Literature summary for 1.3.7.15 extracted from

Kim, E.J.; Kim, J.S.; Lee, I.H.; Rhee, H.J.; Lee, J.K.
Superoxide generation by chlorophyllide a reductase of Rhodobacter sphaeroides (2008), J. Biol. Chem., 283, 3718-3730.

Search for more literature for 1.3.7.15

General Stability

General Stability	Organism
enzyme is labile in the presence of O2	Cereibacter sphaeroides

Organism

Organism	UniProt	Comment	Textmining
Cereibacter sphaeroides	B9KK02	reductase subunit BchX	-
Cereibacter sphaeroides KD131	B9KK02	reductase subunit BchX	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ	Cereibacter sphaeroides	?	-	?
additional information	holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ	Cereibacter sphaeroides KD131	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FMN	-	Cereibacter sphaeroides
iron-sulfur centre	-	Cereibacter sphaeroides

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Release 2023.1 (January 2023)