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Ligand norepinephrine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

catecholamine biosynthesis

KEGG

Adrenergic signaling in cardiomyocytes, cAMP signaling pathway, Chemical carcinogenesis - receptor activation, Gap junction, Neuroactive ligand-receptor interaction, Quorum sensing, Regulation of lipolysis in adipocytes, Renin secretion, Salivary secretion, Synaptic vesicle cycle, Taste transduction, Thermogenesis, Two-component system, Tyrosine metabolism, Vascular smooth muscle contraction more

MetaCyc

catecholamine biosynthesis, noradrenaline and adrenaline degradation

Show all BRENDA pathways known for norepinephrine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.4

noradrenaline + H2O + O2 = ?

725622

-

1.4.3.4

norepinephrine + H2O + O2 = ?

702900, 711407, 711912

-

1.4.3.4

2 entries

1.6.3.5

norepinephrine + O2 = ?

743215

-

2.1.1.28

S-adenosyl-L-methionine + norepinephrine = S-adenosyl-L-homocysteine + epinephrine

697358, 672557, 696719

3hcd, 3D-view

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

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.17.1

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

0, 438601, 438614, 438610, 438613, 438620, 438621

-

1.14.17.1

dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

0

-

1.14.17.1

dopamine + ascorbate + O2 = norepinephrine + dehydroascorbate + H2O

0

-

1.14.17.1

3 entries

Substrate in Enzyme-catalyzed Reactions (29 results)

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Show Substrate (29 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.B4

norepinephrine + NAD+ = ? + NADH + H+

743703

-

1.1.3.38

norepinephrine + O2 = ?

10665

-

1.10.3.1

L-noradrenaline + O2 = ?

657987

-

1.10.3.1

norepinephrine + O2 = ?

686692

-

1.14.18.1

noradrenaline + O2 = ?

636375

-

1.14.18.1

norepinephrine + O2 = ?

636353

-

1.10.3.1

2 entries

1.14.18.1

2 entries

1.16.3.1

L-norepinephrine + Fe2+ + O2 = ?

438006

-

1.4.3.22

norepinephrine + H2O + O2 = ?

391951

-

1.4.3.4

noradrenaline + H2O + O2 = (2R)-(3,4-dihydroxyphenyl)(hydroxy)acetaldehyde + NH3 + H2O2

742990, 742989, 742988

-

1.4.3.4

noradrenaline + H2O + O2 = ?

725621, 725622

-

1.4.3.4

norepinephrine + H2O + O2 = ?

702900, 711407, 711912

-

1.4.3.4

3 entries

1.6.3.5

norepinephrine + O2 = ?

743215

-

2.1.1.28

L-norepinephrine + S-adenosyl-L-methionine = epinephrine + S-adenosyl-L-homocysteine

639430, 639432, 639436, 639440, 639445

3hcd, 3D-view

2.1.1.28

S-adenosyl-L-methionine + noradrenaline = S-adenosyl-L-homocysteine + epinephrine

718999, 720467

3hcd, 3D-view

2.1.1.28

norepinephrine + S-adenosyl-L-methionine = epinephrine + S-adenosyl-L-homocysteine

639451, 639447, 639434, 639435, 639436, 639439, 639440, 639441, 639446

3hcd, 3D-view

2.1.1.28

S-adenosyl-L-methionine + norepinephrine = S-adenosyl-L-homocysteine + epinephrine

697358, 672557, 696719

3hcd, 3D-view

2.1.1.28

4 entries

2.1.1.336

2 S-adenosyl-L-methionine + (-)-norepinephrine = 2 S-adenosyl-L-homocysteine + 4-O-methylnorepinephrine + 3-O-methylnorepinephrine

756959

-

2.1.1.6

noradrenaline + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + ?

441546

-

2.1.1.6

S-adenosyl-L-methionine + noradrenaline = S-adenosyl-L-homocysteine + ?

658517

-

2.1.1.6

norepinephrine + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + normetanephrine

441540, 706484, 441507, 441514

-

2.1.1.6

S-adenosyl-L-methionine + norepinephrine = S-adenosyl-L-homocysteine + ?

686194, 657525, 686075

-

2.1.1.6

S-adenosyl-L-methionine + norepinephrine = S-adenosyl-L-homocysteine + normetanephrine

685455

-

2.1.1.6

5 entries

2.3.1.110

feruloyl-CoA + noradrenaline = CoA + feruloylnoradrenaline

486133, 486132, 486126

-

2.3.1.5

acetyl-CoA + noradrenaline = CoA + ?

487116

-

2.3.1.87

acetyl-CoA + norepinephrine = CoA + N-acetylnorepinephrine

686212, 719595, 673165, 735981, 756913

-

2.8.2.1

3'-phosphoadenylylsulfate + norepinephrine = adenosine 3',5'-bisphosphate + ?

660916

-

2.8.2.1

3'-phosphoadenylylsulfate + norepinephrine = adenosine 3',5'-bisphosphate + norepinephrine sulfate

645654, 645680, 645641

-

2.8.2.1

2 entries

2.8.2.3

3'-phosphoadenylylsulfate + noradrenaline = adenosine 3',5'-bisphosphate + noradrenaline N-sulfate

645860

-

4.2.1.87

norepinephrine = ?

288289

-

Product in Enzyme-catalyzed Reactions (6 results)

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Show Product (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.9

octopamine + FMNH + O2 = norepinephrine + FMN + H2O

0

-

1.14.17.1

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

438631, 438632, 0, 438601, 438614, 438634, 438602, 438598, 438633, 438636, 438597, 438599, 438606, 438607, 438608, 438610, 438611, 438612, 438613, 438615, 438616, 438617, 438618, 438619, 438620, 438621, 438627, 438629, 438626, 438609, 438603

-

1.14.17.1

dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

0

-

1.14.17.1

dopamine + ascorbate + O2 = norepinephrine + dehydroascorbate + H2O

0

-

3.1.6.1

norepinephrine 3-sulfate + H2O = norepinephrine + sulfate

0

-

3.1.6.1

norepinephrine 4-sulfate + H2O = norepinephrine + sulfate

0

-

1.14.17.1

3 entries

3.1.6.1

2 entries

Activator in Enzyme-catalyzed Reactions (10 results)

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Show Activating Compound (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.146

activates isozyme 11beta-HSD1 2.5fold

669504

-

1.14.99.1

-

438392

-

2.5.1.6

induction of enzyme in organ cell culture

659509

-

2.6.1.5

slight activation

640113

-

2.7.1.107

stimulates an increase in diacylglycerol kinase activity in caveolae/rafts of mesenteric arteries. Activation depends on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts

671248

-

4.6.1.1

-

729827

-

4.6.1.1

about 2fold activation by 0.1 mM

709677

-

4.6.1.1

activates endogenously expressed b-adrenergic receptors, signal transduction from beta-adrenergic receptors via trimeric Gs proteins to their downstream targets, e.g. ACs

681532

-

4.6.1.1

significantly activates cortical adenylyl cyclase

716341

-

4.6.1.1

4 entries

7.2.2.13

hypothesis: stimulate Na+/K+ transport via specific receptor inputs

672864

-

Inhibitor in Enzyme-catalyzed Reactions (32 results)

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Show Inhibitors (32 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.153

3 mM: 30% inhibition

286023

-

1.13.11.34

IC50: 0.49 mM

439461

-

1.14.11.4

-

439156

-

1.14.16.1

-

438714

4pah, 3D-view

1.14.16.2

competitive

659762

-

1.14.16.2

-

438706, 659762, 688519, 699645

-

1.14.16.2

-

438688, 438691, 671818

-

1.14.16.2

feedback inhibitor

713957

-

1.14.16.2

4 entries

1.14.17.1

-

438603

-

1.17.3.2

15% inhibition at 0.1 mM, 30% inhibition at 1 mM

654034

-

1.2.3.1

0.1 mM, 51% and 95% inhibition of phenanthridine and N-methylphthalazine oxidation, respectively; 0.1 mM and 1 mM, 90% and 100% inhibition of benzaldehyde oxidation, respectively

654034

-

1.5.1.34

-

484974

-

1.5.1.34

no inhibition below 0.2 mM

484978

-

1.5.1.34

-

484974

-

1.5.1.34

0.2 mM, 50% inhibition

484984

-

2.1.1.28

substrate inhibition

639432

3hcd, 3D-view

2.1.1.28

4 distinct substrate inhibition patterns: enzyme form E1 is not subject to substrate inhibition, isoenzyme E-2 is inhibited by S-adenosyl-L-methionine and norepinephrine, isoenzyme E-3 and E-4 are inhibited by norepinephrine only, isoenzyme E5 is inhibited only by S-adenosyl-L-methionine

639435

3hcd, 3D-view

2.1.1.28

at high concentrations

639433

3hcd, 3D-view

2.1.1.28

noncompetitive inhibition with phenylethanolamine as substrate, competitive inhibition with normetanephrine as substrate

639447

3hcd, 3D-view

1.5.1.34

4 entries

2.1.1.28

4 entries

2.1.1.6

0.01 mM, 41% inhibition of 2-hydroxyestradiol methylation

658885

-

2.3.1.37

-

757560

-

2.6.1.5

competitive inhibition

640109

-

2.7.1.35

-

641414

-

2.7.8.1

substrate: diacylglycerol or alkylacylglycerol

644360

-

2.7.8.2

-

644360

-

4.1.1.28

-

4208

-

4.1.1.28

40% inhibition at 4 mM

743978

-

4.1.1.28

2 entries

4.1.1.29

reversed by addition of 0.1 mM pyridoxal 5'-phosphate

4237

-

4.6.1.1

adenylate cyclase is almost completely inhibited by 0.5 mM noradrenaline

707801

-

6.3.2.11

-

996

-

6.3.2.18

1 mM inhibits synthesis of Nalpha-gamma-L-glutamylhistamine by 73%

1102

-

6.3.2.18

1 mM inhibits Nalpha-gamma-L-glutamylhistamine synthesis by 73%

1102

-

6.3.2.18

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (5 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (5 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.16.1

4pah, 3D-view

2.1.1.28

3hcd, 3D-view

2.7.11.11

5n3l, 3D-view

3.2.1.17

7bu6, 3D-view

3.4.23.22

4y4j, 3D-view

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

1.1.3.38

0.3

-

-

10665

1.10.3.1

0.0000000912

-

pH 7.2, 20°C

657987

1.4.3.22

65

-

-

391951

2.1.1.6

0.04

-

S-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.1.1.6

0.18

-

MB-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.3.1.87

3.17

-

pH 7.3, 22°C, recombinant aaNAT2

719595

2.3.1.87

7.76

-

pH 7.3, 22°C, recombinant aaNAT1

719595

2.1.1.6

2 entries

2.3.1.87

2 entries

K_M Value (43 results)

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Show KM Value (43 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.38

2.9

-

-

10665

1.10.3.1

0.0000194

-

pH 7.2, 20°C

657987

1.14.18.1

0.61

-

-

636353

1.14.18.1

2

-

-

636375

1.14.18.1

2 entries

1.16.3.1

0.00281

-

-

438006

1.4.3.22

1.05

-

-

391951

1.4.3.4

0.57

-

at pH 7.4 and 25°C

742988

1.4.3.4

0.63

-

at pH 7.4 and 25°C

742989

1.4.3.4

0.79

-

at pH 7.4 and 25°C

742988

1.4.3.4

1.04

-

at pH 7.4 and 25°C

742988

1.4.3.4

1.9

-

at pH 7.4 and 25°C

742988

1.4.3.4

3.5

-

at pH 7.4 and 25°C

742990

2.1.1.28

0.015

-

-

639440

2.1.1.28

0.0184

-

wild-type enzyme

639451

2.1.1.28

0.0299

-

enzyme form H-2

639432

2.1.1.28

0.0428

-

enzyme form H-1

639432

2.1.1.28

0.101

-

-

639445

2.1.1.6

0.0055

-

corebral cortex, membrane-bound form

657525

2.1.1.6

0.0055

0.114

membrane-bound enzyme form

686194

2.1.1.6

0.00587

-

cerebellum, membrane-bound form

657525

2.1.1.6

0.00837

-

brain stem, membrane-bound form

657525

2.1.1.6

0.00912

-

hippocampus, membrane-bound form

657525

2.1.1.6

0.0105

-

hypophysis, membrane-bound form

657525

2.1.1.6

0.0114

-

hypothalamus, membrane-bound form

657525

2.1.1.6

0.024

-

recombinant enzyme expressed in Sf9 cells, membrane-bound enzyme form

686194

2.1.1.6

0.0306

-

MB-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.1.1.6

0.169

-

heart

441514

2.1.1.6

0.224

-

S-COMT, 0.1 mM S-adenosyl-L-methionine

686075

2.1.1.6

0.276

-

brain

441514

2.1.1.6

0.304

-

corebral cortex, soluble enzyme

657525

2.1.1.6

0.304

0.464

soluble enzyme form

686194

2.1.1.6

0.305

-

hippocampus, soluble enzyme

657525

2.1.1.6

0.313

-

cerebellum, soluble enzyme

657525

2.1.1.6

0.369

-

recombinant enzyme expressed in Sf9 cells, soluble enzyme form

686194

2.1.1.6

0.39

-

brain stem, soluble enzyme

657525

2.1.1.6

0.443

-

hypothalamus, soluble enzyme

657525

2.1.1.6

0.465

-

hypophysis, soluble enzyme

657525

2.1.1.6

1.856

-

liver

441514

1.4.3.4

6 entries

2.1.1.28

5 entries

2.1.1.6

21 entries

2.3.1.110

1.57

-

-

486132

2.3.1.87

0.05

-

pH not specified in the publication, temperature not specified in the publication

756913

2.3.1.87

0.16

-

pH 7.3, 22°C, recombinant aaNAT1

719595

2.3.1.87

0.17

-

pH 7.3, 22°C, recombinant aaNAT2

719595

2.3.1.87

3 entries

2.8.2.1

0.1

-

pH 9.0, 37°C

645654

K_i Value (13 results)

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Show KI Value (13 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.153

3.1

-

pH 6.4, 25°C, erythrocyte enzyme

286023

1.1.1.153

3.4

-

pH 6.4, 25°C, brain enzyme

286023

1.14.16.2

0.25

-

enzyme from hypothalamus, preparatory phase

659762

1.14.16.2

0.28

-

enzyme from telencephalon, resting phase

659762

1.14.16.2

0.3

-

enzyme from hypothalamus, resting phase

659762

1.14.16.2

0.32

-

enzyme from telencephalom, resting phase

659762

1.1.1.153

2 entries

1.14.16.2

4 entries

1.14.17.1

5

-

-

438603

1.5.1.34

0.016

-

noncompetitive vs. NADH

484984

1.5.1.34

0.19

-

noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine

484984

1.5.1.34

0.49

-

noncompetitive inhibition

484974

2.1.1.28

0.0059

-

noncompetitive with phenylethanolamine

639447

2.1.1.28

0.165

-

enzyme form H-1, substrate inhibition

639432

2.1.1.28

0.631

-

enzyme form H-2, substrate inhibition

639432

1.5.1.34

3 entries

2.1.1.28

3 entries

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.13.11.34

0.49

-

IC50: 0.49 mM

439461

References & Links

Literature References (128)

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Show Reference (128 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

996

954961

The effect of various agents in vitro on homocarnosine-carnosine synthetase from rat brain

1976

Ng, R.H.; Marshall, F.D.

Experientia

32

839-841

1102

6125565

An in vitro characterization of gamma-glutamylhistamine synthetase: a novel enzyme catalyzing histamine metabolism in the central nervous system of the marine mollusk, Aplysia californica

1982

Stein, C.; Weinreich, D.

J. Neurochem.

38

204-214

4208

-

Inhibition of aromatic L-amino acid decarboxylase from Micrococcus percitreus by substrate analogs

1987

Nakazawa, H.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

51

2531-2537

4237

236774

Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties

1975

Guion-Rain, M.C.; Portemer, C.; Chatagner, F.

Biochim. Biophys. Acta

384

265-276

10665

8529652

Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols

1995

Fraaije, M.W.; Veeger, C.; van Berkel, W.J.H.

Eur. J. Biochem.

234

271-277

286023

7046745

Direct inhibition of brain sepiapterin reductase by a catecholamine and an indoleamine

1982

Katoh, S.; Sueoka, T.; Yamada, S.

Biochem. Biophys. Res. Commun.

105

75-81

288289

3034855

Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes

1987

Cuskey, S.M.; Peccoraro, V.; Olsen, R.H.

J. Bacteriol.

169

2398-2404

391951

7727530

Amine oxidases from Aspergillus niger: identification of a novel flavin-dependent enzyme

1995

Schilling, B.; Lerch, K.

Biochim. Biophys. Acta

1243

529-537

438006

775938

Ceruloplasmin: the copper transport protein with essential oxidase activity

1976

Frieden, E.; Hsieh, H.S.

Adv. Enzymol. Relat. Areas Mol. Biol.

44

187-236

438392

5070652

Prostaglandin synthetase activity in the rat stomach fundus. Activation by L-norepinephrine and related compounds

1972

Pace-Asciak, C.

Biochim. Biophys. Acta

280

161-171

438597

6795996

Purification of membrane-bound dopamine beta-monooxygenase from chromaffin granules: relation to soluble dopamine beta-monooxygenase

1981

Slater, E.P.; Zaremba, S.; Hogue-Angeletti, R.A.

Arch. Biochem. Biophys.

211

288-296

438598

6733150

Purification and characterization of rat dopamine beta-monooxygenase and monoclonal antibodies to the enzyme

1984

Okuno, S.; Fujisawa, H.

Biochim. Biophys. Acta

799

260-269

438599

8286345

Oxygen-18 kinetic isotope effects in the dopamine beta-monooxygenase reaction: Evidence for a new chemical mechanism in non-heme, metallomonooxygenase

1994

Tian, G.; Berry, J.A.; Klinman, J.P.

Biochemistry

33

226-234

438601

3101599

Characterization of highly purified dopamine beta-hydroxylase

1987

Colombo, G.; Papadopoulos, N.J.; Ash, D.E.; Villafranca, J.J.

Arch. Biochem. Biophys.

252

71-80

438602

567644

Human plasma dopamine beta-hydroxylase. Purification and properties

1978

Frigon, R.P.; Stone, R.A.

J. Biol. Chem.

253

6780-6786

438603

7326235

Purification and characterization of avian dopamine beta-hydroxylase

1981

Long, R.A.; Weppelman, R.M.; Taylor, J.E.; Tolman, R.L.; Olson, G.

Biochemistry

20

7423-7431

438606

3609611

Characterization and kinetic studies of deglycosylated dopamine beta-hydroxylase

1987

Hamos, J.; Desai, P.R.; Villafranca, J.J.

FASEB J.

1

143-148

438607

14416204

The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine

1960

Levin, E.Y.; Levenberg, B.; Kaufman, S.

J. Biol. Chem.

235

2080-2086

438608

5846992

3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity

1965

Friedman, S.; Kaufman, S.

J. Biol. Chem.

240

4763-4773

438609

7378421

Inhibition of dopamine-beta-hydroxylase by alternative electron donors

1980

Rosenberg, R.C.; Gimble, J.M.; Lovenberg, W.

Biochim. Biophys. Acta

613

62-72

438610

6860408

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J. Evol. Biochem. Physiol.

49

300-308

742989

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Enzymologic characteristics of monoamine oxidase from liver of the skipjack tuna Katsuwonus pelamis

2013

Basova, I.; Yagodina, O.

J. Evol. Biochem. Physiol.

49

562-569

742990

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Catalytic properties of liver monoamine oxidase in the chum salmon Oncorhynchus keta

2015

Basova, I.; Basova, N.; Yagodina, O.

J. Evol. Biochem. Physiol.

51

370-377

743215

24762661

Renalase, a new secretory enzyme Its role in hypertensive-ischemic cardiovascular diseases

2014

Li, X.; Huang, R.; Xie, Z.; Lin, M.; Liang, Z.; Yang, Y.; Jiang, W.

Med. Sci. Monit.

20

688-692

743703

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Purification and characterization of a novel carbonyl reductase involved in oxidoreduction of aromatic beta-amino ketones/alcohols

2014

He, S.; Wang, Z.; Zou, Y.; Chen, S.; Xu, X.

Process Biochem.

49

1107-1112

743978

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Inhibition of aromatic L-amino acid decarboxylase from Micrococcus percitreus by substrate analogs

1987

Nakazawa, H.

Agric. Biol. Chem.

51

2531-2537

756913

27816487

Arylalkylamine N-acetyltransferase 1 gene (TcAANAT1) is required for cuticle morphology and pigmentation of the adult red flour beetle, Tribolium castaneum

2016

Noh, M.Y.; Koo, B.; Kramer, K.J.; Muthukrishnan, S.; Arakane, Y.

Insect Biochem. Mol. Biol.

79

119-129

756959

31494163

The versatile O-methyltransferase LrOMT catalyzes multiple O-methylation reactions in amaryllidaceae alkaloids biosynthesis

2019

Li, W.; Qiao, C.; Pang, J.; Zhang, G.; Luo, Y.

Int. J. Biol. Macromol.

141

680-692

757560

31443750

Hypothesis Metabolic targeting of 5-aminolevulinate synthase by tryptophan and inhibitors of heme utilisation by tryptophan 2,3-dioxygenase as potential therapies of acute hepatic porphyrias

2019

Badawy, A.A.

Med. Hypotheses

131

109314

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