5X5T

Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (KGSADH) from Azospirillum brasilense

Summary for 5X5T

• Entry DOI: 10.2210/pdb5x5t/pdb
• Related: 5X5U
• Descriptor: Alpha-ketoglutaric semialdehyde dehydrogenase, GLYCEROL (3 entities in total)
• Functional Keywords: alpha-ketogluratare semialdehyde dehydrogenase, oxidoreductase
• Biological source: Azospirillum brasilense
• Total number of polymer chains: 2
• Total formula weight: 107806.25

Authors

Son, H.-F.,Kim, K.-J. (deposition date: 2017-02-17, release date: 2017-05-10, Last modification date: 2023-11-22)

Primary citation

Son, H.F.,Park, S.,Yoo, T.H.,Jung, G.Y.,Kim, K.J.
Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense.
Sci Rep, 7:46005-46005, 2017

PubMed Abstract: 3-Hydroxypropionic acid (3-HP) is an important platform chemical to be converted to acrylic acid and acrylamide. Aldehyde dehydrogenase (ALDH), an enzyme that catalyzes the reaction of 3-hydroxypropionaldehyde (3-HPA) to 3-HP, determines 3-HP production rate during the conversion of glycerol to 3-HP. To elucidate molecular mechanism of 3-HP production, we determined the first crystal structure of a 3-HP producing ALDH, α-ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH), in its apo-form and in complex with NAD. Although showing an overall structure similar to other ALDHs, the AbKGSADH enzyme had an optimal substrate binding site for accepting 3-HPA as a substrate. Molecular docking simulation of 3-HPA into the AbKGSADH structure revealed that the residues Asn159, Gln160 and Arg163 stabilize the aldehyde- and the hydroxyl-groups of 3-HPA through hydrogen bonds, and several hydrophobic residues, such as Phe156, Val286, Ile288, and Phe450, provide the optimal size and shape for 3-HPA binding. We also compared AbKGSADH with other reported 3-HP producing ALDHs for the crucial amino acid residues for enzyme catalysis and substrate binding, which provides structural implications on how these enzymes utilize 3-HPA as a substrate.

PubMed: 28393833
DOI: 10.1038/srep46005

Experimental method

X-RAY DIFFRACTION (2.25 Å)