 1.5.3.9, transferred 2002 to EC 1.21.3.3]
 
 
EC 2.1.1.117     
Accepted name: (S)-scoulerine 9-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (S)-scoulerine = S-adenosyl-L-homocysteine + (S)-tetrahydrocolumbamine
For diagram of columbamine, palmatine and corydaline biosynthesis, click here
Systematic name: S-adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase
Comments: The product of this reaction is a precursor for protoberberine alkaloids in plants
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 96380-65-3
References:
1.  Muemmler, S., Rueffer, M., Nagakura, N., Zenk, M.H. S-Adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase, a highly stereo- and regiospecific enzyme in tetrahydroberberine biosynthesis. Plant Cell Reports 4 (1985) 36–39. [PMID: 24253642]
[EC 2.1.1.117 created 1999]
 
 
EC 2.1.1.300     
Accepted name: pavine N-methyltransferase
Reaction: S-adenosyl-L-methionine + (±)-pavine = S-adenosyl-L-homocysteine + N-methylpavine
Other name(s): PavNMT
Systematic name: S-adenosyl-L-methionine:(±)-pavine N-methyltransferase
Comments: The enzyme, isolated from the plant Thalictrum flavum, also methylates (R,S)-stylopine and (S)-scoulerine (11%) with lower activity (14% and 11%, respectively).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jain, A., Ziegler, J., Liscombe, D.K., Facchini, P.J., Tucker, P.A. and Panjikar, S. Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1066–1069. [DOI] [PMID: 18997344]
2.  Liscombe, D.K., Ziegler, J., Schmidt, J., Ammer, C. and Facchini, P.J. Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species. Plant J. 60 (2009) 729–743. [DOI] [PMID: 19624470]
[EC 2.1.1.300 created 2014]
 
 


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