查看“︁组氨醇脱氢酶”︁的源代码

{{enzyme
| Name = 组氨醇脱氢酶
| Systematic_name = L-histidinol:NAD<sup>+</sup> oxidoreductase
| Acronym = HDH
| Other_names = L-histidinol dehydrogenase
| EC_number = 1.1.1.23
| CAS_number = 9028-27-7 | IUBMB_EC_number = 1/1/1/23 | GO_code = 0004399 | image = PDB 1k75 EBI.jpg
| width = 
| caption = 组氨醇脱氢酶（[[蛋白质数据库|PDB]] 1k75）
}}
'''组氨醇脱氢酶'''（{{lang-en|histidinol dehydrogenase}}，[[EC编号|EC]] [http://enzyme.expasy.org/EC/1.1.1.23 1.1.1.23] {{Wayback|url=http://enzyme.expasy.org/EC/1.1.1.23 |date=20190505113348 }}）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-组氨醇]] + 2 [[烟酰胺腺嘌呤二核苷酸|NAD<sup>+</sup>]] + [[水|H<sub>2</sub>O]] <math>\rightleftharpoons</math> [[L-组氨酸]] + 2 NADH + 3 [[氢离子|H<sup>+</sup>]]

组氨醇脱氢酶也能氧化[[组氨醛]]。在[[细菌]]、[[真菌]]和[[植物]][[细胞]]中，组氨醇脱氢酶主要负责催化[[组氨酸]][[生物合成]]的最后一步[[化学反应]]——[[组氨醇]]的四[[电子]][[氧化反应]]。细菌的组氨醇脱氢酶是一个单链[[多肽]]；真菌的组氨醇脱氢酶则是一个多功能酶的C端[[结构域]]，可以催化组氨酸合成过程中的3个反应；植物的组氨醇脱氢酶则是由[[细胞核]][[基因]]编码的[[蛋白质前体]]，需被转运至[[叶绿体]]后才能发挥作用。<ref>{{cite journal | author = Nagai A, Ward E, Beck J, Tada S, Chang JY, Scheidegger A, Ryals J | title = Structural and functional conservation of histidinol dehydrogenase between plants and microbes | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 10 | pages = 4133-4137 | pmid = 2034659 | pmc = 51612 | doi = | url = |date=May 1991}}</ref><ref name="pmid15299582">{{cite journal | author = Cowan-Jacob SW, Rahuel J, Nagai A, Iwasaki G, Ohta D | title = Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase | journal = Acta Crystallogr. D Biol. Crystallogr. | volume = 52 | issue = Pt 6 | pages = 1188–90 | pmid = 15299582 | doi = 10.1107/S0907444996008396 | url = |date=November 1996}}</ref><ref name="pmid11842181">{{cite journal | author = Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M | title = Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 4 | pages = 1859–64 | pmid = 11842181 | pmc = 122284 | doi = 10.1073/pnas.022476199 | url = |date=February 2002}}</ref>

== 参考文献 ==
{{refbegin}}
{{reflist}}
* {{cite journal | author = Adams E | year = 1954 | title = Enzymatic synthesis of histidine from histidinol | url = https://archive.org/details/sim_journal-of-biological-chemistry_1954-08_209_2/page/829 | journal = J. Biol. Chem.  | volume = 209 | pages = 829–846 | pmid=13192138 | issue = 2}}
* {{cite journal | author = Adams E | year = 1955 | title = L-Histidinal, a biosynthetic precursor of histidine | journal = J. Biol. Chem.  | volume = 217| pages = 325–344 | pmid=13271397 | issue = 1}}
* {{cite journal | author = Yourno J, InoI | year = 1968 | title = Purification and crystallization of histidinol dehydrogenase fromSalmonella typhimurium LT-2 | journal = J. Biol. Chem.  | volume = 243 | pages = 3273–6  | pmid = 4872177 | issue = 12 }}
* {{cite journal | author = Loper JC | year = 1968 | title = Histidinol dehydrogenase from Salmonella typhimurium Crystallization and composition studies | journal = J. Biol. Chem.  | volume = 243 | pages = 3264–72  | pmid = 4872176 | issue = 12 }}
{{refend}}

{{EC 1.1}}

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