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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
aurachin B:NAD+ 3-oxidoreductase
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.
the enzyme catalyzes the second step in the biosynthetic pathway from aurachin C to aurachin B. Aurachin C is first converted to 3,4-dihydroxy-2-methy-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide by enzyme AuaG, which is then reduced to aurachin B. The pathway involves the migration of the prenyl group from position C3 to C4, probably via a pinacol type rearrangement. The equilibrium state of AuaG and the instability of 3,4-dihydroxy-2-methy-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide suggests the requirement of immediate reduction catalyzed by AuaH to fix the farnesyl group at the position C4 and prevent the degradation of the intermediate
the enzyme catalyzes the second step in the biosynthetic pathway from aurachin C to aurachin B. Aurachin C is first converted to 3,4-dihydroxy-2-methy-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide by enzyme AuaG, which is then reduced to aurachin B. The pathway involves the migration of the prenyl group from position C3 to C4, probably via a pinacol type rearrangement. The equilibrium state of AuaG and the instability of 3,4-dihydroxy-2-methy-4-[(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide suggests the requirement of immediate reduction catalyzed by AuaH to fix the farnesyl group at the position C4 and prevent the degradation of the intermediate
the enzyme possesses a Rossman fold, and both the conserved TGxxxGxG motif for NAD(P)H binding and the catalytic centers important for ketoreduction activity (YxxxK motif and the catalytic Ser residue)
the enzyme possesses a Rossman fold, and both the conserved TGxxxGxG motif for NAD(P)H binding and the catalytic centers important for ketoreduction activity (YxxxK motif and the catalytic Ser residue)
the enzyme possesses a Rossman fold, and both the conserved TGxxxGxG motif for NAD(P)H binding and the catalytic centers important for ketoreduction activity (YxxxK motif and the catalytic Ser residue)
the enzyme possesses a Rossman fold, and both the conserved TGxxxGxG motif for NAD(P)H binding and the catalytic centers important for ketoreduction activity (YxxxK motif and the catalytic Ser residue)
show
top
