Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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.
    View publication on PubMed

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