組氨醇脫氫酶
外觀
組氨醇脫氫酶 | |||||||||
---|---|---|---|---|---|---|---|---|---|
組氨醇脫氫酶(PDB 1k75) | |||||||||
| |||||||||
識別碼 | |||||||||
EC編號 | 1.1.1.23 | ||||||||
CAS號 | 9028-27-7 | ||||||||
數據庫 | |||||||||
IntEnz | IntEnz瀏覽 | ||||||||
BRENDA | BRENDA入口 | ||||||||
ExPASy | NiceZyme瀏覽 | ||||||||
KEGG | KEGG入口 | ||||||||
MetaCyc | 代謝路徑 | ||||||||
PRIAM | 概述 | ||||||||
PDB | RCSB PDB PDBj PDBe PDBsum | ||||||||
基因本體 | AmiGO / EGO | ||||||||
|
組氨醇脫氫酶(英語:histidinol dehydrogenase,EC 1.1.1.23 (頁面存檔備份,存於互聯網檔案館))是一種以NAD+或NADP+為受體、作用於供體CH-OH基團上的氧化還原酶。這種酶能催化以下酶促反應:
組氨醇脫氫酶也能氧化組氨醛。在細菌、真菌和植物細胞中,組氨醇脫氫酶主要負責催化組氨酸生物合成的最後一步化學反應——組氨醇的四電子氧化反應。細菌的組氨醇脫氫酶是一個單鏈多肽;真菌的組氨醇脫氫酶則是一個多功能酶的C端結構域,可以催化組氨酸合成過程中的3個反應;植物的組氨醇脫氫酶則是由細胞核基因編碼的蛋白質前體,需被轉運至葉綠體後才能發揮作用。[1][2][3]
參考文獻
[編輯]- ^ Nagai A, Ward E, Beck J, Tada S, Chang JY, Scheidegger A, Ryals J. Structural and functional conservation of histidinol dehydrogenase between plants and microbes. Proc. Natl. Acad. Sci. U.S.A. May 1991, 88 (10): 4133–4137. PMC 51612 . PMID 2034659.
- ^ Cowan-Jacob SW, Rahuel J, Nagai A, Iwasaki G, Ohta D. Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase. Acta Crystallogr. D Biol. Crystallogr. November 1996, 52 (Pt 6): 1188–90. PMID 15299582. doi:10.1107/S0907444996008396.
- ^ Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M. Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. February 2002, 99 (4): 1859–64. PMC 122284 . PMID 11842181. doi:10.1073/pnas.022476199.
- Adams E. Enzymatic synthesis of histidine from histidinol. J. Biol. Chem. 1954, 209 (2): 829–846. PMID 13192138.
- Adams E. L-Histidinal, a biosynthetic precursor of histidine. J. Biol. Chem. 1955, 217 (1): 325–344. PMID 13271397.
- Yourno J, InoI. Purification and crystallization of histidinol dehydrogenase fromSalmonella typhimurium LT-2. J. Biol. Chem. 1968, 243 (12): 3273–6. PMID 4872177.
- Loper JC. Histidinol dehydrogenase from Salmonella typhimurium Crystallization and composition studies. J. Biol. Chem. 1968, 243 (12): 3264–72. PMID 4872176.