核黄素激酶
| riboflavin kinase 核黄素激酶 | |||||||
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| Thermoplasma acidophilum中的核黄素激酶晶体结构[1] | |||||||
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| 识别码 | |||||||
| EC編號 | 2.7.1.26 | ||||||
| CAS号 | 9032-82-0 | ||||||
| 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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| Riboflavin kinase 核黄素激酶 | |||||||||
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 crystal structure of flavin binding to fad synthetase from thermotoga maritina | |||||||||
| 鑑定 | |||||||||
| 標誌 | Flavokinase | ||||||||
| Pfam | PF01687（旧版） | ||||||||
| InterPro | IPR015865 | ||||||||
| SCOP | 1mrz / SUPFAM | ||||||||
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| Riboflavin kinase 核黄素激酶 | |||||||||||
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| 鑑定 | |||||||||||
| 標誌 | Riboflavin_kinase | ||||||||||
| Pfam | PF01687（旧版） | ||||||||||
| InterPro | IPR015865 | ||||||||||
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核黄素激酶（英語：riboflavin kinase，EC 2.7.1.26）是一个催化以下化学反应的酶：
- ATP + 核黄素 ADP + FMN
该酶催化的反应的底物为ATP和核黄素，产物是ADP和黄素单核苷酸（FMN）。
但是，在古菌核黄素激酶（EC 2.7.1.161）中，常使用CTP而非ATP作为反应底物，催化如下反应：
- CTP + 核黄素 CDP + FMN [2]
核黄素激酶也在许多细菌中发现，具有类似的功能，但存在若干数量的氨基酸不同。
反应
[编辑]
+ XTP →
+ XDP
结构
[编辑]截止2007年底，这类酶中已有14个三级结构被解决，在PDB的登陆代码为1N05，1N06，1N07，1N08，1NB0，1NB9，1P4M，1Q9S，2P3M，2VBS，2VBT，3CTA，2VBU，2VBV。
参考文献
[编辑]- ^ PDB 3CTA; Bonanno, J.B., Rutter, M., Bain, K.T., Mendoza, M., Romero, R., Smith, D., Wasserman, S., Sauder, J.M., Burley, S.K., Almo, S.C. Crystal structure of riboflavin kinase from Thermoplasma acidophilum. 2008.
- ^ Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M. A CTP-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels. Structure. 2007, 12 (12): 1577–90 [2014-01-30]. PMID 18073108. doi:10.1016/j.str.2007.09.027. （原始内容存档于2016-12-27）.
延伸阅读
[编辑]- CHASSY BM, ARSENIS C, MCCORMICK DB. THE EFFECT OF THE LENGTH OF THE SIDE CHAIN OF FLAVINS ON REACTIVITY WITH FLAVOKINASE. J. Biol. Chem. 1965, 240: 1338–40. PMID 14284745.
- GIRI KV, KRISHNASWAMY PR, RAO NA. Studies on plant flavokinase. Biochem. J. 1958, 70 (1): 66–71. PMC 1196627
. PMID 13584303. - KEARNEY EB. The interaction of yeast flavokinase with riboflavin analogues. J. Biol. Chem. 1952, 194 (2): 747–54. PMID 14927668.
- McCormick DB and Butler RC. Substrate specificity of liver flavokinase. Biochim. Biophys. Acta. 1962, 65 (2): 326–332. doi:10.1016/0006-3002(62)91051-X.
- Sandoval FJ, Roje S. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 2005, 280 (46): 38337–45. PMID 16183635. doi:10.1074/jbc.M500350200.
- Solovieva IM, Tarasov KV, Perumov DA. Main physicochemical features of monofunctional flavokinase from Bacillus subtilis. B. Mosc,. Biochemistry. (2): 177–81. PMID 12693963.
- Solovieva IM, Kreneva RA, Leak DJ, Perumov DA. The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon. Microbiology. Pt 1, 145: 67–73. PMID 10206712. doi:10.1099/13500872-145-1-67.
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