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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.99.B2 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
1.5.99.B2 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

EC Number Organism UniProt Comment Textmining
1.5.99.B2 Pyrococcus horikoshii
-
-
-
1.5.99.B2 Pyrococcus horikoshii O59089 beta-subunit of the L-proline dehydrogenase complex
-
1.5.99.B2 Pyrococcus horikoshii OT-3 O59089 beta-subunit of the L-proline dehydrogenase complex
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.99.B2 recombinant enzyme Pyrococcus horikoshii

Subunits

EC Number Subunits Comment Organism
1.5.99.B2 octamer 4 * alpha subunit + 4 * beta subunit, crystallization data Pyrococcus horikoshii

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.99.B2 ATP
-
 Pyrococcus horikoshii
1.5.99.B2 FAD
-
 Pyrococcus horikoshii
1.5.99.B2 FAD the beta subunit of the L-proline dehydrogenase complex is the catalytic component containing FAD as a cofactor Pyrococcus horikoshii
1.5.99.B2 FMN
-
 Pyrococcus horikoshii