肉碱3-脱氢酶
外观
肉碱3-脱氢酶 | |||||||||
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识别码 | |||||||||
EC编号 | 1.1.1.108 | ||||||||
CAS号 | 9045-45-8 | ||||||||
数据库 | |||||||||
IntEnz | IntEnz浏览 | ||||||||
BRENDA | BRENDA入口 | ||||||||
ExPASy | NiceZyme浏览 | ||||||||
KEGG | KEGG入口 | ||||||||
MetaCyc | 代谢路径 | ||||||||
PRIAM | 概述 | ||||||||
PDB | RCSB PDB PDBj PDBe PDBsum | ||||||||
基因本体 | AmiGO / EGO | ||||||||
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肉碱3-脱氢酶(英语:carnitine 3-dehydrogenase,EC 1.1.1.108 (页面存档备份,存于互联网档案馆)),是一种以NAD+或NADP+为受体、作用于供体CH-OH基团上的氧化还原酶。这种酶能催化以下酶促反应:
上述反应是L-肉碱生物降解过程的第一步,[1]该反应被用于L-肉碱生产以及量化地鉴定生物体液中L-肉碱的水平。[2]从根瘤菌(Rhizobium sp.)和半透明黄单胞菌(Xanthomonas translucens)细胞中分别提取出的肉碱3-脱氢酶Rs-CDH和Xt-CDH的相对分子质量分别为50kDa和37kDa,它们的初级结构与3-羟酰辅酶A脱氢酶有高度的相似性。[3]
参考文献
[编辑]- ^ Hanschmann H, Ehricht R, Kleber HP. Purification and properties of L(-)-carnitine dehydrogenase from Agrobacterium sp.. Biochim Biophys Acta. Jun 4, 1996, 1290 (2): 177–183. PMID 8645721.
- ^ Clemens Uanschou, Roswitha Frieht, and Fritz Pittner. What to Learn from a Comparative Genomic Sequence Analysis of L-Carnitine Dehydrogenase. Monatsh. Chem. 2005, 136 (8): 1365–1381. doi:10.1007/s00706-005-0331-x.[永久失效链接]
- ^ Arima J, Uesumi A, Mitsuzumi H, Mori N. Biochemical characterization of L-carnitine dehydrogenases from izobium sp. and Xanthomonas translucens.. Biosci Biotechnol Biochem. 2010, 74 (6): 1237–1242. PMID 20530902.
- Aurich H, Kleber HP, Sorger H, Tauchert H. Purification and properties of carnitine dehydrogenase from Pseudomonas aeruginosa. Eur. J. Biochem. 1968, 6 (2): 196–201. PMID 4302217. doi:10.1111/j.1432-1033.1968.tb00437.x.
- Schopp W, Sorger H, Kleber HP, Aurich H. Kinetic studies of the reaction mechanism of carnitine dehydrogenase of Pseudomonas aeruginosa. Eur. J. Biochem. 1969, 10 (1): 56–60. PMID 4310279. doi:10.1111/j.1432-1033.1969.tb00654.x.