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Ligand (S)-coclaurine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for (S)-coclaurine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.140

(S)-coclaurine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine

15230, 288659

-

2.1.1.140

S-Adenosyl-L-methionine + (S)-coclaurine = ?

15231

-

2.1.1.140

S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine

720710, 674802, 735093, 689880, 659190

-

2.1.1.140

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.128

S-adenosyl-L-methionine + (S)-norcoclaurine = S-adenosyl-L-homocysteine + (S)-coclaurine

0

-

Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Substrate (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.17.B1

(S)-coclaurine + ascorbate + O2 = (S)-3-hydroxycoclaurine + dehydroascorbate + H2O

636344

-

1.14.19.50

(S)-coclaurine + [reduced NADPH-hemoprotein reductase] + O2 = ? + [oxidized NADPH-hemoprotein reductase] + 2 H2O

738305

-

1.14.19.66

(S)-N-methylcoclaurine + (R)-N-methylcoclaurine + (S)-coclaurine + [reduced NADPH-hemoprotein reductase] + O2 = (R,S)-berbamunine + (R,R)-guattegaumerine + (R,S)-2'-norberbamunine + [oxidized NADPH-hemoprotein reductase] + H2O

393212, 393214

-

2.1.1.115

S-Adenosylmethionine + (S)-coclaurine = S-Adenosylhomocysteine + N-methylcoclaurine

15190

-

2.1.1.140

(S)-coclaurine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine

15230, 288659

-

2.1.1.140

S-Adenosyl-L-methionine + (S)-coclaurine = ?

15231

-

2.1.1.140

S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine

720710, 674802, 735093, 757949, 689880, 659190, 288659

-

2.1.1.140

S-Adenosyl-L-methionine + (S)-coclaurine = S-Adenosyl-L-homocysteine + N-methylcoclaurine

15231

-

2.1.1.337

2 S-adenosyl-L-methionine + (S)-coclaurine = 2 S-adenosyl-L-homocysteine + (S)-N,N-dimethylcoclaurine

757949

-

2.1.1.337

S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine

757949

-

2.1.1.140

4 entries

2.1.1.337

2 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.3.3

(S)-N-methylcoclaurine + O2 = (S)-coclaurine + H2O2

0

-

2.1.1.128

S-adenosyl-L-methionine + (S)-norcoclaurine = S-adenosyl-L-homocysteine + (S)-coclaurine

0

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.27

-

13450, 13452

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (7 results)

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Show Turnover Number (7 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.19.50

0.022

-

pH 8.0, 30°C

738305

2.1.1.140

0.249

-

mutant E204G, pH 8.0, 30°C

757949

2.1.1.140

6.28

-

wild-type, pH 8.0, 30°C

757949

2.1.1.337

0.00004

-

mutant G204E, pH 8.0, 30°C

757949

2.1.1.337

0.0000404

-

pH 8.0, 37°C, wild-type enzyme

757949

2.1.1.337

0.0003

-

wild-type, pH 8.0, 30°C

757949

2.1.1.337

0.000331

-

pH 8.0, 37°C, mutant enzyme G204E

757949

2.1.1.140

2 entries

2.1.1.337

4 entries

K_M Value (8 results)

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Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.19.50

0.637

-

pH 8.0, 30°C

738305

2.1.1.140

0.0102

-

wild-type, pH 8.0, 30°C

757949

2.1.1.140

0.04

-

-

15230

2.1.1.140

0.0799

-

mutant E204G, pH 8.0, 30°C

757949

2.1.1.337

0.0508

-

mutant G204E, pH 8.0, 30°C

757949

2.1.1.337

0.0508

-

pH 8.0, 37°C, wild-type enzyme

757949

2.1.1.337

0.0624

-

pH 8.0, 37°C, mutant enzyme G204E

757949

2.1.1.337

0.0624

-

wild-type, pH 8.0, 30°C

757949

2.1.1.140

3 entries

2.1.1.337

4 entries

References & Links

Literature References (16)

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Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

13450

-

Purification and properties of 1,2-dehydroreticuline reductase from Papaver somniferum seedlings

1992

De-Eknamkul, W.; Zenk, M.H.

Phytochemistry

31

813-821

13452

-

Homogeneous 1,2-dehydroreticuline reductase from opium poppy plant

1991

De-Eknamkul, W.; Zenk, M.H.

Microb. Util. Renewable Resour.

7

87-98

15190

-

Purification and characterization of three isoforms of S-adenosyl-L-methionine: (R,S)-tetrahydrobenzylisoquinoline-N-methyltransferase from Berberis koetineana cell cultures

1990

Frenzel, T.; Zenk, M.H.

Phytochemistry

29

3491-3497

15230

-

S-Adenosyl-L-methionine:(S)-coclaurine-N-methyltransferase from Tinospora cordifolia

1995

Loeffler, S.; Deus-Neumann, B.; Zenk, M.H.

Phytochemistry

38

1387-1395

15231

-

A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline alkaloid reticuline

1990

Stadler, R.M.; Zenk, M.H.

Liebigs Ann. Chem.

1990

555-562

288659

11314949

Purification and characterization of coclaurine N-methyltransferase from cultured Coptis japonica cells

2001

Choi, K.B.; Morishige, T.; Sato, F.

Phytochemistry

56

649-655

393212

8380416

The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolonifera plant cell cultures

1993

Stadler, R.; Zenk, M.H.

J. Biol. Chem.

268

823-831

393214

8955631

Heterologous expression of alkaloid biosynthetic genes - a review

1996

Kutchan, T.M.

Gene

179

73-81

636344

-

The hydroxylation step in the biosynthetic pathway leading from norcolaurine to reticuline

1990

Loeffler, S.; Zenk, M.H.

Phytochemistry

29

3499-3503

659190

11682473

Molecular cloning and characterization of coclaurine N-methyltransferase from cultured cells of Coptis japonica

2002

Choi, K.B.; Morishige, T.; Shitan, N.; Yazaki, K.; Sato, F.

J. Biol. Chem.

277

830-835

674802

17389594

Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy

2007

Liscombe, D.K.; Facchini, P.J.

J. Biol. Chem.

282

14741-14751

689880

18639640

Heterologous protein production in Escherichia coli using the propionate-inducible pPro system by conventional and auto-induction methods

2008

Lee, S.K.; Keasling, J.D.

Protein Expr. Purif.

61

197-203

720710

22725256

Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes reveals the major route to papaverine in opium poppy

2012

Desgagne-Penix, I.; Facchini, P.

Plant J.

72

331-344

735093

23738019

Comparative transcriptome analysis using high papaverine mutant of Papaver somniferum reveals pathway and uncharacterized steps of papaverine biosynthesis

2013

Pathak, S.; Lakhwani, D.; Gupta, P.; Mishra, B.; Shukla, S.; Asif, M.; Trivedi, P.

PLoS ONE

8

e65622

738305

26941773

CYP96T1 of Narcissus sp. aff. pseudonarcissus catalyzes formation of the para-para' C-C phenol couple in the Amaryllidaceae alkaloids

2016

Kilgore, M.B.; Augustin, M.M.; May, G.D.; Crow, J.A.; Kutchan, T.M.

Front. Plant Sci.

7

225

757949

31765874

A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases

2020

Morris, J.; Yu, L.; Facchini, P.

Phytochemistry

170

112193

Links to other databases for (S)-coclaurine

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Show Links (1 entry)

ChEBI

PubChem