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Ligand mesalamine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.86

5-aminosalicylate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate

747014, 748114

-

2.3.1.5

acetyl-CoA + 5-aminosalicylic acid = CoA + 5-acetylaminosalicylic acid

674321

-

Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Substrate (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.7

5-aminosalicylic acid + H2O2 = ? + H2O

658137

-

1.13.11.4

5-aminosalicylate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate

748157

-

1.13.11.4

5-aminosalicylate + O2 = ?

672692, 698560, 724975, 743728

-

1.13.11.4

2 entries

1.13.11.86

5-aminosalicylate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate

747014, 748114

-

1.14.13.1

5-aminosalicylate + NADH + 2 H+ + O2 = 5-aminocatechol + NAD+ + H2O + CO2

764872

-

1.14.13.1

5-aminosalicylate + NADH + H+ + O2 = 5-aminobenzene-1,2-diol + NAD+ + H2O + CO2

741666

-

1.14.13.1

5-aminosalicylate + NADH + O2 = 5-aminocatechol + CO2 + NAD+ + H2O

439423

-

1.14.13.1

3 entries

2.3.1.331

acetyl-CoA + 5-aminosalicylic acid = ?

776852

-

2.3.1.5

acetyl-CoA + 5-aminosalicylate = ?

688423, 689354

-

2.3.1.5

acetyl-CoA + 5-aminosalicylate = CoA + 5-acetylamino-2-hydroxybenzoate

658261, 689354

-

2.3.1.5

acetyl-CoA + 5-aminosalicylate = CoA + N-acetyl-5-aminosalicylate

657856, 688393, 688423, 685166, 689354, 735366, 735860, 758541, 777308

-

2.3.1.5

malonyl-CoA + 5-aminosalicylate = CoA + N-malonyl-5-aminosalicylate

758541, 777308

-

2.3.1.5

propionyl-CoA + 5-aminosalicylate = CoA + N-propionyl-5-aminosalicylate

758541, 777308

-

2.3.1.5

succinyl-CoA + 5-aminosalicylate = CoA + N-succinyl-5-aminosalicylate

758541

-

2.3.1.5

4-nitrophenyl acetate + 5-aminosalicylic acid = 4-nitrophenol + 5-acetylaminosalicylic acid

675802

-

2.3.1.5

4-nitrophenyl acetate + 5-aminosalicylic acid = 4-nitrophenol + N-acetyl-5-aminosalicylic acid

672795

-

2.3.1.5

acetyl-CoA + 5-aminosalicylic acid = CoA + 5-acetylamino-2-hydroxybenzoate

487132, 657856, 657884

-

2.3.1.5

acetyl-CoA + 5-aminosalicylic acid = CoA + 5-acetylaminosalicylic acid

674321, 675599, 675802, 672795

-

2.3.1.5

acetyl-CoA + 5-aminosalicylic acid = CoA + N-acetyl-5-aminosalicylic acid

661996, 672795, 687848, 685029, 706607

-

2.3.1.5

p-nitrophenyl acetate + 5-aminosalicylic acid = p-nitrophenol + 5-acetylaminosalicylic acid

672795

-

2.3.1.5

p-nitrophenylacetate + 5-aminosalicylic acid = 4-nitrophenol + N-acetyl-5-aminosalicylate

672795

-

2.3.1.5

13 entries

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.11.2.2

converts inactive myeloperoxidase compound II rapidly into active myeloperoxidase

711274

-

1.14.14.18

induces HO-1 expression in the colon and stimulates its catalytic activity

686565

-

Inhibitor in Enzyme-catalyzed Reactions (11 results)

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Show Inhibitors (11 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.153

-

761589

-

1.11.2.2

-

765512

-

1.14.14.94

50% inhibition at 0.05 mM

390072

-

2.1.1.67

-

485524

-

2.1.1.67

-

703355

-

2.1.1.67

-

686275, 690115

-

2.1.1.67

thiopurine S-methyltransferase inhibition of multimatrix mesalazine is lower than that of time-dependent mesalazine

778204

-

2.1.1.67

4 entries

2.3.1.5

substrate inhibition; substrate inhibition through 5-aminosalicylic acid in which the substrate binds both to the free form of the enzyme and the acetyl coenzyme A-enzyme complex; substrate inhibition, in which the substrate binds both to the free form of the enzyme and the acetyl coenzyme A-enzyme complex in non-productive reaction pathways

672795

-

2.7.11.10

weak inhibition of IKK-2

661547

-

3.1.3.16

1 mg/ml efficiently inhibits PP2A

679065

-

3.5.3.15

-

685554

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.4

2.8

-

wild-type enzyme, pH and temperature not specified in the publication

724975

1.13.11.4

59

-

-

698560

1.13.11.4

59.3

-

pH 8.0, temperature not specified in the publication

748157

2.3.1.5

0.0017

-

wild-type, pH 8.0, 28°C

706607

2.3.1.5

0.044

-

-

658261

2.3.1.5

1.8

-

chimeric enzyme, replacement of the third domain of Mycobacterium marinum enzyme with that from Mycobacterium tuberculosis, pH 8.0, 28°C

706607

2.3.1.5

1.8

-

chimeric enzyme, replacement of the third domain of Mycobacterium tuberculosis enzyme with that from Mycobacterium marinum, pH 8.0, 28°C

706607

2.3.1.5

5.2

-

wild-type, pH 8.0, 28°C

706607

2.3.1.5

47

-

apparent value, at pH 7.5 and 37°C

735366

2.3.1.5

434

-

-

672795

1.13.11.4

3 entries

2.3.1.5

7 entries

K_M Value (28 results)

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Show KM Value (28 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.4

0.216

-

wild-type enzyme, pH and temperature not specified in the publication

724975

1.13.11.4

2.7

-

at pH 8.0 and 25°C

743728

1.13.11.4

3.1

-

-

698560

1.13.11.4

3.1

-

pH 8.0, temperature not specified in the publication

748157

1.13.11.4

4 entries

1.13.11.86

0.052

-

pH 8.0, 25°C, wild-type enzyme

748114

2.3.1.5

0.0067

-

isoform NAT 1, pH 7.4, 37°C

661996

2.3.1.5

0.026

-

pH 7.4, 37°C

661996

2.3.1.5

0.061

-

pH 7.4, 37°C

661996

2.3.1.5

0.112

-

pH 7.4, 37°C

661996

2.3.1.5

0.117

-

strain 54.8, pH 7.4, 37°C

661996

2.3.1.5

0.158

-

pH 7.4, 37°C

661996

2.3.1.5

0.184

-

isoform NAT 2, pH 7.4, 37°C

661996

2.3.1.5

0.2

-

-

688393

2.3.1.5

0.208

-

strain 60.62, pH 7.4, 37°C

661996

2.3.1.5

0.21

-

pH 7.4, 37°C

661996

2.3.1.5

0.219

-

-

672795

2.3.1.5

0.228

-

apparent KM

685166

2.3.1.5

0.228

-

isoenzyme BanatC

685166

2.3.1.5

0.25

-

-

658261

2.3.1.5

0.347

-

pH 7.4, 37°C

661996

2.3.1.5

0.622

-

apparent KM

685166

2.3.1.5

0.622

-

isoenzyme BanatB

685166

2.3.1.5

0.662

-

apparent value, at pH 7.5 and 37°C

735366

2.3.1.5

1

-

wild-type, pH 8.0, 28°C

706607

2.3.1.5

1.02

-

-

672795

2.3.1.5

1.2

-

chimeric enzyme, replacement of the third domain of Mycobacterium marinum enzyme with that from Mycobacterium tuberculosis, pH 8.0, 28°C

706607

2.3.1.5

1.2

-

chimeric enzyme, replacement of the third domain of Mycobacterium tuberculosis enzyme with that from Mycobacterium marinum, pH 8.0, 28°C

706607

2.3.1.5

1.7

-

wild-type, pH 8.0, 28°C

706607

2.3.1.5

23 entries

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.1.1.153

0.00037

-

pH and temperature not specified in the publication

761589

3.5.3.15

10

-

above, pH 7.6, 37°C, recombinant PAD4

685554

References & Links

Literature References (53)

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Show Reference (53 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

390072

7938083

5-Aminosalicylic acid inhibits leukotriene B4 omega-hydroxylase activity in human polymorphonuclear leukocytes

1994

Ikehata, A.; Hiwatashi, N.; Kinouchi, Y.; Ito, K.; Yamazaki, H.; Toyota, T.

Prostaglandins Leukot. Essent. Fatty Acids

50

317-320

439423

6539772

Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum

1984

Sze, I.S.Y.; Dagley, S.

J. Bacteriol.

159

353-359

485524

8866635

Inhibition of human thiopurine methyltransferase by furosemide, bendroflumethiazide and trichlormethiazide

1996

Lysaa, R.A.; Giverhaug, T.; Wold, H.L.; Aarbakke, J.

Eur. J. Clin. Pharmacol.

49

393-396

487132

2924904

Evidence for two closely related isozymes of arylamine N-acetyltransferase in human liver

1989

Grant, D.M.; Lottspeich, F.; Meyer, U.A.

FEBS Lett.

244

203-207

657856

15447630

Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase

2005

Westwood, I.M.; Holton, S.J.; Rodrigues-Lima, F.; Dupret, J.M.; Bhakta, S.; Noble, M.E.; Sim, E.

Biochem. J.

385

605-612

657884

15627487

Eukaryotic arylamine N-acetyltransferase. Investigation of substrate specificity by high-throughput screening

2005

Kawamura, A.; Graham, J.; Mushtaq, A.; Tsiftsoglou, S.A.; Vath, G.M.; Hanna, P.E.; Wagner, C.R.; Sim, E.

Biochem. Pharmacol.

69

347-359

658137

12693977

Activation of peroxidase-catalyzed oxidation of aromatic amines with 2-aminothiazole and melamine

2003

Karasyova, E.I.; Naumchik, I.V.; Metelitza, D.I.

Biochemistry

68

54-62

658261

12628650

An approach to identifying novel substrates of bacterial arylamine N-acetyltransferases

2003

Brooke, E.W.; Davies, S.G.; Mulvaney, A.W.; Pompeo, F.; Sim, E.; Vickers, R.J.

Bioorg. Med. Chem.

11

1227-1234

661547

14579522

Targeting IkB kinase for the treatment of inflammatory and other disorders

2003

Burke, J.R.

Curr. Opin. Drug Discov. Devel.

6

720-728

661996

11344150

Identification and functional characterization of arylamine N-acetyltransferases in eubacteria: evidence for highly selective acetylation of 5-aminosalicylic acid

2001

Delomenie, C.; Fouix, S.; Longuemaux, S.; Brahimi, N.; Bizet, C.; Picard, B.; Denamur, E.; Dupret, J.M.

J. Bacteriol.

183

3417-3427

672692

17213679

Gentisate 1,2-dioxygenase from Xanthobacter polyaromaticivorans 127W

2007

Hirano, S.; Morikawa, M.; Takano, K.; Imanaka, T.; Kanaya, S.

Biosci. Biotechnol. Biochem.

71

192-199

672795

17374145

Kinetic characterization of arylamine N-acetyltransferase from Pseudomonas aeruginosa

2007

Westwood, I.M.; Sim, E.

BMC Biochem.

8

3

674321

17158669

Arylamine N-acetyltransferase responsible for acetylation of 2-aminophenols in Streptomyces griseus

2007

Suzuki, H.; Ohnishi, Y.; Horinouchi, S.

J. Bacteriol.

189

2155-2159

675599

16829624

Identification and characterization of functional rat arylamine N-acetyltransferase 3: comparisons with rat arylamine N-acetyltransferases 1 and 2

2006

Walraven, J.M.; Doll, M.A.; Hein, D.W.

J. Pharmacol. Exp. Ther.

319

369-375

675802

16399351

Inactivation of human arylamine N-acetyltransferase 1 by hydrogen peroxide and peroxynitrite

2005

Dupret, J.M.; Dairou, J.; Atmane, N.; Rodrigues-Lima, F.

Methods Enzymol.

400

215-229

679065

16728434

Protein phosphatase 2A is required for mesalazine-dependent inhibition of Wnt/beta-catenin pathway activity

2006

Bos, C.L.; Diks, S.H.; Hardwick, J.C.; Walburg, K.V.; Peppelenbosch, M.P.; Richel, D.J.

Carcinogenesis

27

2371-2382

685029

18280460

Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1

2008

Kawamura, A.; Westwood, I.; Wakefield, L.; Long, H.; Zhang, N.; Walters, K.; Redfield, C.; Sim, E.

Biochem. Pharmacol.

75

1550-1560

685166

17511472

Cloning and molecular characterization of three arylamine N-acetyltransferase genes from Bacillus anthracis: identification of unusual enzymatic properties and their contribution to sulfamethoxazole resistance

2007

Pluvinage, B.; Dairou, J.; Possot, O.M.; Martins, M.; Fouet, A.; Dupret, J.M.; Rodrigues-Lima, F.

Biochemistry

46

7069-7078

685554

17964793

Profiling protein arginine deiminase 4 (PAD4): a novel screen to identify PAD4 inhibitors

2008

Knuckley, B.; Luo, Y.; Thompson, P.R.

Bioorg. Med. Chem.

16

739-745

686275

-

Clinical significance of thiopurine S-methyltransferase gene polymorphisms

2007

Zhou, S.; Chowbay, B.

Curr. Pharmacogenomics

5

103-115

686565

18215658

The involvement of heme oxygenase-1 activity in the therapeutic actions of 5-aminosalicylic acid in rat colitis

2008

Horvath, K.; Varga, C.; Berko, A.; Posa, A.; Laszlo, F.; Whittle, B.J.

Eur. J. Pharmacol.

581

315-323

687848

17368397

Bacillus cereus strain 10-L-2 produces two arylamine N-acetyltransferases that transform 4-phenylenediamine into 4-aminoacetanilide

2007

Mulyono, R.; Takenaka, S.; Sasano, Y.; Murakami, S.; Aoki, K.

J. Biosci. Bioeng.

103

147-154

688393

18005984

Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase

2008

Fullam, E.; Westwood, I.M.; Anderton, M.C.; Lowe, E.D.; Sim, E.; Noble, M.E.

J. Mol. Biol.

375

178-191

688423

18778714

Functional and structural characterization of the arylamine N-acetyltransferase from the opportunistic pathogen Nocardia farcinica

2008

Martins, M.; Pluvinage, B.; de la Sierra-Gallay, I.L.; Barbault, F.; Dairou, J.; Dupret, J.M.; Rodrigues-Lima, F.

J. Mol. Biol.

383

549-560

689354

17460546

Description of a novel polymorphic gene encoding for arylamine N-acetyltransferase in the rhesus macaque (Macaca mulatta), a model animal for endometriosis

2007

Fakis, G.; Boukouvala, S.; Kawamura, A.; Kennedy, S.

Pharmacogenet. Genomics

17

181-188

690115

17304143

Monitoring of thiopurine methyltransferase activity in postsurgical patients with Crohns disease during 1 year of treatment with azathioprine or mesalazine

2007

Dilger, K.; Schaeffeler, E.; Lukas, M.; Strauch, U.; Herfarth, H.; Mueller, R.; Schwab, M.

Ther. Drug Monit.

29

1-5

698560

11698383

Direct ring fission of salicylate by a salicylate 1,2-dioxygenase activity from Pseudaminobacter salicylatoxidans

2001

Hintner, J.P.; Lechner, C.; Riegert, U.; Kuhm, A.E.; Storm, T.; Reemtsma, T.; Stolz, A.

J. Bacteriol.

183

6936-6942

703355

-

Role of monitoring thiopurine methyltransferase (TPMT) activity in the individualized therapy with azathioprine or 6-mercaptopurine

2008

Gisbert, J.

Curr. Pharmacogenomics Person. Med.

6

33-44

706607

19636684

Comparison of the arylamine N-acetyltransferase from Mycobacterium marinum and Mycobacterium tuberculosis

2009

Fullam, E.; Kawamura, A.; Wilkinson, H.; Abuhammad, A.; Westwood, I.; Sim, E.

Protein J.

28

281-293

711274

2155024

The chlorinating activity of human myeloperoxidase: high initial activity at neutral pH value and activation by electron donors

1990

Zuurbier, K.W.; Bakkenist, A.R.; Wever, R.; Muijsers, A.O.

Biochim. Biophys. Acta

1037

140-146

724975

23384287

The salicylate 1,2-dioxygenase as a model for a conventional gentisate 1,2-dioxygenase: crystal structures of the G106A mutant and its adducts with gentisate and salicylate

2013

Ferraroni, M.; Matera, I.; Buerger, S.; Reichert, S.; Steimer, L.; Scozzafava, A.; Stolz, A.; Briganti, F.

FEBS J.

280

1643-1652

735366

25372695

Structural and functional characterization of an arylamine N-acetyltransferase from the pathogen Mycobacterium abscessus: differences from other mycobacterial isoforms and implications for selective inhibition

2014

Cocaign, A.; Kubiak, X.; Xu, X.; Garnier, G.; Li de la Sierra-Gallay, I.; Chi-Bui, L.; Dairou, J.; Busi, F.; Abuhammad, A.; Haouz, A.; Dupret, J.M.; Herrmann, J.L.; Rodrigues-Lima, F.

Acta Crystallogr. Sect. D

70

3066-3079

735860

25432241

Differences between murine arylamine N-acetyltransferase type 1 and human arylamine N-acetyltransferase type 2 defined by substrate specificity and inhibitor binding

2014

Laurieri, N.; Kawamura, A.; Westwood, I.M.; Varney, A.; Morris, E.; Russell, A.J.; Stanley, L.A.; Sim, E.

BMC Pharmacol. Toxicol.

15

68

741666

26027357

Properties of non-homologous salicylate hydroxylases of Pseudomonas bacteria

2015

Puntus, I.; Vlasova, E.; Sokolov, A.; Zakharchenko, N.; Funtikova, T.

Appl. Biochem. Microbiol.

51

215-221

741666

26027357

Properties of non-homologous salicylate hydroxylases of Pseudomonas bacteria

2015

Puntus, I.; Vlasova, E.; Sokolov, A.; Zakharchenko, N.; Funtikova, T.

Appl. Biochem. Microbiol.

51

215-221

743728

27887027

Expansion of the substrate range of the gentisate 1,2-dioxygenase from Corynebacterium glutamicum for the conversion of monohydroxylated benzoates

2017

Eppinger, E.; Stolz, A.

Protein Eng. Des. Sel.

30

57-65

743728

27887027

Expansion of the substrate range of the gentisate 1,2-dioxygenase from Corynebacterium glutamicum for the conversion of monohydroxylated benzoates

2017

Eppinger, E.; Stolz, A.

Protein Eng. Des. Sel.

30

57-65

747014

1554350

Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage

1992

Stolz, A.; Noertemann, B.; Knackmuss, H.J.

Biochem. J.

282

675-680

747014

1554350

Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage

1992

Stolz, A.; Noertemann, B.; Knackmuss, H.J.

Biochem. J.

282

675-680

748114

29038259

Novel Gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme

2018

Yu, H.; Zhao, S.; Guo, L.

J. Bacteriol.

200

e00395-17

748114

29038259

Novel Gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme

2018

Yu, H.; Zhao, S.; Guo, L.

J. Bacteriol.

200

e00395-17

748157

15220336

Biochemical and molecular characterization of a ring fission dioxygenase with the ability to oxidize (substituted) salicylate(s) from Pseudaminobacter salicylatoxidans

2004

Hintner, J.P.; Reemtsma, T.; Stolz, A.

J. Biol. Chem.

279

37250-37260

748157

15220336

Biochemical and molecular characterization of a ring fission dioxygenase with the ability to oxidize (substituted) salicylate(s) from Pseudaminobacter salicylatoxidans

2004

Hintner, J.P.; Reemtsma, T.; Stolz, A.

J. Biol. Chem.

279

37250-37260

758541

31673919

The actinobacterium Tsukamurella paurometabola has a functionally divergent arylamine N-acetyltransferase (NAT) homolog

2019

Garefalaki, V.; Kontomina, E.; Ioannidis, C.; Savvidou, O.; Vagena-Pantoula, C.; Papavergi, M.G.; Olbasalis, I.; Patriarcheas, D.; Fylaktakidou, K.C.; Felfoeldi, T.; Marialigeti, K.; Fakis, G.; Boukouvala, S.

World J. Microbiol. Biotechnol.

35

174

758541

31673919

The actinobacterium Tsukamurella paurometabola has a functionally divergent arylamine N-acetyltransferase (NAT) homolog

2019

Garefalaki, V.; Kontomina, E.; Ioannidis, C.; Savvidou, O.; Vagena-Pantoula, C.; Papavergi, M.G.; Olbasalis, I.; Patriarcheas, D.; Fylaktakidou, K.C.; Felfoeldi, T.; Marialigeti, K.; Fakis, G.; Boukouvala, S.

World J. Microbiol. Biotechnol.

35

174

741666

2 entries

743728

2 entries

747014

2 entries

748114

2 entries

748157

2 entries

758541

2 entries

761589

32734666

Sepiapterin reductase Characteristics and role in diseases

2020

Wu, Y.; Chen, P.; Sun, L.; Yuan, S.; Cheng, Z.; Lu, L.; Du, H.; Zhan, M.

J. Cell. Mol. Med.

24

9495-9506

764872

30703421

Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase

2019

Costa, D.M.A.; Gomez, S.V.; de Araujo, S.S.; Pereira, M.S.; Alves, R.B.; Favaro, D.C.; Hengge, A.C.; Nagem, R.A.P.; Brandao, T.A.S.

Int. J. Biol. Macromol.

129

588-600

764872

30703421

Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase

2019

Costa, D.M.A.; Gomez, S.V.; de Araujo, S.S.; Pereira, M.S.; Alves, R.B.; Favaro, D.C.; Hengge, A.C.; Nagem, R.A.P.; Brandao, T.A.S.

Int. J. Biol. Macromol.

129

588-600

765512

34071735

Myeloperoxidase inhibitory and antioxidant activities of (E)-2-hydroxy-alpha-aminocinnamic acids obtained through microwave-assisted synthesis

2021

Rivera-Antonio, A.; Rosales-Hernandez, M.C.; Balbuena-Rebolledo, I.; Santiago-Quintana, J.M.; Mendieta-Wejebe, J.E.; Correa-Basurto, J.; Garcia-Vazquez, J.B.; Garcia-Baez, E.V.; Padilla-Martinez, I.I.

Pharmaceuticals

14

513

765512

34071735

Myeloperoxidase inhibitory and antioxidant activities of (E)-2-hydroxy-alpha-aminocinnamic acids obtained through microwave-assisted synthesis

2021

Rivera-Antonio, A.; Rosales-Hernandez, M.C.; Balbuena-Rebolledo, I.; Santiago-Quintana, J.M.; Mendieta-Wejebe, J.E.; Correa-Basurto, J.; Garcia-Vazquez, J.B.; Garcia-Baez, E.V.; Padilla-Martinez, I.I.

Pharmaceuticals

14

513

764872

2 entries

765512

2 entries

776852

23479412

Enantioselective N-acetylation of 2-phenylglycine by an unusual N-acetyltransferase from Chryseobacterium sp.

2013

Takenaka, S.; Honma, Y.; Yoshida, K.; Yoshida, K.

Biotechnol. Lett.

35

1053-1059

777308

36178468

Fusarium verticillioides NAT1 (FDB2) N-malonyltransferase is structurally, functionally and phylogenetically distinct from its N-acetyltransferase (NAT) homologues

2023

Karagianni, E.P.; Kontomina, E.; Lowe, E.D.; Athanasopoulos, K.; Papanikolaou, G.; Garefalaki, V.; Kotseli, V.; Zaliou, S.; Grimaud, T.; Arvaniti, K.; Tsatiri, M.A.; Fakis, G.; Glenn, A.E.; Roversi, P.; Abuhammad, A.; Ryan, A.; Sim, R.B.; Sim, E.; Boukouvala, S.

FEBS J.

290

2412-2436

778204

33470487

Differential effects of mesalazine formulations on thiopurine metabolism through thiopurine S-methyltransferase inhibition

2021

Morikubo, H.; Kobayashi, T.; Ozaki, R.; Okabayashi, S.; Kuronuma, S.; Takeuchi, O.; Shiba, T.; Kiyohara, H.; Matsubayashi, M.; Sagami, S.; Nakano, M.; Ikezaki, O.; Hisamatsu, T.; Tanaka, Y.; Hibi, T.

J. Gastroenterol. Hepatol.

36

2116-2124

Links to other databases for mesalamine

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