查看“︁L-艾杜糖醇2-脱氢酶”︁的源代码

{{DISPLAYTITLE:<small>L</small>-艾杜糖醇2-脱氢酶}}
{{enzyme
| Name = <small>L</small>-艾杜糖醇2-脱氢酶
| Systematic_name = <small>L</small>-iditol:NAD<sup>+</sup> 2-oxidoreductase
| Acronym = 
| Other_names = polyol dehydrogenase; sorbitol dehydrogenase; <small>L</small>-iditol:NAD<sup>+</sup> 5-oxidoreductase; <small>L</small>-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; <small>L</small>-iditol:NAD<sup>+</sup> oxidoreductase; NAD<sup>+</sup>-dependent sorbitol dehydrogenase; NAD<sup>+</sup>-sorbitol dehydrogenase
| EC_number = 1.1.1.14
| CAS_number = 9028-21-1 
| IUBMB_EC_number = 1/1/1/14 
| GO_code = 0003939 
| image = 1pl8.jpg
| width = 270
| caption = 
}}
'''<small>L</small>-艾杜糖醇2-脱氢酶'''（{{lang-en|<small>L</small>-iditol 2-dehydrogenase}}，[[EC编号|EC]] [http://enzyme.expasy.org/EC/1.1.1.14 1.1.1.14] {{Wayback|url=http://enzyme.expasy.org/EC/1.1.1.14 |date=20200228193854 }}）是一种以[[烟酰胺腺嘌呤二核苷酸|NAD<sup>+</sup>]]或[[烟酰胺腺嘌呤二核苷酸磷酸|NADP<sup>+</sup>]]为[[受体 (生物化学)|受体]]、作用于[[供体]][[次甲基|CH]]-[[羟基|OH]][[基团]]上的[[氧化还原酶]]。这种[[酶]]能[[催化]]以下[[酶促反应]]：

:[[L-艾杜糖醇|<small>L</small>-艾杜糖醇]] + [[烟酰胺腺嘌呤二核苷酸|NAD<sup>+</sup>]] <math>\rightleftharpoons</math> [[L-山梨糖|<small>L</small>-山梨糖]] + NADH + [[氢离子|H<sup>+</sup>]]

<small>L</small>-艾杜糖醇2-脱氢酶广泛存在于各种[[生物]][[细胞]]中，现已在[[古菌]]、[[细菌]]、[[真菌]]、[[植物]]和[[动物]]细胞中发现了这种酶。<small>L</small>-艾杜糖醇2-脱氢酶可以作用于包括<small>L</small>-艾杜糖醇、[[D-葡萄糖醇|<small>D</small>-葡萄糖醇]]、[[D-木糖醇|<small>D</small>-木糖醇]]和[[D-半乳糖醇|<small>D</small>-半乳糖醇]]（<small>D</small>-卫矛醇）等[[糖醇]][[分子]]。不同生物不同[[组织 (生物学)|组织]]中的<small>L</small>-艾杜糖醇2-脱氢酶对不同的[[底物]]具有特异性。<small>L</small>-艾杜糖醇2-脱氢酶对能特异性识别NAD<sup>+</sup>，但不能利用NADP<sup>+</sup>。这种酶主要参与[[果糖]]和[[甘露糖]]之间的转化过程。

== 参考文献 ==
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{{reflist}}
* {{cite journal | author = Bailey JP, Renz C and McGuinness ET | year = 1981 | title = Sorbitol dehydrogenase from horse liver: purification, characterization and comparative properties | journal = Comp. Biochem. Physiol. | volume = 69B | pages = 909–914 }}
* {{cite journal | author = Burnell JN, Holmes RS | year = 1983 | title = Purification and properties of sorbitol dehydrogenase from mouse liver | journal = Int. J. Biochem. | volume = 15 | pages = 507–11  | pmid = 6852349 | doi = 10.1016/0020-711X(83)90124-6 | issue = 4 }}
* {{cite journal | author = Leissing N, McGuinness ET | year = 1978 | title = Rapid affinity purification and properties of rat liver sorbitol dehydrogenase | journal = Biochim. Biophys. Acta. | volume = 524 | pages = 254–61 | pmid = 667078 | issue = 2 }}
* {{cite journal | author = Negm FB and Loescher WH | year = 1979 | title = Detection and Characterization of Sorbitol Dehydrogenase from Apple Callus Tissue | url = https://archive.org/details/sim_plant-physiology_1979-07_64_1/page/n74 | journal = Plant Physiol. | volume = 64 | pages = 69–73 | doi = 10.1104/pp.64.1.69 | pmid=16660917 | issue = 1 | pmc = 543026}}
* {{cite journal | author = O'Brien MM, Schofield PJ, Edwards MR | year = 1983 | title = Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase | journal = Biochem. J. | volume = 211 | pages = 81–90  | pmid = 6870831 | issue = 1 | pmc = 1154331 }}
{{refend}}

{{EC 1.1}}

[[Category:EC 1.1.1]]
[[Category:NADH依赖性酶]]
[[Category:已知结构的酶]]