The Enzyme Database

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EC 1.1.1.394     
Accepted name: aurachin B dehydrogenase
Reaction: aurachin B + NAD+ + H2O = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+ (overall reaction)
(1a) 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide + NAD+ = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+
(1b) aurachin B + H2O = 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide (spontaneous)
For diagram of aurachine biosynthesis, click here
Glossary: aurachin B= 4-[(2E,6E,10E)-3,7-dimethyldodeca-2,6,10-trien-1-yl]-3-hydroxy-2-methylquinoline 1-oxide
Other name(s): AuaH
Systematic name: aurachin B:NAD+ 3-oxidoreductase
Comments: The enzyme from the bacterium Stigmatella aurantiaca catalyses the final step in the conversion of aurachin C to aurachin B. In vivo the enzyme catalyses the reduction of 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline-1-oxide to form 4-[(2E,6E)-farnesyl]-2-methyl-1-oxo-3,4-dihydroquinoline-3,4-diol (note that the reactions written above proceed from right to left), which then undergoes a spontaneous dehydration to form aurachin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Katsuyama, Y., Harmrolfs, K., Pistorius, D., Li, Y. and Muller, R. A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase. Angew. Chem. Int. Ed. Engl. 51 (2012) 9437–9440. [DOI] [PMID: 22907798]
[EC 1.1.1.394 created 2016]
 
 
EC 1.14.13.222     
Accepted name: aurachin C monooxygenase/isomerase
Reaction: aurachin C + NAD(P)H + H+ + O2 = 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + NAD(P)+ + H2O (overall reaction)
(1a) aurachin C + NAD(P)H + H+ + O2 = 2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one + NAD(P)+ + H2O
(1b) 2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one = 4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide
Glossary: aurachin C = 1-hydroxy-2-methyl-3-[(2E,6E)-farnesyl]-4(1H)-quinolinone
2-hydroxy-1a-methyl-7a-[(2E,6E)-farnesyl]-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one = 2-hydroxy-1a-methyl-7a-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl)-1a,2-dihydrooxireno[2,3-b]quinolin-7(7aH)-one
4-hydroxy-2-methyl-3-oxo-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide = 4-hydroxy-2-methyl-4-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]quinolin-3(4H)-one 1-oxide
aurachin B = 2-methyl-4-[(2E,6E)-farnesyl]-3-quinolinol 1-oxide
Other name(s): auaG (gene name); aurachin C monooxygenase
Systematic name: aurachin C:NAD(P)H:oxygen oxidoreductase (4-hydroxy-2-methyl-3-oxo-4-farnesyl-3,4-dihydroquinoline-1-oxide-forming)
Comments: The aurachin C monooxygenase from the bacterium Stigmatella aurantiaca accepts both NADH and NADPH as cofactor, but has a preference for NADH. It catalyses the initial steps in the conversion of aurachin C to aurachin B. The FAD-dependent monooxygenase catalyses the epoxidation of the C2-C3 double bond of aurachin C, which is followed by a semipinacol rearrangement, causing migration of the farnesyl group from C3 to C4.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Katsuyama, Y., Harmrolfs, K., Pistorius, D., Li, Y. and Muller, R. A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase. Angew. Chem. Int. Ed. Engl. 51 (2012) 9437–9440. [DOI] [PMID: 22907798]
[EC 1.14.13.222 created 2016]
 
 


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