print visible entries

print all entries

Ligand anthraniloyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

tryptophan metabolism

KEGG

Aminobenzoate degradation, Biosynthesis of secondary metabolites, Biosynthesis of various antibiotics, Microbial metabolism in diverse environments, Phenazine biosynthesis

MetaCyc

2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis, 4-hydroxy-2(1H)-quinolone biosynthesis, anthranilate degradation II (aerobic), anthranilate degradation III (anaerobic), aurachin A, B, C and D biosynthesis, aurachin RE biosynthesis more

Show all BRENDA pathways known for anthraniloyl-CoA

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.40

2-aminobenzoyl-CoA + NAD(P)H + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+

438853, 438851

-

1.14.13.40

anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+

744409

-

1.14.13.40

2 entries

2.3.1.230

malonyl-CoA + 2-aminobenzoyl-CoA = 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2

721616, 722456, 721932, 722661, 722047

-

2.3.1.232

anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate

726171

-

3.1.2.23

2-aminobenzoyl-CoA + H2O = 2-aminobenzoate + CoA

690642

-

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

top print hide

Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA

0

-

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA

438854, 438855, 713, 438858, 0

-

6.2.1.32

2 entries

Substrate in Enzyme-catalyzed Reactions (20 results)

top print hide

Show Substrate (20 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.40

2-aminobenzoyl-CoA + NAD(P)H + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+

438851, 438854, 438853, 438852, 438858, 438856, 438857

-

1.14.13.40

anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+

744409

-

1.14.13.40

anthraniloyl-CoA + NADH + H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD+

438851, 438857

-

1.3.7.8

2-amino-benzoyl-CoA + reduced methyl viologen + ATP = 2-amino-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate

654733

-

1.3.7.8

2-aminobenzoyl-CoA + reduced methyl viologen + ATP = ?

12559

-

2.3.1.212

anthraniloyl-CoA + malonyl-CoA + H2O = 4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?

723330

-

2.3.1.212

anthraniloyl-CoA + methylmalonyl-CoA + H2O = ?

723330

-

2.3.1.230

3-oxodecanoate + 2-aminobenzoyl-CoA = CoA + 2-heptyl-4(1H)-quinolone + CO2 + H2O

722047, 722927

-

2.3.1.230

3-oxodecanoate + 2-aminobenzoyl-CoA = CoA + 2-heptyl-4-hydroxyquinoline + CO2 + H2O

721932

-

2.3.1.230

3-oxodecanoyl-CoA + 2-aminobenzoyl-CoA = 2 CoA + 2-heptyl-3-hydroxy-4(1H)-quinolone + CO2

722047

-

2.3.1.230

3-oxodecanoyl-N-acetylcysteamine + 2-aminobenzoyl-CoA = N-acetylcysteamine + 2-heptyl-3-hydroxy-4(1H)-quinolone + CO2

722047

-

2.3.1.230

3-oxohexanoate + 2-aminobenzoyl-CoA = CoA + 2-propyl-4(1H)-quinolone + CO2 + H2O

722047

-

2.3.1.230

3-oxopentanoate + 2-aminobenzoyl-CoA = CoA + 2-ethyl-4(1H)-quinolone + CO2 + H2O

722047

-

2.3.1.230

malonyl-CoA + 2-aminobenzoyl-CoA = 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2

722456, 721616, 721932, 722661, 722047

-

2.3.1.230

malonyl-[acyl-carrier protein] + 2-aminobenzoyl-CoA = CoA + acyl-carrier protein + 4-hydroxy-2(1H)-quinolone + CO2

722661

-

1.14.13.40

3 entries

1.3.7.8

2 entries

2.3.1.212

2 entries

2.3.1.230

8 entries

2.3.1.232

anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate

726171

-

2.3.1.262

anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA

736669

-

2.3.1.262

anthraniloyl-CoA + malonyl-CoA = 2,4-dihydroxyquinoline + 2 CoA + CO2 + ?

721616

-

2.3.1.262

anthraniloyl-CoA + malonyl-CoA = 2-aminobenzoylacetyl-CoA + CoA + CO2

757068, 735925

-

2.3.1.262

3 entries

3.1.2.23

2-aminobenzoyl-CoA + H2O = 2-aminobenzoate + CoA

690642

-

Product in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.2.1.2

ATP + 2-aminobenzoate + CoA = AMP + diphosphate + 2-aminobenzoyl-CoA

650334

-

6.2.1.25

ATP + 2-aminobenzoate + CoA = AMP + diphosphate + 2-aminobenzoyl-CoA

0, 651721, 649526

-

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA

0

-

6.2.1.32

ATP + anthranilate + CoA = AMP + diphosphate + anthranilyl-CoA

0, 438854, 438855, 713, 438858

-

6.2.1.32

ATP + CoA + anthranilate = AMP + diphosphate + anthranilyl-CoA

713, 438854, 438858, 438855

-

6.2.1.32

3 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

top print hide

Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.40

substrate inhibition above 0.15 mM

438851

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.1.180

3h77, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (5 results)

top print hide

Show Turnover Number (5 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.13.40

70.8

-

-

438851

2.3.1.230

0.0165

-

pH 7, 37°C

721932

2.3.1.232

0.01

-

pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme

726171

2.3.1.232

0.022

-

pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme

726171

2.3.1.232

2 entries

2.3.1.262

0.3

-

pH 7.5, 37°C

721616

K_M Value (8 results)

top print hide

Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.40

0.02

-

value below, cell extract

438858

1.14.13.40

0.025

-

value below

438851

1.14.13.40

2 entries

1.3.7.8

0.019

-

-

654733

2.3.1.230

0.035

-

pH 7.5, 37°C

722661

2.3.1.230

0.599

-

pH and temperature not specified in the publication

722047

2.3.1.230

0.875

-

pH 7, 37°C

721932

2.3.1.232

0.00251

-

pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme

726171

2.3.1.232

0.00478

-

pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme

726171

2.3.1.230

3 entries

2.3.1.232

2 entries

References & Links

Literature References (27)

top print hide

Show Reference (27 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

713

1885526

Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligase from a denitrifying Pseudomonas sp.

1991

Altenschmidt, U.; Oswald, B.; Fuchs, G.

J. Bacteriol.

173

5494-5501

12559

8575453

Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thaurea aromatica strain K172

1995

Boll, M.; Fuchs, G.

Eur. J. Biochem.

234

921-933

438851

2591379

2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme

1989

Buder, R.; Fuchs, G.

Eur. J. Biochem.

185

629-635

438852

2591380

2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Studies on the stoichiometry and the course of the reaction

1989

Buder, R.; Ziegler, K.; Fuchs, G.; Langkau, B.; Ghisla, S.

Eur. J. Biochem.

185

637-643

438853

2384085

2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Identification of the reaction products

1990

Langkau, B.; Ghisla, S.; Buder, R.; Ziegler, K.; Fuchs, G.

Eur. J. Biochem.

191

365-371

438854

2176602

Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid

1990

Altenschmidt, U.; Eckerskorn, C.; Fuchs, G.

Eur. J. Biochem.

194

647-653

438855

11514509

Two similar gene clusters coding for enzymes of a new type of aerobic 2-aminobenzoate (anthranilate) metabolism in the bacterium Azoarcus evansii

2001

Schuhle, K.; Jahn, M.; Ghisla, S.; Fuchs, G.

J. Bacteriol.

183

5268-5278

438856

10611284

Theoretical investigation of the [1,2]-sigmatropic hydrogen migration in the mechanism of oxidation of 2-aminobenzoyl-CoA by 2-aminobenzoyl-CoA monooxygenase/reductase

1999

Torres, R.A.; Bruice, T.C.

Proc. Natl. Acad. Sci. USA

96

14748-14752

438857

7607242

2-Aminobenzoyl-CoA monooxygenase/reductase. Evidence for two distinct loci catalyzing substrate monooxygenation and hydrogenation

1995

Langkau, B.; Vock, P.; Massey, V.; Fuchs, G.; Ghisla, S.

Eur. J. Biochem.

230

676-685

438858

1592816

Anaerobic degradation of 2-aminobenzoic acid (anthranilic acid) via benzoyl-coenzyme A (CoA) and cyclohex-1-enecarboxyl-CoA in a denitrifying bacterium

1992

Lochmeyer, C.; Koch, J.; Fuchs, G.

J. Bacteriol.

174

3621-3628

649526

12054436

Purification and characterization of benzoate:coenzyme A ligase from Clarkia breweri

2002

Beuerle, T.; Pichersky, E.

ARCH. BIOCHEM. BIOPHYS.

400

258-264

650334

11690636

The macrophage-induced gene (mig) of Mycobacterium avium encodes a medium-chain acyl-coenzyme A synthetase

2001

Morsczeck, C.; Berger, S.; Plum, G.

Biochim. Biophys. Acta

1521

59-65

651721

12897012

Benzoate-coenzyme A ligase from Thauera aromatica: an enzyme acting in anaerobic and aerobic pathways

2003

Schuhle, K.; Gescher, J.; Feil, U.; Paul, M.; Jahn, M.; Schagger, H.; Fuchs, G.

J. Bacteriol.

185

4920-4929

654733

14756575

Substrate binding and reduction of benzoyl-CoA reductase: evidence for nucleotide-dependent conformational changes

2004

Mobitz, H.; Friedrich, T.; Boll, M.

Biochemistry

43

1376-1385

690642

18542924

Benzoyl-coenzyme A thioesterase of Azoarcus evansii: properties and function

2008

Ismail, W.

Arch. Microbiol.

190

451-460

721616

19694421

Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate

2009

Bera, A.K.; Atanasova, V.; Robinson, H.; Eisenstein, E.; Coleman, J.P.; Pesci, E.C.; Parsons, J.F.

Biochemistry

48

8644-8655

721932

23916145

Molecular basis of HHQ biosynthesis: molecular dynamics simulations, enzyme kinetic and surface plasmon resonance studies

2013

Steinbach, A.; Maurer, C.K.; Weidel, E.; Henn, C.; Brengel, C.; Hartmann, R.W.; Negri, M.

BMC Biophys.

6

10

722047

21425231

Biosynthesis of 2-Alkyl-4(1H)-quinolones in Pseudomonas aeruginosa: potential for therapeutic interference with pathogenicity

2011

Pistorius, D.; Ullrich, A.; Lucas, S.; Hartmann, R.W.; Kazmaier, U.; Müller, R.

Chembiochem

12

850-853

722456

22992202

Validation of PqsD as an anti-biofilm target in Pseudomonas aeruginosa by development of small-molecule inhibitors

2012

Storz, M.P.; Maurer, C.K.; Zimmer, C.; Wagner, N.; Brengel, C.; de Jong, J.C.; Lucas, S.; Müsken, M.; Häussler, S.; Steinbach, A.; Hartmann, R.W.

J. Am. Chem. Soc.

134

16143-16146

722661

18728009

PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by Pseudomonas aeruginosa

2008

Zhang, Y.M.; Frank, M.W.; Zhu, K.; Mayasundari, A.; Rock, C.O.

J. Biol. Chem.

283

28788-28794

722927

23834469

Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking

2013

Weidel, E.; de Jong, J.C.; Brengel, C.; Storz, M.P., Braunshausen, A.; Negri, M.; Plaza, A.; Steinbach, A.; Müller, R.; Hartmann, R.W.

J. Med. Chem.

56

6146-6155

723330

17165930

Enzymatic formation of quinolone alkaloids by a plant type III polyketide synthase

2006

Abe, I.; Abe, T.; Wanibuchi, K.; Noguchi, H.

Org. Lett.

8

6063-6065

726171

16262710

The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate

2005

Wang, J.; De Luca, V.

Plant J.

44

606-619

735925

24239007

The end of an old hypothesis: the Pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids

2013

Dulcey, C.E.; Dekimpe, V.; Fauvelle, D.A.; Milot, S.; Groleau, M.C.; Doucet, N.; Rahme, L.G.; Lepine, F.; Deziel, E.

Chem. Biol.

20

1481-1491

736669

24842325

Mechanistic details for anthraniloyl transfer in PqsD: the initial step in HHQ biosynthesis

2014

Hutter, M.C.; Brengel, C.; Negri, M.; Henn, C.; Zimmer, C.; Hartmann, R.W.; Empting, M.; Steinbach, A.

J. Mol. Model.

20

2255

744409

25843773

Anthranoyl-CoA monooxygenase/reductase from Azoarcus evansii possesses both FMN and FAD in two distinct and independent active sites

2015

Bergner, T.; Pavkov-Keller, T.; Kreuzer, K.; Kowaliuk, J.; Plank, M.; Runggatscher, K.; Turrini, N.G.; Zucol, B.; Wallner, S.; Faber, K.; Gruber, K.; Macheroux, P.

Biochim. Biophys. Acta

1854

890-896

757068

30336005

Competitive live-cell profiling strategy for discovering inhibitors of the quinolone biosynthesis of Pseudomonas aeruginosa

2018

Prothiwa, M.; Englmaier, F.; Boettcher, T.

J. Am. Chem. Soc.

140

14019-14023

Links to other databases for anthraniloyl-CoA

top print hide

Show Links (1 entry)

ChEBI

PubChem