D-苏醛糖1-脱氢酶
外观
D-苏醛糖1-脱氢酶 | |||||||||
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识别码 | |||||||||
EC编号 | 1.1.1.122 | ||||||||
CAS号 | 9082-70-6 | ||||||||
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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D-苏醛糖1-脱氢酶(英语:D-threo-aldose 1-dehydrogenase,EC 1.1.1.122(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:
D-苏醛糖1-脱氢酶也能催化L-岩藻糖、D-阿拉伯糖、L-木糖等发生反应,石竹假单胞菌(Pseudomonas caryophylli)和动物的D-苏醛糖1-脱氢酶和还分别表现出对L-葡萄糖和L-阿拉伯糖的活性,并可能受到对氯汞基苯甲酸、对羟基汞基苯甲酸、N-乙基顺丁烯二酰亚胺等有机物质或Cu2+、Hg2+等阳离子的抑制。[1][2][3]
参考文献
[编辑]- ^ Itoh, H.; Miyoshi, T.; Yoshino, A.; Shiragami, K.; Izumori, K. Purification and characterization of L-fucose dehydrogenase from Agrobacterium tumefaciens K-28. J. Ferment. Bioeng. 1994, 77 (1): 100–102. doi:10.1016/0922-338X(94)90218-6.
- ^ Schacter, H.; Sarney, J.; McGuire, E.J.; Roseman, S. Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver. J. Biol. Chem. 1969, 244 (17): 4785–4792 [2013-07-16]. PMID 4309152. (原始内容存档于2019-02-15).
- ^ Tsuji, Y.; Koike, A.; Yamamoto, K.; Tochikura, T. Purification and some properties of L-fucose dehydrogenase from Agrobacterium radiobacter and its application to the assay of bound-fucose in glycoconjugates. Biochim. Biophys. Acta. 1992, 1117 (2): 167–173 [2013-07-16]. PMID 1525177. (原始内容存档于2019-02-15).
- Sasajima KI, Sinskey AJ. Oxidation of L-glucose by a Pseudomonad. Biochim. Biophys. Acta. 1979, 571 (1): 120–6. PMID 40609.
- Schachter H, Sarney J, McGuire EJ, Roseman S. Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver. J. Biol. Chem. 1969, 244 (17): 4785–92. PMID 4309152.