Literature summary for 1.14.13.8 extracted from

Cho, H.J.; Cho, H.Y.; Kim, K.J.; Kim, M.H.; Kim, S.W.; Kang, B.S.
Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism (2011), J. Struct. Biol., 175, 39-48.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Methylophaga aminisulfidivorans

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of enzyme and enzyme in complex with NADP+, and a mutant Y207S, which lacks indole oxygenation activity, with and without indole. The crystal structures reveal overlapping binding sites for NADP+ and indole, suggestive of a double-displacement reaction mechanism. NADPH induces conformational changes in two active site motifs. One of the motifs contains Arg229, which participates in interactions with the phosphate group of NADPH and appears be a determinant of the preferential binding to NADPH rather than NADH. The second motif contains Tyr207	Methylophaga aminisulfidivorans

Crystallization (Comment)

Organism

crystal structures of enzyme and enzyme in complex with NADP+, and a mutant Y207S, which lacks indole oxygenation activity, with and without indole. The crystal structures reveal overlapping binding sites for NADP+ and indole, suggestive of a double-displacement reaction mechanism. NADPH induces conformational changes in two active site motifs. One of the motifs contains Arg229, which participates in interactions with the phosphate group of NADPH and appears be a determinant of the preferential binding to NADPH rather than NADH. The second motif contains Tyr207

Methylophaga aminisulfidivorans

Protein Variants

Protein Variants	Comment	Organism
Y207S	mutant exhibits very little indoxyl producing activity but the NADPH oxidase activity of the mutant is higher than that of the wild-type enzyme	Methylophaga aminisulfidivorans

Inhibitors

Inhibitors	Comment	Organism	Structure
indole	inhibits NADPH oxidase activity	Methylophaga aminisulfidivorans
NADPH	inhibits the binding of indole and decreases indoxyl production	Methylophaga aminisulfidivorans

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.005	-	indole	wild-type, pH 8.0, temperature not specified in the publication	Methylophaga aminisulfidivorans
0.008	-	indole	mutant Y207S, pH 8.0, temperature not specified in the publication	Methylophaga aminisulfidivorans

Organism

Organism	UniProt	Comment	Textmining
Methylophaga aminisulfidivorans	Q83XK4	-	-
Methylophaga aminisulfidivorans SK1	Q83XK4	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
indole + NADPH + H+ + O2	-	Methylophaga aminisulfidivorans	indoxyl + NADP+ + H2O	-	?
indole + NADPH + H+ + O2	-	Methylophaga aminisulfidivorans SK1	indoxyl + NADP+ + H2O	-	?