| EC |
1.14.13.40 |
| Accepted name: |
anthraniloyl-CoA monooxygenase |
| Reaction: |
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+ |
| Glossary: |
anthraniloyl-CoA = 2-aminobenzoyl-CoA |
| Other name(s): |
anthraniloyl coenzyme A reductase; 2-aminobenzoyl-CoA monooxygenase/reductase |
| Systematic name: |
anthraniloyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing) |
| Comments: |
A flavoprotein (FAD). The non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexanedione. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 112692-57-6 |
| References: |
| 1. |
Buder, R. and Fuchs, G. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme. Eur. J. Biochem. 185 (1989) 629–635. [DOI] [PMID: 2591379] |
| 2. |
Buder, R., Ziegler, K., Fuchs, G., Langkau, B. and Ghisla, S. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Studies on the stoichiometry and the course of the reaction. Eur. J. Biochem. 185 (1989) 637–643. [DOI] [PMID: 2591380] |
| 3. |
Langkau, B., Ghisla, S., Buder, R., Ziegler, K. and Fuchs, G. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Identification of the reaction products. Eur. J. Biochem. 191 (1990) 365–371. [DOI] [PMID: 2384085] |
|
| [EC 1.14.13.40 created 1992] |
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| EC |
2.3.1.159 |
| Accepted name: |
acridone synthase |
| Reaction: |
3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2 |
|
For diagram of acridone alkaloid biosynthesis, click here |
| Systematic name: |
malonyl-CoA:N-methylanthraniloyl-CoA malonyltransferase (cyclizing) |
| Comments: |
Belongs to a superfamily of plant polyketide synthases. Has many similarities to chalcone and stilbene synthases (see reaction synthesis) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99085-53-7 |
| References: |
| 1. |
Baumert, A., Maier, W., Gröger, D. and Deutzmann, R. Purification and properties of acridone synthase from cell suspension cultures of Ruta graveolens L. Z. Naturforsch. C: Biosci. 49 (1994) 26–32. [PMID: 8148006] |
| 2. |
Maier, W., Baumert, A., Schumann, B., Furukawa, H. and Gröger, D. Synthesis of 1,3-dihydroxy-N-methylacridone and its conversion to rutacridone by cell-free extracts of Ruta-graveolens cell cultures. Phytochemistry 32 (1993) 691–698. |
| 3. |
Lukačin, R., Springob, K., Urbanke, C., Ernwein, C., Schroder, G., Schroder, J. and Matern, U. Native acridone synthases I and II from Ruta graveolens L. form homodimers. FEBS Lett. 448 (1999) 135–140. [DOI] [PMID: 10217426] |
| 4. |
Junghanns, K.T., Kneusel, R.E., Groger, D. and Matern, U. Differential regulation and distribution of acridone synthase in Ruta graveolens. Phytochemistry 49 (1998) 403–411. [DOI] [PMID: 9747538] |
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| [EC 2.3.1.159 created 2002] |
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| EC |
2.3.1.230 |
| Accepted name: |
2-heptyl-4(1H)-quinolone synthase |
| Reaction: |
octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O (overall reaction)
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O
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| Glossary: |
2-heptyl-4-quinolone = 2-heptylquinolin-4(1H)-one |
| Other name(s): |
pqsBC (gene names); malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating) |
| Systematic name: |
octanoyl-CoA:(2-aminobenzoyl)acetate octanoyltransferase |
| Comments: |
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481–1491. [DOI] [PMID: 24239007] |
| 2. |
Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. and Fetzner, S. PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291 (2016) 6610–6624. [DOI] [PMID: 26811339] |
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| [EC 2.3.1.230 created 2013, modified 2017] |
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| EC |
2.3.1.232 |
| Accepted name: |
methanol O-anthraniloyltransferase |
| Reaction: |
anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate |
| Glossary: |
anthraniloyl-CoA = 2-aminobenzoyl-CoA |
| Other name(s): |
AMAT; anthraniloyl-coenzyme A (CoA):methanol acyltransferase |
| Systematic name: |
anthraniloyl-CoA:methanol O-anthraniloyltransferase |
| Comments: |
The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes. Also catalyses EC 2.3.1.196, benzyl alcohol O-benzoyltransferase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Wang, J. and De Luca, V. The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate. Plant J. 44 (2005) 606–619. [DOI] [PMID: 16262710] |
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| [EC 2.3.1.232 created 2014] |
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| EC |
2.3.1.262 |
| Accepted name: |
anthraniloyl-CoA anthraniloyltransferase |
| Reaction: |
anthraniloyl-CoA + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CoA + CO2 (overall reaction)
(1a) anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
(1b) S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CO2 + L-cysteinyl-[PqsD protein] |
| Glossary: |
anthraniloyl-CoA = 2-aminobenzoyl-CoA |
| Other name(s): |
pqsD (gene name) |
| Systematic name: |
anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase |
| Comments: |
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable (2-aminobenzoyl)acetate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Bera, A.K., Atanasova, V., Robinson, H., Eisenstein, E., Coleman, J.P., Pesci, E.C. and Parsons, J.F. Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate. Biochemistry 48 (2009) 8644–8655. [DOI] [PMID: 19694421] |
| 2. |
Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481–1491. [DOI] [PMID: 24239007] |
| 3. |
Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611–618. [DOI] [PMID: 25960261] |
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| [EC 2.3.1.262 created 2017] |
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| EC |
6.2.1.32 |
| Accepted name: |
anthranilate—CoA ligase |
| Reaction: |
ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA |
|
For diagram of acridone alkaloid biosynthesis, click here |
| Glossary: |
anthraniloyl-CoA = 2-aminobenzoyl-CoA |
| Other name(s): |
anthraniloyl coenzyme A synthetase; 2-aminobenzoate—CoA ligase; 2-aminobenzoate—coenzyme A ligase; 2-aminobenzoate coenzyme A ligase |
| Systematic name: |
anthranilate:CoA ligase (AMP-forming) |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 112692-58-7 |
| References: |
| 1. |
Altenschmidt, U., Eckerskorn, C. and Fuchs, G. Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid. Eur. J. Biochem. 194 (1990) 647–653. [DOI] [PMID: 2176602] |
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| [EC 6.2.1.32 created 1992] |
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