Aldehyde Dehydrogenase
Disulfiram
Acetaldehyde
Retinal Dehydrogenase
Alcohol Dehydrogenase
Betaine-Aldehyde Dehydrogenase
Cyanamide
NAD
L-Lactate Dehydrogenase
Alcohol Oxidoreductases
Glyceraldehyde-3-Phosphate Dehydrogenases
Isoenzymes
Glutamate Dehydrogenase
Sjogren-Larsson Syndrome
Malate Dehydrogenase
Isocitrate Dehydrogenase
Phosphoramide Mustards
NADP
Liver
L-Iditol 2-Dehydrogenase
Dihydrolipoamide Dehydrogenase
Molecular Sequence Data
Carbohydrate Dehydrogenases
Succinate Dehydrogenase
Mitochondria, Liver
Substrate Specificity
Ethanol
Amino Acid Sequence
Oxidation-Reduction
Aldehyde Reductase
Methylmalonate-Semialdehyde Dehydrogenase (Acylating)
Succinate-Semialdehyde Dehydrogenase
Flushing
Hydroxysteroid Dehydrogenases
Glucose 1-Dehydrogenase
Sugar Alcohol Dehydrogenases
Coenzymes
p-Aminoazobenzene
Xanthine Dehydrogenase
Glucose Dehydrogenases
Phosphogluconate Dehydrogenase
Oxidoreductases
NADH Dehydrogenase
IMP Dehydrogenase
Base Sequence
Formate Dehydrogenases
Acyl-CoA Dehydrogenase
17-Hydroxysteroid Dehydrogenases
Neoplastic Stem Cells
Alcohols
Catalysis
Cloning, Molecular
3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
Oxidoreductases Acting on CH-NH Group Donors
Nitroglycerin
Ditiocarb
Pyruvate Dehydrogenase (Lipoamide)
3-Hydroxyacyl CoA Dehydrogenases
Sequence Homology, Amino Acid
Escherichia coli
11-beta-Hydroxysteroid Dehydrogenases
Pentaerythritol Tetranitrate
Cytosol
Uridine Diphosphate Glucose Dehydrogenase
Hydrogen-Ion Concentration
Retinaldehyde
Dihydrouracil Dehydrogenase (NADP)
Mitochondria
Betaine
Gene Expression Regulation, Enzymologic
Alcohol Deterrents
3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
Glucosephosphate Dehydrogenase Deficiency
Enzyme Induction
11-beta-Hydroxysteroid Dehydrogenase Type 1
Binding Sites
Stereoisomerism
Alanine Dehydrogenase
Sheep
Hydroxyprostaglandin Dehydrogenases
Electrophoresis, Polyacrylamide Gel
Mannitol Dehydrogenases
Fatty Alcohols
Isoelectric Focusing
Butyryl-CoA Dehydrogenase
Spectrophotometry
Pseudomonas
20-Hydroxysteroid Dehydrogenases
11-beta-Hydroxysteroid Dehydrogenase Type 2
Chlorpropamide
Mitochondrial Proteins
Acyl-CoA Dehydrogenase, Long-Chain
Benzodioxoles
Mutation
Chromatography, High Pressure Liquid
Homoserine Dehydrogenase
Tretinoin
Metabolic Detoxication, Drug
Choline Dehydrogenase
Isovaleryl-CoA Dehydrogenase
3-Isopropylmalate Dehydrogenase
Sequence Alignment
RNA, Messenger
Dimethyl Adipimidate
Biotransformation
Horses
Pyruvate Dehydrogenase (Lipoamide)-Phosphatase
Leucine Dehydrogenase
Multienzyme Complexes
Phosphoglycerate Dehydrogenase
Enzyme Stability
Molecular Structure
Chemistry
Estradiol Dehydrogenases
Alcohol Drinking
Chemical Phenomena
Alkanes
Acetates
Cytoplasm
Vibrio
Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (1/1111)
Thionein (T) has not been isolated previously from biological material. However, it is generated transiently in situ by removal of zinc from metallothionein under oxidoreductive conditions, particularly in the presence of selenium compounds. T very rapidly activates a group of enzymes in which zinc is bound at an inhibitory site. The reaction is selective, as is apparent from the fact that T does not remove zinc from the catalytic sites of zinc metalloenzymes. T instantaneously reverses the zinc inhibition with a stoichiometry commensurate with its known capacity to bind seven zinc atoms in the form of clusters in metallothionein. The zinc inhibition is much more pronounced than was previously reported, with dissociation constants in the low nanomolar range. Thus, T is an effective, endogenous chelating agent, suggesting the existence of a hitherto unknown and unrecognized biological regulatory system. T removes the metal from an inhibitory zinc-specific enzymatic site with a resultant marked increase of activity. The potential significance of this system is supported by the demonstration of its operations in enzymes involved in glycolysis and signal transduction. (+info)Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (2/1111)
Amino acid sequencing of an internal peptide fragment derived from purified Xenopus cytosolic thyroid hormone-binding protein (xCTBP) demonstrates high similarity to the corresponding sequence of mammalian aldehyde dehydrogenase 1 (ALDH1) (Yamauchi, K., and Tata, J. R. (1994) Eur. J. Biochem. 225, 1105-1112). Here we show that xCTBP was co-purified with ALDH and 3,3',5-triiodo-L-thyronine (T3) binding activities. By photoaffinity labeling with [125I]T3, a T3-binding site in the xCTBP was estimated to reside in amino acid residues 93-114, which is distinct from the active site of the enzyme but present in the NAD+ binding domain. The amino acid sequences deduced from the two isolated xALDH1 cDNAs (xALDH1-I and xALDH1-II) were 94.6% identical to each other and very similar to those of mammalian ALDH1 enzymes. The two recombinant xALDH1 proteins exhibit both T3 binding activity and ALDH activity converting retinal to retinoic acid (RA), which are similar to those of xCTBP. The mRNAs were present abundantly in kidney and intestine of adult female Xenopus. Interestingly, their T3 binding activities were inhibited by NAD+ and NADH but not by NADP+ and NADPH, whereas NAD+ was required for their ALDH activities. Our results demonstrate that xCTBP is identical to ALDH1 and suggest that this protein might modulate RA synthesis and intracellular level of free T3. (+info)Stimulation of premature retinoic acid synthesis in Xenopus embryos following premature expression of aldehyde dehydrogenase ALDH1. (3/1111)
In order for nuclear retinoic acid receptors to mediate retinoid signaling, the ligand retinoic acid must first be produced from its vitamin A precursor retinal. Biochemical studies have shown that retinal can be metabolized in vitro to retinoic acid by members of the aldehyde dehydrogenase enzyme family, including ALDH1. Here we describe the first direct evidence that ALDH1 plays a physiological role in retinoic acid synthesis by analysis of retinoid signaling in Xenopus embryos, which have plentiful stores of maternally derived retinal. The Xenopus ALDH1 gene was cloned and shown to be highly conserved with chick and mammalian homologs. Xenopus ALDH1 was not expressed at blastula and gastrula stages, but was expressed at the neurula stage. We used a retinoic acid bioassay to demonstrate that retinoic acid is normally undetectable in embryos from fertilization to the initial gastrula stage, but that a tremendous increase in retinoic acid occurs during neurulation when ALDH1 is first expressed. Overexpression of ALDH1 by injection of Xenopus embryos with mRNAs encoding the mouse, chick or Xenopus ALDH1 homologs induced high levels of retinoic acid detection during the blastula stage. Thus, premature expression of ALDH1 stimulates premature synthesis of retinoic acid. These findings reveal an important conserved role for ALDH1 in retinoic acid synthesis in vivo, and demonstrate that conversion of retinoids from the aldehyde form to the carboxylic acid form is a crucial regulatory step in retinoid signaling. (+info)The negative regulation of the rat aldehyde dehydrogenase 3 gene by glucocorticoids: involvement of a single imperfect palindromic glucocorticoid responsive element. (4/1111)
Glucocorticoids repressed the polycyclic aromatic hydrocarbon-dependent induction of Class 3 aldehyde dehydrogenase (ALDH3) enzyme activity and mRNA levels in isolated rat hepatocytes by more than 50 to 80%, with a concentration-dependence consistent with the involvement of the glucocorticoid receptor (GR). No consistent effect on the low basal transcription rate was observed. This effect of glucocorticoids (GC) on polycyclic aromatic hydrocarbon induction was effectively antagonized at the mRNA and protein level by the GR antagonist RU38486. The response was cycloheximide-sensitive, because the protein synthesis inhibitor caused a GC-dependent superinduction of ALDH3 mRNA levels. This suggests that the effects of GC on this gene are complex and both positive and negative gene regulation is possible. The GC-response was recapitulated in HepG2 cells using transient transfection experiments with CAT reporter constructs containing 3.5 kb of 5'-flanking region from ALDH3. This ligand-dependent response was also observed when a chimeric GR (GR DNA-binding domain and peroxisome proliferator-activated receptor ligand-binding domain) was used in place of GR in the presence of the peroxisome proliferator, nafenopin. A putative palindromic glucocorticoid-responsive element exists between -930 and -910 base pairs relative to the transcription start site. If this element was either deleted or mutated, the negative GC-response was completely lost, which suggests that this sequence is responsible, in part, for the negative regulation of the gene. Electrophoretic mobility shift analysis demonstrated that this palindromic glucocorticoid-responsive element is capable of forming a specific DNA-protein complex with human glucocorticoid receptor. In conclusion, the negative regulation of ALDH3 in rat liver is probably mediated through direct GR binding to its canonical responsive element. (+info)Molecular analysis of two closely related mouse aldehyde dehydrogenase genes: identification of a role for Aldh1, but not Aldh-pb, in the biosynthesis of retinoic acid. (5/1111)
Mammalian class I aldehyde dehydrogenase (ALDH1) has been implicated as a retinal dehydrogenase in the biosynthesis of retinoic acid, a modulator of gene expression and cell differentiation. As the first step towards studying the regulation of ALDH1 and its physiological role in the biosynthesis of retinoic acid, mouse ALDH1 cDNA and genomic clones have been characterized. During the cloning process, an additional closely related gene was also isolated and named Aldh-pb, owing to its high amino acid sequence identity (92%) with the rat phenobarbitol-inducible ALDH protein (ALDH-PB). Aldh1 spans about 45 kb in length, whereas Aldh-pb spans about 35 kb. Both genes are composed of 13 exons, and the positions of all the exon/intron boundaries are conserved with those of human ALDH1. The promoter regions of Aldh1 and Aldh-pb demonstrate high sequence similarity with those of human ALDH1 and rat ALDH-PB. Expression of Aldh1 and Aldh-pb is tissue-specific, with mRNAs for both genes being found in the liver, lung and testis, but not in the heart, spleen or muscle. Expression of Aldh-pb, but not Aldh1, was also detected at high levels in the kidney. Aldh1 and Aldh-pb encode proteins of 501 amino acids with 90% positional identity. To examine the relative roles of these two enzymes in retinoic acid synthesis in vivo, Xenopus embryos were injected with mRNAs encoding these enzymes to assay the effect on conversion of endogenous retinal into retinoic acid. Injection of ALDH1, but not ALDH-PB, mRNA stimulated retinoic acid synthesis in Xenopus embryos at the blastula stage. Thus our results indicate that Aldh1 can function in retinoic acid synthesis under physiological conditions, but that the closely related Aldh-pb does not share this property. (+info)Relationships within the aldehyde dehydrogenase extended family. (6/1111)
One hundred-forty-five full-length aldehyde dehydrogenase-related sequences were aligned to determine relationships within the aldehyde dehydrogenase (ALDH) extended family. The alignment reveals only four invariant residues: two glycines, a phenylalanine involved in NAD binding, and a glutamic acid that coordinates the nicotinamide ribose in certain E-NAD binary complex crystal structures, but which may also serve as a general base for the catalytic reaction. The cysteine that provides the catalytic thiol and its closest neighbor in space, an asparagine residue, are conserved in all ALDHs with demonstrated dehydrogenase activity. Sixteen residues are conserved in at least 95% of the sequences; 12 of these cluster into seven sequence motifs conserved in almost all ALDHs. These motifs cluster around the active site of the enzyme. Phylogenetic analysis of these ALDHs indicates at least 13 ALDH families, most of which have previously been identified but not grouped separately by alignment. ALDHs cluster into two main trunks of the phylogenetic tree. The largest, the "Class 3" trunk, contains mostly substrate-specific ALDH families, as well as the class 3 ALDH family itself. The other trunk, the "Class 1/2" trunk, contains mostly variable substrate ALDH families, including the class 1 and 2 ALDH families. Divergence of the substrate-specific ALDHs occurred earlier than the division between ALDHs with broad substrate specificities. A site on the World Wide Web has also been devoted to this alignment project. (+info)The loss in hydrophobic surface area resulting from a Leu to Val mutation at the N-terminus of the aldehyde dehydrogenase presequence prevents import of the protein into mitochondria. (7/1111)
An apparent conservative mutation, Leu to Val, at the second residue of the rat liver mitochondrial aldehyde dehydrogenase (ALDH) presequence resulted in a precursor protein that was not imported into mitochondria. Additional mutants were made to substitute various amino acids with nonpolar side chains for Leu2. The Ile, Phe, and Trp mutants were imported to an extent similar to that of the native precursor, but the Ala mutant was imported only about one-fourth as well. It was shown that the N-terminal methionine was removed from the L2V mutant in a reaction catalyzed by methionine aminopeptidase. The N-terminal methionine of native pALDH and the other mutant presequences was blocked, presumably by acetylation. Because of the difference in co-translational modification, the L2V mutant sustained a significant loss in the available hydrophobic surface of the presequence. Import competence was restored to the L2V mutant when it was translated using a system that did not remove Met1. The removal of an Arg-Gly-Pro helix linker segment (residues 11-14) from the L2V mutant, which shifted three leucine residues toward the N-terminus, also restored import competence. These results lead to the conclusion that a minimum amount of hydrophobic surface area near the N-termini of mitochondrial presequences is an essential property to determine their ability to be imported. As a result, both electrostatic and hydrophobic components must be considered when trying to understand the interactions between precursor proteins and proteins of the mitochondrial import apparatus. (+info)In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import. (8/1111)
The positive charges and structural properties of the mitochondrial leader sequence of aldehyde dehydrogenase have been extensively studied in vitro. The results of these studies showed that increasing the helicity of this leader would compensate for reduced import from positive charge substitutions of arginine with glutamine or the insertion of negative charged residues made in the native leader. In this in vivo study, utilizing the green fluorescent protein (GFP) as a passenger protein, import results showed the opposite effect with respect to helicity, but the results from mutations made within the native leader sequence were consistent between the in vitro and in vivo experiments. Leader mutations that reduced the efficiency of import resulted in a cytosolic accumulation of a truncated GFP chimera that was fluorescent but devoid of a mitochondrial leader. The native leader efficiently imported before GFP could achieve a stable, import-incompetent structure, suggesting that import was coupled with translation. As a test for a co-translational mechanism, a chimera of GFP that contained the native leader of aldehyde dehydrogenase attached at the N terminus and a C-terminal endoplasmic reticulum targeting signal attached to the C terminus of GFP was constructed. This chimera was localized exclusively to mitochondria. The import result with the dual signal chimera provides support for a co-translational mitochondrial import pathway. (+info)* Intellectual disability: Individuals with Sjogren-Larsson syndrome typically have mild to moderate intellectual disability, which can range from mild cognitive impairment to more severe developmental delays.
* Seizures: Seizures are a common feature of Sjogren-Larsson syndrome, and they can be difficult to control with medication.
* Physical abnormalities: Individuals with Sjogren-Larsson syndrome may have distinctive physical features, such as short stature, thinning of the hair on the scalp, and thin, brittle skin. They may also have joint deformities, such as clubfoot or scoliosis.
* Vision problems: Sjogren-Larsson syndrome can cause vision problems, including nearsightedness, farsightedness, and astigmatism.
* Hearing loss: Some individuals with Sjogren-Larsson syndrome may experience hearing loss or auditory processing disorders.
There is no cure for Sjogren-Larsson syndrome, but various treatments can help manage the symptoms. These may include medications to control seizures, physical therapy to improve joint mobility and strength, and occupational therapy to develop daily living skills. In addition, speech and language therapy may be helpful for individuals with hearing loss or communication difficulties.
Early diagnosis of Sjogren-Larsson syndrome is important to ensure that children receive appropriate interventions and support as early as possible. Diagnosis typically involves a combination of clinical evaluation, genetic testing, and imaging studies, such as MRI or CT scans. Genetic counseling can also be helpful for families who have a history of the condition.
Overall, Sjogren-Larsson syndrome is a rare and complex disorder that requires careful management and support. With appropriate interventions and resources, individuals with this condition can lead fulfilling lives.
Flushing can also be a side effect of certain medications, such as beta-blockers, aspirin, and some antidepressants. In addition, flushing can be a sign of an underlying condition that affects blood flow or blood vessels, such as Raynaud's disease or lupus.
Treatment for flushing will depend on the underlying cause. For example, if flushing is caused by an allergic reaction, medications such as antihistamines may be prescribed. If the flushing is caused by a medical condition, treatment will focus on managing that condition. In some cases, lifestyle changes such as avoiding triggers, wearing protective clothing, and using cool compresses can help reduce flushing.
It is important to seek medical attention if flushing is severe, persistent, or accompanied by other symptoms such as fever, chest pain, or difficulty breathing. Your healthcare provider can diagnose the underlying cause of flushing and recommend appropriate treatment.
The condition is inherited in an X-linked recessive pattern, meaning that the gene for G6PD deficiency is located on the X chromosome and affects males more frequently than females. Females may also be affected but typically have milder symptoms or may be carriers of the condition without experiencing any symptoms themselves.
G6PD deficiency can be caused by mutations in the G6PD gene, which can lead to a reduction in the amount of functional enzyme produced. The severity of the condition depends on the specific nature of the mutation and the degree to which it reduces the activity of the enzyme.
Symptoms of G6PD deficiency may include jaundice (yellowing of the skin and eyes), fatigue, weakness, and shortness of breath. In severe cases, the condition can lead to hemolytic anemia, which is characterized by the premature destruction of red blood cells. This can be triggered by certain drugs, infections, or foods that contain high levels of oxalic acid or other oxidizing agents.
Diagnosis of G6PD deficiency typically involves a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment is focused on managing symptoms and preventing complications through dietary modifications, medications, and avoidance of triggers such as certain drugs or infections.
Overall, G6PD deficiency is a relatively common genetic disorder that can have significant health implications if left untreated. Understanding the causes, symptoms, and treatment options for this condition is important for ensuring appropriate care and management for individuals affected by it.
Aldehyde dehydrogenase
Betaine-aldehyde dehydrogenase
Aldehyde dehydrogenase (NAD+)
Coniferyl-aldehyde dehydrogenase
Aldehyde dehydrogenase (NADP+)
Aryl-aldehyde dehydrogenase
Aldehyde dehydrogenase (FAD-independent)
Aldehyde dehydrogenase (pyrroloquinoline-quinone)
Aryl-aldehyde dehydrogenase (NADP+)
Aldehyde dehydrogenase (NAD(P)+)
Long-chain-aldehyde dehydrogenase
Aldehyde dehydrogenase 18 family, member A1
Aldehyde dehydrogenase 6 family, member A1
Aldehyde dehydrogenase 4 family, member A1
Aldehyde dehydrogenase 3 family, member A1
Aldehyde dehydrogenase 9 family, member A1
Aldehyde dehydrogenase 5 family, member A1
Malonate-semialdehyde dehydrogenase (acetylating)
Phenethylamine
ALDH3B1
ALDH1A3
Acetaldehyde dehydrogenase
Dehydrogenase
Aldehyde
Lillian Dyck
Alda-1
3,4-Dihydroxyphenylacetaldehyde
Short-term effects of alcohol consumption
Selin Kara
Glycolaldehyde dehydrogenase
Molybdopterin
Metabolism
Aflatoxin B1
Tropoflavin
Oxoglutarate dehydrogenase (NADP+)
Hypochlorous acid
Sobrietol
Malondialdehyde
4-Hydroxyphenylacetaldehyde
Coniferyl aldehyde
Glyoxylic acid
ALDH7A1
Oxalate oxidase
Alcanivorax borkumensis
Methylglyoxal pathway
Α,β-Unsaturated carbonyl compound
Thermoplasma acidophilum
Glycolysis
Toxication
Lactaldehyde
Alcohol-induced respiratory reactions
Agmatine
Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
Benzene
Fluoroacetaldehyde dehydrogenase
Prunetin
Alcoholism Medication: Glutamate receptor blockers, Aldehyde dehydrogenase inhibitors, Opiate antagonists
DailyMed - Search Results for Aldehyde Dehydrogenase Inhibitor
Alcoholism Medication: Glutamate receptor blockers, Aldehyde dehydrogenase inhibitors, Opiate antagonists
Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) (NBP2-02483): Novus Biologicals
Comprehensive proteomic profiling of aldehyde dehydrogenases in lung adenocarcinoma cell lines.
Sjögren-Larsson syndrome: seven novel mutations in the fatty aldehyde dehydrogenase gene ALDH3A2.<...
Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2. | College of...
DailyMed - Search Results for Aldehyde Dehydrogenase Inhibitor
Substituted Quinoline Analogs as Aldehyde Dehydrogenase 1A1 (ALDH1A1) Inhibitors | Technology Transfer
Human ALDM(Aldehyde Dehydrogenase, Mitochondrial) ELISA Kit - Circadian Bio-engineering Research Committee Presentation
Mitochondrial aldehyde dehydrogenase 2 alleviates septic liver injury by inhibiting ferroptosis in mouse model]. | Zhonghua...
Potentiating mitochondrial aldehyde dehydrogenase 2 to treat post-infarction heart failure. - Radcliffe Department of Medicine
MEDLINE Data Changes-2021. NLM Technical Bulletin. 2020 Nov-Dec
MOLECULAR CLONING, BACULOVIRUS EXPRESSION, AND TISSUE DISTRIBUTION OF THE ZEBRAFISH ALDEHYDE DEHYDROGENASE 2 | College of...
Müller glial dysfunction during diabetic retinopathy in rats is reduced by the acrolein-scavenging drug, 2-hydrazino-4,6...
Enzymology
Life
Alcohol Dehydrogenase-2*3 Allele Protects Against Alcohol-Related Birth Defects Among African Americans | Journal of...
MedlinePlus: Genetic Conditions: F
LGR5 promotes cancer stem cell traits and chemoresistance in cervical cancer | Cell Death & Disease
Bafilomycin A1 triggers proliferative potential of senescent cancer cells in vitro and in NOD/SCID mice | Oncotarget
Medical Complications: Common Alcohol-Related Concerns | National Institute on Alcohol Abuse and Alcoholism (NIAAA)
NIOSHTIC-2 Search Results - Full View
PA-12-235: Unconventional Roles of Ethanol Metabolizing Enzymes, Metabolites, and Cofactors in Health and Disease (R01)
Sol Genomics Network
indole-containing compound biosynthetic process - Ontology Report - Rat Genome Database
ALDH23
- Acetaldehyde, which is responsible for some of the deleterious effects of ethanol, is further oxidized to acetic acid by aldehyde dehydrogenases (ALDHs), of which mitochondrial ALDH2 is the most efficient. (oregonstate.edu)
- This chemotype demonstrated a high degree of selectivity over other ALDH isozymes (ALDH1B1, ALDH3A1, and ALDH2) and other dehydrogenases (HPGD and HSD17ß4). (nih.gov)
- To observe the ferroptosis triggered by in different pathways during cecal ligation and puncture (CLP)-induced liver injury in septic mice , and to investigate whether mitochondrial aldehyde dehydrogenase 2 (ALDH2) can alleviate sepsis -induced liver injury by inhibiting ferroptosis . (bvsalud.org)
Enzyme10
- Sjögren-Larsson syndrome (SLS) is an inherited neurocutaneous disease caused by mutations in the ALDH3A2 gene that codes for fatty aldehyde dehydrogenase (FALDH), an enzyme involved in lipid metabolism. (nebraska.edu)
- abstract = "Sj{\"o}gren-Larsson syndrome (SLS) is an inherited neurocutaneous disease caused by mutations in the ALDH3A2 gene that codes for fatty aldehyde dehydrogenase (FALDH), an enzyme involved in lipid metabolism. (nebraska.edu)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) in Tissue homogenates, cell lysates and other biological fluids. (jsce-ip.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Aldehyde Dehydrogenase, Mitochondrial (ALDM) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (jsce-ip.com)
- Recent studies on a bacterial version of an enzyme of this pathway, 2-aminomuconate semialdehyde (2-AMS) dehydrogenase (AMSDH), have provided a detailed understanding of the catalytic mechanism and identified residues conserved for muconate semialdehyde recognition and activation. (jbc.org)
- Here, we show that in advanced ovarian cancers NFκB signaling via the RelB transcription factor supports TIC populations by directly regulating the cancer stem-like associated enzyme aldehyde dehydrogenase (ALDH). (nih.gov)
- In humans, molybdenum is a cofactor for three enzyme classes-sulfiteoxidase, aldehyde dehydrogenase, and xanthine oxidase (Kisker et al. (cdc.gov)
- Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH) ( EC 1.2.1.12) is an enzyme that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. (bionity.com)
- Doing so is a multi-step process: First, a liver enzyme called alcohol dehydrogenase transforms the alcohol you've ingested into a compound called acetaldehyde. (thecut.com)
- Next, another enzyme called aldehyde dehydrogenase breaks that down into acetate, which then becomes carbon dioxide and water. (thecut.com)
Mitochondrial aldehyde dehydrogenase2
- Mitochondrial aldehyde dehydrogenase 2 alleviates septic liver injury by inhibiting ferroptosis in mouse model]. (bvsalud.org)
- Potentiating mitochondrial aldehyde dehydrogenase 2 to treat post-infarction heart failure. (ox.ac.uk)
Oxidase2
- The conversion of 6-deoxy penciclovir to penciclovir is catalyzed by aldehyde oxidase. (medscape.com)
- Raloxifene, a potent aldehyde oxidase inhibitor in vitro, could decrease the formation of penciclovir. (medscape.com)
Cytochrome P4501
- The primary enzymes of alcohol metabolism are alcohol dehydrogenase (ADH), cytochrome p450 (CYP2E1) and, to a lesser extent, catalase, enzymes that primarily reside in the cytoplasm, the endoplasmic reticulum (ER) and the peroxisome, respectively. (nih.gov)
Alcohol2
- Ethanol is metabolized to acetaldehyde mainly by the alcohol dehydrogenase pathway and, to a lesser extent, through microsomal oxidation (CYP2E1) and the catalase-H(2)O(2) system. (oregonstate.edu)
- 6. Effects of Gene Polymorphisms, Metabolic Activity, and Content of Alcohol Dehydrogenase and Acetaldehyde Dehydrogenases on prognosis of Hepatocellular Carcinoma Patients. (nih.gov)
ALDH1A11
- Aldehyde dehydrogenase 1 (ALDH1A1) is specifically expressed by a subpopulation of nigral DA neurons located in the ventrolateral(VL) tier of rodent SNpc. (nih.gov)
Neurons1
- In a PD mouse model, scientists targeted dehydrogenase 1A1-positive (ALDH1A1+) nigrostriatal dopaminergic neurons (nDANs)-the dopamine-producing brain cells that experience the most loss in PD, causing severe impairments in motor skill learning and modest reduction in high-speed walking. (nih.gov)
ALDHs1
- Aldehyde dehydrogenase enzymes (ALDHs) have a broad spectrum of biological activities through the oxidation of both endogenous and exogenous aldehydes. (nih.gov)
Antibody5
- Western Blot: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - Analysis of extracts (10ug) from 2 different cell lines by using anti-ALDH3A1 monoclonal antibody at 1:200 dilution. (novusbio.com)
- Immunocytochemistry/ Immunofluorescence: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - Staining of COS7 cells transiently transfected by pCMV6-ENTRY ALDH3A1. (novusbio.com)
- Immunohistochemistry-Paraffin: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - Staining of paraffin-embedded prostate tissue using anti-ALDH3A1 mouse monoclonal antibody. (novusbio.com)
- Flow Cytometry: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - HEK293T cells transfected with either pCMV6-ENTRY ALDH3A1. (novusbio.com)
- Western Blot: Aldehyde Dehydrogenase 3-A1/ALDH3A1 Antibody (OTI1B6) [NBP2-02483] - HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY ALDH3A1 (Right lane) cDNA for 48 hrs and lysed. (novusbio.com)
Catalytic1
- We used activity-based protein profiling to discover that the primary target of DKM 3-42 was the catalytic cysteine in aldehyde dehydrogenase 3A1 (ALDH3A1). (nih.gov)
Vitro1
- Isolated cancer cells with relatively high aldehyde dehydrogenase 1 (ALDH1) activity display in vitro features of CSCs, including capacities for proliferation, self-renewal, and differentiation, resistance to chemotherapy, and expressing CSC surface marker CD133. (nih.gov)
Parkinson's1
- Aldehyde dehydrogenase variation enhances effect of pesticides associated with Parkinson's disease . (snpedia.com)
Tissue1
- Molecular cloning, baculovirus expression, and tissue distribution of the zebrafish aldehyde dehydrogenase 2. (oregonstate.edu)
Cancer1
- Aldehyde dehydrogenase 1 is a tumor stem cell-associated marker in lung cancer. (nih.gov)
Conversion1
- Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses the conversion of glyceraldehyde 3-phosphate as the name indicates. (bionity.com)
Alcohol Dehydrogenase2
- The primary enzymes of alcohol metabolism are alcohol dehydrogenase (ADH), cytochrome p450 (CYP2E1) and, to a lesser extent, catalase, enzymes that primarily reside in the cytoplasm, the endoplasmic reticulum (ER) and the peroxisome, respectively. (nih.gov)
- 3. Effects of Gene Polymorphisms, Metabolic Activity, and Content of Alcohol Dehydrogenase and Acetaldehyde Dehydrogenases on Prognosis of Hepatocellular Carcinoma Patients. (nih.gov)
ALDH4
- Twelve aldehyde dehydrogenase (ALDH) genes have been identified in humans. (nih.gov)
- This chemotype demonstrated a high degree of selectivity over other ALDH isozymes (ALDH1B1, ALDH3A1, and ALDH2) and other dehydrogenases (HPGD and HSD17ß4). (nih.gov)
- The ALDH7A1 gene is a member of the aldehyde dehydrogenase (ALDH) gene family. (medlineplus.gov)
- 10. Expression pattern, ethanol-metabolizing activities, and cellular localization of alcohol and aldehyde dehydrogenases in human large bowel: association of the functional polymorphisms of ADH and ALDH genes with hemorrhoids and colorectal cancer. (nih.gov)
Superfamily2
- Aldehyde dehydrogenase gene superfamily: the 2000 update. (nih.gov)
- Antiquitin, a relatively unexplored member in the superfamily of aldehyde dehydrogenases with diversified physiological functions. (medlineplus.gov)
Enzymes3
- These genes, located on different chromosomes, encode a group of enzymes which oxidizes varieties of aliphatic and aromatic aldehydes. (nih.gov)
- Aldehyde dehydrogenase enzymes (ALDHs) have a broad spectrum of biological activities through the oxidation of both endogenous and exogenous aldehydes. (nih.gov)
- These genes provide instructions for producing enzymes that alter molecules called aldehydes. (medlineplus.gov)
Polymorphism3
- Low Km aldehyde dehydrogenase (ALDH2) polymorphism, alcohol-drinking behavior, and chromosome alterations in peripheral lymphocytes. (nih.gov)
- 11. Genetic polymorphisms of aldehyde dehydrogenase 2, cytochrome p450 2E1 for liver cancer risk in HCV antibody-positive japanese patients and the variations of CYP2E1 mRNA expression levels in the liver due to its polymorphism. (nih.gov)
- 19. Polymorphism of alcohol and aldehyde dehydrogenase genes and alcoholic cirrhosis in Chinese patients. (nih.gov)
Metabolism2
Activity2
- We used activity-based protein profiling to discover that the primary target of DKM 3-42 was the catalytic cysteine in aldehyde dehydrogenase 3A1 (ALDH3A1). (nih.gov)
- 6. Use of an "acetaldehyde clamp" in the determination of low-KM aldehyde dehydrogenase activity in H4-II-E-C3 rat hepatoma cells. (nih.gov)
Cell1
- Comprehensive proteomic profiling of aldehyde dehydrogenases in lung adenocarcinoma cell lines. (nih.gov)