推荐产品
应用
醛缩酶用于将 1，6-二磷酸果糖转化为磷酸二羟丙酮和 3-磷酸甘油醛。来自家兔肌肉的醛缩酶已用于 DHAP C3 的立体特异性去质子化 。产品 A2714 基本上不含硫酸盐，含有柠檬酸盐缓冲盐。
生化/生理作用
醛缩酶可参与到糖原异生、卡尔文循环和糖酵解。来自兔肌肉中的醛缩酶属于I类醛缩酶，可形成共价席夫碱中间体。醛缩酶的活性位点在 α/β8 桶型褶皱中央。
单位定义
在 pH 7.4、25 °C 条件下，一个单位每分钟将 1.0 μmol 1,6-二磷酸果糖转化为磷酸二羟丙酮和 3-磷酸甘油醛。
外形
基本不含硫酸盐的柠檬酸盐缓冲盐
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
动植物源性产品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Xiaochen He et al.
Journal of cellular physiology, 237(8), 3317-3327 (2022-05-28)
Hypertension is an important risk factor in the pathogenesis of diastolic dysfunction. Growing evidence indicates that glucose metabolism plays an essential role in diastolic dysfunction. TP53-induced glycolysis and apoptosis regulator (TIGAR) has been shown to regulate glucose metabolism and heart
Clotilde LowKam et al.
The Journal of biological chemistry, 285(27), 21143-21152 (2010-04-30)
Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the reversible cleavage of four
Bang Shen et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(9), 3567-3572 (2014-02-20)
Gliding motility and host-cell invasion by apicomplexan parasites depend on cell-surface adhesins that are translocated via an actin-myosin motor beneath the membrane. The current model posits that fructose-1,6-bisphosphate aldolase (ALD) provides a critical link between the cytoplasmic tails of transmembrane
N C Cross et al.
Lancet (London, England), 335(8685), 306-309 (1990-02-10)
The molecular basis of hereditary fructose intolerance (HFI) was studied in 50 subjects (41 pedigrees, 82 apparently independent mutant alleles of aldolase B) by direct analysis of aldolase B genes amplified by means of the polymerase chain reaction. The mutation
Tiia Kittilä et al.
Chembiochem : a European journal of chemical biology, 17(7), 576-584 (2016-01-12)
Nonribosomal peptide synthetases (NRPSs) produce many important and structurally complex natural products. Because of their architectures, reprogramming NRPSs has long been attempted to access new bioactive compounds. However, detailed characterization of NRPS catalysis and substrate selectivity by adenylation (A) domains
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