生物源
equine
重組細胞
expressed in E. coli
描述
Isozyme E sequence
形狀
lyophilized powder
比活性
≥0.5 U/mg
顏色
white
light yellow
pH值
7
溶解度
water: 5 mg/mL
應用
life science and biopharma
儲存溫度
−20°C
基因資訊
equine ... ADH1(111772995)
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一般說明
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.
應用
Alcohol Dehydrogenase equine has been used in in vitro alcohol dehydrogenase (Adh) assay.
生化／生理作用
乙醇脱氢酶催化醇向醛的氧化转化。它具有同二聚体结构，其在 C 端和 N 端催化结构域具有辅酶结合结构域。它的活性位点位于域间裂缝处。NAD+ 在活性位点的结合会导致构象变化，从而形成醇底物的结合位点。
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.
單位定義
在 pH 7.0 和 30°C 下，1 U 相当于每分钟还原 1 μmol 苯甲醛所需的酶量。
訊號詞
Danger
危險聲明
危險分類
Resp. Sens. 1
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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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