核黄素激酶

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riboflavin kinase
核黄素激酶
Riboflavkinase.png
Thermoplasma acidophilum中的核黄素激酶晶体结构[1]
识别码
EC编号 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 PDBe PDBsum
基因本体 AmiGO / EGO
Riboflavin kinase
核黄素激酶
PDB 1s4m EBI.jpg
crystal structure of flavin binding to fad synthetase from thermotoga maritina
鉴定
标志 Flavokinase
Pfam(蛋白家族查询站) PF01687
InterPro(蛋白数据整合站) IPR015865
SCOP(蛋白结构分类数据站) 1mrz
Riboflavin kinase
核黄素激酶
鉴定
标志 Riboflavin_kinase
Pfam(蛋白家族查询站) PF01687
InterPro(蛋白数据整合站) IPR015865

核黄素激酶英语:riboflavin kinaseEC 2.7.1.26)是一个催化以下化学反应的酶:

ATP + 核黄素 \rightleftharpoons ADP + FMN

酶催化的反应的底物ATP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 \rightleftharpoons 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。

目录

反应

核黄素 + XTP → FMN + XDP

Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase (EC 2.7.1.26), which converts it into FMN, and FAD synthetase (EC 2.7.7.2), which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme,[3] the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family.[4] The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases.[5]

This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:riboflavin 5'-phosphotransferase. This enzyme is also called flavokinase. This enzyme participates in riboflavin metabolism.

结构

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1N051N061N071N081NB01NB91P4M1Q9S2P3M2VBS2VBT3CTA2VBU2VBV

参考文献

  1. 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. 
  2. 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. doi:10.1016/j.str.2007.09.027. PMID 18073108. 
  3. Osterman AL, Zhang H, Zhou Q, Karthikeyan S. Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. Biochemistry. 2003, 42 (43): 12532–8. doi:10.1021/bi035450t. PMID 14580199. 
  4. Galluccio M, Brizio C, Torchetti EM, Ferranti P, Gianazza E, Indiveri C, Barile M. Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase. Protein Expr. Purif.. 2007, 52 (1): 175–81. doi:10.1016/j.pep.2006.09.002. PMID 17049878. 
  5. Srinivasan N, Krupa A, Sandhya K, Jonnalagadda S. A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer. Trends Biochem. Sci.. 2003, 28 (1): 9–12. doi:10.1016/S0968-0004(02)00009-9. PMID 12517446. 

延伸阅读

  • 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. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC1196627/ Studies on plant flavokinase]. Biochem. J.. 1958, 70 (1): 66–71. PMID 13584303. PMC 1196627. 
  • 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. doi:10.1074/jbc.M500350200. PMID 16183635. 
  • 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. doi:10.1099/13500872-145-1-67. PMID 10206712. 

此条目包含有源于Pfam以及InterPro的属于公有领域的文本 IPR015865

参考来源

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