EC Number   |
General Information |
Reference |
|---|
    1.2.1.8 | evolution |
all BADHs known have cysteine in the active site involved in the aldehyde binding, whereas the porcine kidney enzyme (pkBADH) also has a neighborhood cysteine, both sensitive to oxidation |
763469 |
| 1.2.1.8 | malfunction |
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes |
762849 |
| 1.2.1.8 | malfunction |
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. But the BADH transcripts from plant species such as Arabidopsis (Arabidopsis thaliana), spinach (Spinacia oleracea) and tomato (Solanum lycopersicum), correctly process the mRNA |
762849 |
| 1.2.1.8 | malfunction |
some truncated transcripts of BADH are present in several crops. Such truncated transcripts may cause the accumulation of 2AP (2-acetyl-1-pyrroline), which is a key aroma compound. There is a possibility that inhibition of BADH function produces 2AP-based fragrance in main crops because of the existence of BADH isozymes. Even though 2AP formation in Bassia latifolia occurs only in flowers (fleshy corolla), in fragrant rice and plants such as Pandanus amaryllifolius and Vallaris glabra, it exists in all aerial parts |
762849 |
| 1.2.1.8 | metabolism |
betaine aldehyde dehydrogenase 2 is a key enzyme in the synthesis of fragrance aroma compounds. The extremely low activity of the enzyme in catalyzing the oxidation of acetaldehyde is crucial for the accumulation of the volatile compound 2-acetyl-1-pyrroline in fragrant rice |
723844 |
| 1.2.1.8 | metabolism |
in higher plants, glycine betaine (GB) is synthesized by two-step oxidation of choline. The first step is catalyzed by ferredoxin-dependent choline monooxygenase (CMO, EC 1.14.15.7) to produce betaine aldehyde (BAL). BAL is converted to GB by aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) containing the activities of betaine aldehyde dehydrogenase (BADH) |
763552 |
| 1.2.1.8 | metabolism |
NO's involvement in the biosynthetic pathway of GB production in plants takes place prior to the involvement of BADH in converting the toxic intermediate betaine aldehyde to GB. The extent of the impact of NO on GB content and BADH activity also varies with light exposure, but the pattern observed is similar to that observed in dark-grown seedlings |
763598 |
| 1.2.1.8 | more |
for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity |
763552 |
| 1.2.1.8 | more |
pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+. Binding of NAD+ to the enzyme causes changes in its secondary structure, the presence of K+ helps maintain its alpha-helix content. BADH enzyme structure homology modeing using the human ALDH9A1 structure (HsALDH9A1, PDB ID 6QAK) as template. The conserved catalytic residues C288, G285, N157, and E254 and the decapeptide VTLELGGKSP are identified |
763372 |
| 1.2.1.8 | more |
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 |
763723 |
