Structural insights into betaine aldehyde dehydrogenase (BADH2) from Oryza sativa explored by modeling and simulations.

ABSTRACT: Betaine aldehyde dehydrogenase 2 (BADH2) plays a key role in the accumulation of 2-acetyl-1-pyrroline (2AP), a fragrant compound in rice (Oryza sativa). BADH2 catalyses the oxidation of aminoaldehydes to carboxylic acids. An inactive BADH2 is known to promote fragrance in rice. The 3D structure and atomic level protein-ligand interactions are currently unknown. Here, the 3D dimeric structure of BADH2 was modeled using homology modeling. Furthermore, two 0.5 µs simulations were performed to explore the nature of BADH2 dimer structurally and dynamically. Each monomer comprises of 3 domains (substrate-binding, NAD⁺-binding, and oligomerization domains). The NAD⁺-binding domain is the most mobile. A scissor-like motion was observed between the monomers. Inside the binding

SUBMITTER: Baicharoen A 

PROVIDER: S-EPMC6110774 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature