Literature summary for 1.5.99.B2 extracted from

Tsuge, H.; Kawakami, R.; Sakuraba, H.; Ago, H.; Miyano, M.; Aki, K.; Katunuma, N.; Ohshima, T.
Crystal structure of a novel FAD-, FMN-, and ATP-containing L-proline dehydrogenase complex from Pyrococcus horikoshii (2005), J. Biol. Chem., 280, 31045-31049.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
beta subunit is the L-proline dehydrogenase catalytic component and contains FAD, alpha subunit has a classical dinucleotide fold domain with ATP and a Cys-clustered domain. FMN is located at the interface of alpha and beta subunits	Pyrococcus horikoshii
crystal structure of PDH1, which is a heterooctameric complex containing three different cofactors: FAD, FMN, and ATP. The structure is determined by x-ray crystallography to a resolution of 2.86 A. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, is similar to that of monomeric sarcosine oxidase	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	-	-	-
Pyrococcus horikoshii	O59089	beta-subunit of the L-proline dehydrogenase complex	-
Pyrococcus horikoshii OT-3	O59089	beta-subunit of the L-proline dehydrogenase complex	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Pyrococcus horikoshii

Subunits

Subunits	Comment	Organism
octamer	4 * alpha subunit + 4 * beta subunit, crystallization data	Pyrococcus horikoshii

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Pyrococcus horikoshii
FAD	-	Pyrococcus horikoshii
FAD	the beta subunit of the L-proline dehydrogenase complex is the catalytic component containing FAD as a cofactor	Pyrococcus horikoshii
FMN	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)