추천 제품
생물학적 소스
Saccharomyces cerevisiae
Quality Level
양식
lyophilized powder (contains buffer salts)
특이 활성도
≥300 units/mg protein
분자량
Mw 141-151 kDa
정제법
crystallization
저장 조건
(Keep container tightly closed in a dry and well-ventilated place.)
환경친화적 대안 제품 특성
Waste Prevention
Design for Energy Efficiency
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sustainability
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색상
white to light yellow-brown, Light brown
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관련 카테고리
일반 설명
Research area: Neuroscience
Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.
Yeast alcohol dehydrogenase 1 (ADH1) belongs to the family of zinc-containing alcohol dehydrogenases. It is a homotetramer with each subunit containing one catalytic domain and coenzyme-binding domain.
애플리케이션
Alcohol dehydrogenase has been used along with lactic dehydrogenase for the enzymatic reduction of acetaldehyde using sodium(R,S)-[2-3H] lactate. It has also been used to study the inhibitory effect of zinc-chelated silymarin flavonolignans on yeast alcohol dehydrogenase.
Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of NAD using alcohol dehydrogenase after preremoval of the aldehyde group.
Ethanol concentration can be determined colorimentrically by monitoring the enzymatic reduction of NAD using alcohol dehydrogenase after preremoval of the aldehyde group.
생화학적/생리학적 작용
ADH (alcohol dehydrogenase) is one of the first enzymes to be isolated and purified. NAD+ is its coenzyme. Three isozymes of yeast ADH, that is, yeast alcohol dehydrogenase-1, 2 and 3 (YADH-1, -2, -3) have been identified. YADH-1 is expressed during anaerobic fermentation, YADH-2 is expressed in the cytoplasm and YADH-3 is localized to the mitochondria. A 141kDa tetramer containing 4 equal subunits. The active site of each subunit contains a zinc atom. Each active site also contains 2 reactive sulfhydryl groups and a histidine residue.
Isoelectric point: 5.4-5.8
Optimal pH: 8.6-9.0
Substrates: Yeast ADH is most active with ethanol and its activity decreases as the size of the alcohol increases or decreases. Branched chain alcohols and secondary alcohols also have very low activity.
KM (ethanol) = 2.1 × 10-2 M
KM (methanol = 1.3 × 10-1 M
KM (isopropanol) = 1.4 × 10-1 M
Inhibitors: Compounds that react with free sulfhydryls, including N-alkylmaleimides and iodoacetamide.
Zinc chelator inhibitors, including 1,10-phenanthroline,
8-hydroxyquinoline, 2,2′-dipyridyl, and thiourea.
Substrate analogue inhibitors, including β-NAD analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol.
Extinction Coefficient: E1% = 14.6 (water, 280 nm)
Isoelectric point: 5.4-5.8
Optimal pH: 8.6-9.0
Substrates: Yeast ADH is most active with ethanol and its activity decreases as the size of the alcohol increases or decreases. Branched chain alcohols and secondary alcohols also have very low activity.
KM (ethanol) = 2.1 × 10-2 M
KM (methanol = 1.3 × 10-1 M
KM (isopropanol) = 1.4 × 10-1 M
Inhibitors: Compounds that react with free sulfhydryls, including N-alkylmaleimides and iodoacetamide.
Zinc chelator inhibitors, including 1,10-phenanthroline,
8-hydroxyquinoline, 2,2′-dipyridyl, and thiourea.
Substrate analogue inhibitors, including β-NAD analogs, purine and pyrimidine derivatives, chloroethanol, and fluoroethanol.
Extinction Coefficient: E1% = 14.6 (water, 280 nm)
Yeast alcohol dehydrogenase 1 (YADH1) catalyzes the conversion of acetaldehyde to ethanol during glucose fermentation pathway. It is also implicated in the production of alcohol from amino acid breakdown via the Ehrlich pathway.
주의사항
Contains bound β-NAD and β-NADH and is not suitable for the recycling microassay of β-NAD and β-NADH. If you require ADH for this purpose, see Catalog No. A3263.
단위 정의
One unit will convert 1.0 μmole of ethanol to acetaldehyde per min at pH 8.8 at 25 °C.
물리적 형태
Solids containing ≤ 2% citrate buffer salts
제조 메모
Dissolves in water at a concentration of 1 mg/mL to form a clear to slightly hazy, colorless to faintly yellow colored solution.
항체
제품 번호
설명
가격
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
Stereospecificity of the oxidation of ethanol by catalase.
R J Corrall et al.
The Journal of biological chemistry, 249(10), 3181-3182 (1974-05-25)
Václav Tvrdý et al.
Nutrients, 13(12) (2021-12-29)
Silymarin is known for its hepatoprotective effects. Although there is solid evidence for its protective effects against Amanita phalloides intoxication, only inconclusive data are available for alcoholic liver damage. Since silymarin flavonolignans have metal-chelating activity, we hypothesized that silymarin may
Mark D Redwood et al.
FEMS microbiology letters, 278(1), 48-55 (2007-11-13)
Escherichia coli can perform at least two modes of anaerobic hydrogen metabolism and expresses at least two types of hydrogenase activity. Respiratory hydrogen oxidation is catalysed by two 'uptake' hydrogenase isoenzymes, hydrogenase -1 and -2 (Hyd-1 and -2), and fermentative
Savarimuthu Baskar Raj et al.
Biochemistry, 53(36), 5791-5803 (2014-08-27)
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray
Cheol Woong Ha et al.
Nucleic acids research, 42(13), 8486-8499 (2014-07-02)
In Saccharomyces cerevisiae, the stability of highly repetitive rDNA array is maintained through transcriptional silencing. Recently, a β-1,3-glucanosyltransferase Gas1 has been shown to play a significant role in the regulation of transcriptional silencing in S. cerevisiae. Here, we show that
프로토콜
To measure alcohol dehydrogenase activity, this assay uses β-nicotinamide adenine dinucleotide phosphate and a continuous spectrophotometric rate determination at 340 nm.
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