生物来源
Porcine brain
质量水平
方案
≥85%
表单
powder
溶解性
water: 50 mg/mL, clear, colorless to faintly yellow
储存温度
−20°C
SMILES字符串
CC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](COP([O-])(=O)OP(O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
InChI
1S/C22H28N6O14P2/c1-10(29)11-3-2-4-27(5-11)21-17(32)15(30)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(31)18(33)22(41-13)28-9-26-14-19(23)24-8-25-20(14)28/h2-5,8-9,12-13,15-18,21-22,30-33H,6-7H2,1H3,(H3-,23,24,25,34,35,36,37)/t12-,13-,15-,16-,17-,18-,21-,22-/m1/s1
InChI key
KPVQNXLUPNWQHM-RBEMOOQDSA-N
一般描述
3-乙酰吡啶腺嘌呤二核苷酸是一种结晶固体。3-乙酰吡啶腺嘌呤二核苷酸在各种交替氧化的酶活动中是一种突出的电子转运体。 APAD比NAD具有更显著的氧化电势。 NAD类似物APAD在电化学上比真正的NAD更有效地还原，其还原产物的稳定性也显著高于NADH。 在与NADH或NADPH的转氢化过程中，APAD也作为质子受体起作用。
应用
许多分子使用3-乙酰吡啶腺嘌呤二核苷酸作为信号分子、辅因子或底物。各种脱氢酶过程使用APAD代替NAD作为氢接受辅因子。 氧化磷酸化可以用ADAP进行研究。 ADAP也可以用作合适的底物。
生化/生理作用
APAD是一种NAD类似物，具有比NAD高的氧化电位。在许多脱氢酶反应中可代替 NAD 作为受氢辅助因子；例如， 弓形虫、华支睾吸虫、 和 疟原虫 中的乳酸脱氢酶、细菌硫辛酰胺脱氢酶以及哺乳动物脱氢酶。在与 NADH 或 NADPH 的各种转氢反应中也可作为质子受体。
其他说明
NAD 类似物
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
C Dando et al.
Molecular and biochemical parasitology, 118(1), 23-32 (2001-11-13)
Toxoplasma gondii differentially expresses two forms of lactate dehydrogenase in tachyzoites and bradyzoites, respectively, designated LDH1 and LDH2. Previously it was demonstrated that LDH1 and LDH2 share a unique structural feature with LDH from the malarial parasite Plasmodium falciparum (pLDH)
A model of Plasmodium falciparum lactate dehydrogenase and its implications for the design of improved antimalarials and the enhanced detection of parasitaemia.
R B Sessions et al.
Protein engineering, 10(4), 301-306 (1997-04-01)
N V Zakharova
Biochemistry. Biokhimiia, 67(6), 651-661 (2002-07-20)
The kinetics of the NADH-->3;-acetylpyridine adenine dinucleotide (APAD+) transhydrogenase reaction (DD-reaction) catalyzed by different preparations of mitochondrial NADH-dehydrogenase (submitochondrial particles (SMP), purified Complex I, and three-subunit fragment of Complex I (FP)) have been studied. Complex I (in SMP or in
T Bizouarn et al.
European journal of biochemistry, 267(11), 3281-3288 (2000-05-29)
Nicotinamide nucleotide transhydrogenase from Escherichia coli is composed of two subunits, the alpha and the beta subunits, each of which contains a hydrophilic domain, domain I and III, respectively, as well as several transmembrane helices, collectively denoted domain II. The
Guang Yang et al.
Parasitology research, 99(1), 55-64 (2006-02-16)
From a Clonorchis sinensis adult worm cDNA library, we isolated a cDNA clone encoding a novel lactate dehydrogenase (LDH) gene which encoded a putative protein with a predicted molecular weight of 35.6 kDa. The optimum pH and temperature for the
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