55689
Alcohol Dehydrogenase equine
recombinant, expressed in E. coli, ≥0.5 U/mg
Sinonimo/i:
ADH
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About This Item
Prodotti consigliati
Origine biologica
equine
Livello qualitativo
Ricombinante
expressed in E. coli
Descrizione
Isozyme E sequence
Forma fisica
lyophilized powder
Attività specifica
≥0.5 U/mg
Colore
white
light yellow
pH
7
Solubilità
water: 5 mg/mL
applicazioni
life science and biopharma
Temperatura di conservazione
−20°C
Informazioni sul gene
equine ... ADH1(111772995)
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Descrizione generale
Research Area: Neuroscience
Alcohol dehydrogenase is a zinc metalloprotein that forms five classes of isoenzymes through the dimerization of eight different subunits.
Alcohol dehydrogenase is a zinc metalloprotein that forms five classes of isoenzymes through the dimerization of eight different subunits.
Applicazioni
Alcohol Dehydrogenase equine has been used in in vitro alcohol dehydrogenase (Adh) assay.
Azioni biochim/fisiol
Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain. The active site is located at the interdomain cleft. Binding of NAD+ in the active site causes conformational changes which create the binding site for the alcohol substrate.
Horse liver alcohol dehydrogenase (HL-ADH) is an enzyme with broad specificity, capable of catalyzing the reversible oxidation of a wide variety of primary and secondary alcohols to form their corresponding aldehydes and ketones. Moreover, alcohol dehydrogenase can oxidize ethanol while simultaneously reducing nicotinamide adenine dinucleotide (NAD+) to NADH. Previous studies have demonstrated that ADH and ALDH variants can influence alcohol dependence. Additionally, the ADH genotype has been linked to lacunar infarction and neuropsychiatric diseases.
Definizione di unità
1 U corresponds to the amount of enzyme which reduces 1 μmol benzaldehyde per minute at pH 7.0 and 30 °C.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Resp. Sens. 1
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
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Ioanna A Gorbunova et al.
The journal of physical chemistry. B, 125(34), 9692-9707 (2021-08-20)
The dynamics of polarized fluorescence in NADH in alcohol dehydrogenase (ADH) in buffer solution has been studied using the TCSPC spectroscopy. A global fit procedure was used for determination of the fluorescence parameters from experiment. The interpretation of the results
Steven Hayward et al.
Biophysical journal, 91(5), 1823-1831 (2006-05-23)
Horse liver alcohol dehydrogenase is a homodimer, the protomer having a coenzyme-binding domain and a catalytic domain. Using all available x-ray structures and 50 ns of molecular dynamics simulations, we investigated the mechanism of NAD+-induced domain closure. When the well-known
Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution.
H Eklund et al.
Journal of molecular biology, 146(4), 561-587 (1981-03-15)
F Colonna-Cesari et al.
The Journal of biological chemistry, 261(32), 15273-15280 (1986-11-15)
A study of the hinge bending mode in the enzyme liver alcohol dehydrogenase is made by use of empirical energy functions. The enzyme is a dimer, with each monomer composed of a coenzyme binding domain and a catalytic domain with
H Eklund et al.
Biochemistry, 23(25), 5982-5996 (1984-12-04)
The binding of NAD to liver alcohol dehydrogenase has been studied in four different ternary complexes by using crystallographic methods. These complexes crystallize isomorphously in a triclinic crystal form which contains the whole dimer of the enzyme in the asymmetric
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