Name | Dehydrogenase, alcohol |
Synonyms | Alcohol dehydrogenase Dehydrogenase, alcohol ADH, NAD+ oxidoreductase Alcohol Dedydrogenase,from Yeast ALCOHOL DEHYDROGENASE extrapure for biochemistry Alcohol Dehydrogenase from Candida parapsilosis Alcohol dehydrogenase-Agarose from baker's yeast (S.cerevisiae) |
CAS | 9031-72-5 |
EINECS | 232-870-4 |
Molecular Formula | n.a. |
Water Solubility | Soluble in water. |
Solubility | H2O: soluble1.0mg/mL, clear to slightly hazy, colorless to faintly yellow |
Appearance | solution |
Color | slightly beige |
Storage Condition | -20°C |
Sensitive | Hygroscopic |
MDL | MFCD00081305 |
Physical and Chemical Properties | Alcohol dehydrogenase is white-like freeze-dried powder, soluble in water, pI5.4, and the optimum pH value is 8.6-9.0 (ethanol oxidation) or 7.0 (aldehyde reduction). Stability: The near-neutral high-concentration enzyme in pure water can exist stably for several days at 5°C, and is unstable in acidic (pH lower than 6.0) and alkaline (pH greater than 8.5) solutions; adding glutathione to dilute solution, Cysteine or serum albumin can increase its stability; freeze-dried powder containing sucrose and phosphate can reduce its activity by 10% after storage for six months at 4°C; crystalline suspension containing phosphate, the activity of storage for six months at 4 ℃ decreased by 40%. Activators include mercaptoethanol, dimercaptoethretol, cysteine and heavy metal chelating agents; inhibitors include heavy metals and sulfhydryl reagents. Enzyme reaction: alcohol + coenzyme I, aldehyde or ketone + reduction coenzyme I. |
WGK Germany | 3 |
RTECS | SZ5999500 |
FLUKA BRAND F CODES | 3-10-21 |
TSCA | Yes |
HS Code | 35079090 |
Reference Show more | 1. Hou Jinglong, Mao with years, Hu Yuan, etc. Study on antioxidant activity of Pueraria lobata and Hovenia dulcis Thunb in vitro [J]. Progress in animal medicine, 2020, 041(002):63-69. 2. [IF = 17.97] Yiying Miu et al."A Type I-F Anti-CRISPR Protein traits the CRISPR-Cas survey Complex by ADP-Ribosylation." Mol Cell. 2020 Nov;80:512 3. [IF = 4.411] SARU Wu et al."Interaction of Soy Protein Isolate sodium with Cyanidin-3-O-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition." Molecules. 2021 Jan;26(6):1721 Note: For some products, we can only provide some information, and we do not guarantee the authority of the information provided, for customer reference and communication purposes only. purpose: storage condition: -20 ℃ absorption coefficient: E1% = 14.6 (water, 280nm) inhibitor: compounds capable of reacting with free thiols include N-alkyl maleimides and iodoacetamides. Inhibitors of zinc chelators include 1, 10-phenanthroline, 8-hydroxyquinoline, 2,2 '-bipyridine, and thiourea. Inhibitors of substrate analogs, including β-nad analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol. KM (ethanol) = 2.1 × 10-3MKM (methanol) = 1.3 × 10-1MKM (isopropanol) = 1.4 × 10-1M |
The relative molecular mass of alcohol dehydrogenase prepared from horse liver is about 73000, and the relative molecular mass of alcohol dehydrogenase prepared from yeast is about 1510 00, all of which contain sulfhydryl groups related to activity. Commercially available are freeze-dried bodies containing sucrose and phosphate (stored at 4 °c, viability may decrease by 10% within 6 months) and crystalline suspensions containing phosphate (stored at 4 °c), viability may decrease by 40% within 6 months.
commonly used diagnostic enzymes. Determination of blood and urine ethanol concentration, clinical diagnosis of diabetes, liver necrosis and alcohol poisoning, decarboxylase assay, NAP and NADH2 qualitative determination.
sealed at 4 °c.
EPA chemical substance information | information provided by: ofmpeb.epa.gov (external link) |
Overview | Alcohol dehydrogenase (ADH) is a zinc-containing enzyme, distribution in the body has a high organ specificity, the most abundant in the liver. In normal physiological metabolism, ADH can catalyze ethanol (alcohol) metabolism. |
Use | Alcohol dehydrogenase can be used for the determination of alcohol content, blood alcohol concentration, clinical for the diagnosis of diabetes, liver necrosis and alcohol poisoning, assay of decarboxylase, qualitative determination of coenzyme I and reduced coenzyme I. The tetramer of alcohol dehydrogenase with a molecular weight of 141kDa contains four identical subunits. The active site of each subunit contains one zinc atom. Each active site also contains two reactive thiols and one histidine residue. Isoelectric point: 5.4-5.8 optimum pH:8.6-9.0 substrate: Yeast alcohol dehydrogenase reacts most easily with ethanol, and its reactivity decreases as the volume of alcohol increases or decreases. The reactivity with branched and secondary alcohols is also very low. KM (ethanol) = 2.1 × 10-3m (methanol) = 1.3 × 10-1m (isopropanol) = 1.4 × 10-1m inhibitor: compound capable of reacting with free thiol group, included are N-alkyl maleimides and iodoacetamide. Inhibitors of zinc chelators include 1, 10-phenanthroline, 8-hydroxyquinoline, 2,2 '-bipyridine, and thiourea. Inhibitors of substrate analogs, including β-nad analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol. Absorption coefficient: E1% = 14.6 (water, 280nm) |
production method | with horse liver as raw material, it is extracted after grinding, and the supernatant is fractionated and precipitated with ammonium sulfate to obtain crude product, after dialysis and recrystallization, the pure product was obtained. |