the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences
the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences. The Loktanella ALDH16 structure may be considered to be the archetype of the ALDH16 family
ALDH2 inhibition suppresses cocaine self-administration and seeking behavior and prevents cocaine- or cue-induced reinstatement in a rat model of cocaine relapse-like behavior
inhibition of ALDH2 leads to accumulation of cytotoxic 4-hydroxynonenal and malondialdehyde, which can cause cell death through activation of c-Jun N-terminal protein kinase and/or p38 kinase
the loss of ALDH2 enzyme activity leads to increased mitochondrial oxidative stress in aortic endothelia by three pro-oxidant stimuli, nitroglycerin, doxorubicin, and acetaldehyde
vascular tolerance to nitroglycerin may be caused by impaired nitroglycerin bioactivation due to inactivation of mitochondrial aldehyde dehydrogenase ALDH2
enzyme residues Ala505 and Gln506 interact with the conserved aldehyde anchor loop structure in the closed state. The apparent involvement of these residues in catalysis is significant because they are replaced by Pro505 and Lys506 in a genetic deletion (c.1512delG) that causes pyridoxine-dependent epilepsy, a rare autosomal recessive disorder that typically presents with seizures in the first days of life. Compromised ALDH7A1 activity leads to increased levels of alpha-aminoadipate semialdehyde and DELTA1-piperideine-6-carboxylic acid (P6C), the cyclized form of alpha-aminoadipate semialdehyde. P6C reacts with a ubiquitous cofactor, pyridoxal 5'-phosphate, and the resulting adduct is incapable as an enzyme cofactor. Site-directed single mutations A505P and Q506K and double mutation A505P/Q506K as well as the C-terminal truncation mutant DELTA504-511, which lacks residues 504-511, are analyzed with steady-state kinetics assays and analytical ultracentrifugation. The mutant enzymes exhibit a common phenotype characterized by a very high Km for alpha-aminoadipate semialdehyde (AASAL) and a perturbed self-association equilibrium
the combined disruption of ALDH3I1 and ALDH7B4 decreases the cellular NAD(P)H contents and alters the NAD(P)H/NAD(P)+ ratio. The aldh double mutant has higher glucose-6-phosphate dehydrogenase activity and a reduced quantum yield of photosystem II and photosynthetic capacity at relatively high light intensities compared to the wild-type. Mutant KO6 plants accumulate higher levels of reactive oxygen species (ROS) and malondialdehyde (MDA) than the wild-type plants. Disruption of ALDH3I1 and ALDH7B4 affects glutathione metabolism and photosynthesis
ALDH2 plays an essential role in nitroglycerin bioactivation. ALDH2-catalyzed superoxide formation may essentially contribute to oxidative stress in nitroglycerin-exposed blood vessels
ALDH2 reduces cardiac damage caused by ischaemia insult. ALDH2 protects the heart from aldehyde toxicity and is able to elicit signalling events that can protect against myocardial damages caused by acute ethanol toxicity
isoform ALDH3A1 plays a protective role against ultraviolet radiation-induced oxidative damage to ocular tissues. The nuclear presence of isoform ALDH3A1 may be involved in cell cycle regulation
isoforms ALDH3A1 plays a protective role against ultraviolet radiation-induced oxidative damage to ocular tissues. The nuclear presence of isoform ALDH3A1 may be involved in cell cycle regulation
rice ALDH7 is needed for seed maturation and viability. ALDH7 is involved in removing various aldehydes formed by oxidative stress during seed desiccation
in white spot syndrome virus- (WSSV-)infected shrimps cultured at 32°C, transcriptional levels of representative immediate-early, early, and late genes are initially higher than those at 25°C. NAD-dependent aldehyde dehydrogenase (ALDH) and the proteasome alpha 4 subunit (proteasome alpha4) are markedly upregulated in WSSV-infected shrimps at 32°C. In addition, hsp70 is upregulated at 32°C. When aldh, proteasome alpha4, and hsp70 are knocked down by double-stranded RNA interference and shrimps are challenged with WSSV, the aldh and hsp70 knockdown shrimps become severely infected at 32°C, while the proteasome alpha4 knockdown shrimps remain uninfected
transgenic Arabidopsis plants overexpressing grapevine ALDH2B8 show sustained growth upon salt stress and increased tolerance against oxidative stress, which is correlated with decreased accumulation of reactive oxygen species and malondialdehyde derived from cellular lipid peroxidation
transgenic Arabidopsis plants overexpressing grapevine ALDH2B8 show sustained growth upon salt stress and increased tolerance against oxidative stress, which was correlated with decreased accumulation of reactive oxygen species and malondialdehyde derived from cellular lipid peroxidation
aldehyde dehydrogenase 7A1 (ALDH7A1) catalyzes the terminal step of lysine catabolism, the NAD+-dependent oxidation of alpha-aminoadipate semialdehyde to alpha-aminoadipate
human ALDH16A1 apparently lacks measurable aldehyde oxidation activity, suggesting it is a pseudoenzyme, consistent with the absence of the catalytic Cys in its sequence
residues Ala505 and Gln506, that interact with the conserved aldehyde anchor loop structure in the closed state, are involved in catalysis. Discovery of the C-terminus as a mobile part of the active site. The C-terminus of ALDH7A1 is crucial for the maintenance of both the oligomeric state and the catalytic activity
active site structure modeling of LsALDH16 from 1.65 A resolution crystal structure with the catalytic loop in complex with NAD+. Structure comparison of the human and the Loktanella sp. ALDH16 enzymes, overview
enzyme structure analysis and modeling, overview. ALDHTt adopts the ALDH superfamily common structural architecture. The ALDHTt monomer is composed of the three domains common to all ALDHs: (i) The NAD(P)+ binding domain (1-125 + 148-261) comprising a Rossman fold, (ii) the catalytic domain (267-458) and (iii) the oligomerization domain (126-147 + 494-501). (i, ii) are separated by two loops, a short linker loop region containing Glu261 (261-267), required to activate the catalytic cysteine Cys295, and a long inter-domain linker (459-493) harboring the aldehyde anchor loop (464-466). This anchor loop, containing regulatory residues such as the substrate entry channel (SEC) mouth residue and the gating aromatic residue, interacts with the substrate and product. The catalytic and cofactor-binding domains form a central tunnel through the monomer with NAD(P)+ at one side and the classical entrance for substrate on the opposite side. The catalytic residues are deep within the center of the tunnel about 16 A from the cofactor binding site to Glu261 and substrate entry tunnel to the catalytic Cys295. The tunnel is about 5 A in diameter at its widest point
enzyme structure analysis and modeling, overview. ALDHTt adopts the ALDH superfamily common structural architecture. The ALDHTt monomer is composed of the three domains common to all ALDHs: (i) The NAD(P)+ binding domain (1-125 + 148-261) comprising a Rossman fold, (ii) the catalytic domain (267-458) and (iii) the oligomerization domain (126-147 + 494-501). (i, ii) are separated by two loops, a short linker loop region containing Glu261 (261-267), required to activate the catalytic cysteine Cys295, and a long inter-domain linker (459-493) harboring the aldehyde anchor loop (464-466). This anchor loop, containing regulatory residues such as the substrate entry channel (SEC) mouth residue and the gating aromatic residue, interacts with the substrate and product. The catalytic and cofactor-binding domains form a central tunnel through the monomer with NAD(P)+ at one side and the classical entrance for substrate on the opposite side. The catalytic residues are deep within the center of the tunnel about 16 A from the cofactor binding site to Glu261 and substrate entry tunnel to the catalytic Cys295. The tunnel is about 5 A in diameter at its widest point
enzyme structure analysis and modeling, overview. ALDHTt adopts the ALDH superfamily common structural architecture. The ALDHTt monomer is composed of the three domains common to all ALDHs: (i) The NAD(P)+ binding domain (1-125 + 148-261) comprising a Rossman fold, (ii) the catalytic domain (267-458) and (iii) the oligomerization domain (126-147 + 494-501). (i, ii) are separated by two loops, a short linker loop region containing Glu261 (261-267), required to activate the catalytic cysteine Cys295, and a long inter-domain linker (459-493) harboring the aldehyde anchor loop (464-466). This anchor loop, containing regulatory residues such as the substrate entry channel (SEC) mouth residue and the gating aromatic residue, interacts with the substrate and product. The catalytic and cofactor-binding domains form a central tunnel through the monomer with NAD(P)+ at one side and the classical entrance for substrate on the opposite side. The catalytic residues are deep within the center of the tunnel about 16 A from the cofactor binding site to Glu261 and substrate entry tunnel to the catalytic Cys295. The tunnel is about 5 A in diameter at its widest point
enzyme structure analysis and modeling, overview. ALDHTt adopts the ALDH superfamily common structural architecture. The ALDHTt monomer is composed of the three domains common to all ALDHs: (i) The NAD(P)+ binding domain (1-125 + 148-261) comprising a Rossman fold, (ii) the catalytic domain (267-458) and (iii) the oligomerization domain (126-147 + 494-501). (i, ii) are separated by two loops, a short linker loop region containing Glu261 (261-267), required to activate the catalytic cysteine Cys295, and a long inter-domain linker (459-493) harboring the aldehyde anchor loop (464-466). This anchor loop, containing regulatory residues such as the substrate entry channel (SEC) mouth residue and the gating aromatic residue, interacts with the substrate and product. The catalytic and cofactor-binding domains form a central tunnel through the monomer with NAD(P)+ at one side and the classical entrance for substrate on the opposite side. The catalytic residues are deep within the center of the tunnel about 16 A from the cofactor binding site to Glu261 and substrate entry tunnel to the catalytic Cys295. The tunnel is about 5 A in diameter at its widest point