Literature summary for 1.2.1.8 extracted from

Baicharoen, A.; Vijayan, R.; Pongprayoon, P.
Structural insights into betaine aldehyde dehydrogenase (BADH2) from Oryza sativa explored by modeling and simulations (2018), Sci. Rep., 8, 12892 .

Search for more literature for 1.2.1.8

Application

Application	Comment	Organism
food industry	the BADH2 could play a role in the improvement of rice fragrance, which could lead to an enhancement in rice quality and market price	Oryza sativa Japonica Group

Organism

Organism	UniProt	Comment	Textmining
Oryza sativa Japonica Group	O24174	-	-

Subunits

Subunits	Comment	Organism
dimer	the 3D dimeric structure of BADH2 is modeled using homology modeling. 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 is observed between the monomers. Key inter-subunit salt bridges contributing to dimerization are identified. E487, D491, E492, K498, and K502 form strong salt bridges with charged residues on the adjacent monomer. Specifically, the nearly permanent R430-E487 hydrogen bond (over 90%) highlights its key role in dimer association	Oryza sativa Japonica Group

Synonyms

Synonyms	Comment	Organism
BADH2	-	Oryza sativa Japonica Group
betaine aldehyde dehydrogenase 2	-	Oryza sativa Japonica Group

General Information

General Information	Comment	Organism
additional information	the 3D dimeric structure of BADH2 is modeled using homology modeling. 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 is observed between the monomers. Inside the binding pocket, N162 and E260 are tethered by strong hydrogen bonds to residues in close proximity. In contrast, the catalytic C294 is very mobile and interacts occasionally with N162. The flexibility of the nucleophilic C294 can facilitate the attack of free carbonyl on an aldehyde substrate. Mainly, N162, E260, C294 are found to play a role in catalytic activity. C294 and E260 are involved in a key step of hemithioacetal-enzyme formation, while N162 helps stabilize an intermediate. Molecular dynamics (MD) simulations of substrate-bound enzyme. Both N162 and C294 form different degrees of hydrogen bonds. C294 seems to weakly hydrogen bond with adjacent amino acids (below 1% of hydrogen bonds with N162), whereas N162 forms a strong hydrogen bond with Q292 (over90%). Apparently, C294 seems to be flexible, whilst N162 is tethered by Q292 inside a pocket. The catalytic C294 is located in the middle of a cavity. The high flexibility of C294 which supports the role of the nucleophile C294's ability to attack a free carbonyl group of a bound substrate. On the contrary, N162 and E260 appear to be rigid due to strong interactions with their neighbours. Such interactions tethering N162 and E260 may help to shape a suitable environment for a catalytic activity	Oryza sativa Japonica Group
physiological function	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. But the inactive BADH2 is known to promote fragrance in rice	Oryza sativa Japonica Group

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Release 2023.1 (January 2023)