Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/16 12:21:36」(JST)
[Wiki en表示]
| Flavoprotein |
|
the fmn binding protein athal3
|
| Identifiers |
| Symbol |
Flavoprotein |
| Pfam |
PF02441 |
| InterPro |
IPR003382 |
| SCOP |
1e20 |
| SUPERFAMILY |
1e20 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).
Flavoproteins are involved in a wide array of biological processes, including, but by no means limited to, bioluminescence, removal of radicals contributing to oxidative stress, photosynthesis, DNA repair, and apoptosis. The spectroscopic properties of the flavin cofactor make it a natural reporter for changes occurring within the active site; this makes flavoproteins one of the most-studied enzyme families.
Contents
- 1 Discovery
- 2 Examples
- 3 See also
- 4 References
- 5 External links
Discovery
The first mention of a flavoprotein in the scientific literature dates back to 1879, when the work on the composition of cow’s milk resulted in the isolation of a bright-yellow pigment, that we now know as flavin, but termed lactochrome at the time. By the early 1930s, this same pigment had been isolated from a range of sources, and recognised as a component of the vitamin B complex. Its structure was determined almost simultaneously by two groups in 1934, and given the name riboflavin, derived from the ribityl side chain and yellow colour of the conjugated ring system.[1]
The first evidence for the requirement of flavin as an enzyme cofactor came in 1935. Hugo Theorell and coworkers showed that a bright-yellow-coloured yeast protein, identified previously as essential for cellular respiration, could be separated into apoprotein and a bright-yellow pigment. Neither apoprotein nor pigment alone could catalyse the oxidation of NADH, but mixing of the two restored the enzyme activity. However, replacing the isolated pigment with riboflavin did not restore enzyme activity, despite their being indistinguishable under spectroscopy. This led to the discovery that the protein studied required not riboflavin but flavin mononucleotide to be catalytically active[1][2]
Similar experiments with D-amino acid oxidase[3] led to the identification of flavin adenine dinucleotide (FAD) as a second form of flavin utilised by enzymes.[4]
Examples
The flavoprotein family contains a diverse range of enzymes, including:
- Epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyses the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond.[5]
- The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid.[6]
- Phenylacrylic acid decarboxylase EC 4.1.1.-, and enzyme which confers resistance to cinnamic acid in yeast[7]
See also
References
- ^ a b Massey, V (2000). "The chemical and biological versatility of riboflavin". Biochemical Society transactions 28 (4): 283–96. PMID 10961912.
- ^ Theorell, H. (1935). "Preparation in pure state of the effect group of yellow enzymes". Biochemische Zeitschrift 275: 344–6.
- ^ Warburg, O.; Christian, W. (1938). "Isolation of the prosthetic group of the amino acid oxydase". Biochemische Zeitschrift 298: 150–68.
- ^ Christie, S. M. H.; Kenner, G. W.; Todd, A. R. (1954). "Nucleotides. Part XXV. A synthesis of flavin?adenine dinucleotide". Journal of the Chemical Society: 46–52. doi:10.1039/JR9540000046.
- ^ Kupke, T; Stevanović, S; Sahl, H. G.; Götz, F (1992). "Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin". Journal of bacteriology 174 (16): 5354–61. PMC 206373. PMID 1644762.
- ^ Daniel, R.A.; Errington, J. (1993). "Cloning, DNA Sequence, Functional Analysis and Transcriptional Regulation of the Genes Encoding Dipicolinic Acid Synthetase Required for Sporulation in Bacillus subtilis". Journal of Molecular Biology 232 (2): 468–83. doi:10.1006/jmbi.1993.1403. PMID 8345520.
- ^ Clausen, Monika; Lamb, Christopher J.; Megnet, Roland; Doerner, Peter W. (1994). "PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae". Gene 142 (1): 107–12. doi:10.1016/0378-1119(94)90363-8. PMID 8181743.
External links
- The menu "science" of the program STRAP provides A comprehensive collection of all flavo-proteins with known 3D-structure. It compares the protein structures to elucidate phylogenetic relationships.
|
Protein: flavoproteins
|
|
- Acetolactate synthase
- Acyl CoA dehydrogenase
- Apoptosis-inducing factor
- Butyryl CoA dehydrogenase
- Cryptochrome
- Cytochrome b5 reductase
- Dihydrolipoamide dehydrogenase
- Flavodoxin
- Methemoglobin reductase
- Methylenetetrahydrofolate reductase
- NADH dehydrogenase
- NADPH oxidase
- Nitrate reductase
- Sarcosine oxidase
- Thioredoxin reductase
|
|
This article incorporates text from the public domain Pfam and InterPro IPR003382
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Loss of NOX2 (gp91phox) prevents oxidative stress and progression to advanced heart failure.
- Parajuli N, Patel VB, Wang W, Basu R, Oudit GY.
- Clinical science (London, England : 1979).Clin Sci (Lond).2014 Sep;127(5):331-40. doi: 10.1042/CS20130787.
- Oxidative stress plays a key pathogenic role in experimental and human heart failure. However, the source of ROS (reactive oxygen species) is a key determinant of the cardiac adaptation to pathological stressors. In the present study, we have shown that human dilated cardiomyopathy is associated wit
- PMID 24624929
- Metformin ameliorates ovariectomy-induced vascular dysfunction in non-diabetic Wistar rats.
- Oliveira PW1, de Sousa GJ1, Caliman IF1, Lamas AZ1, Santos de Medeiros AR2, de Andrade TU, de Abreu GR1, de Figueiredo SG1, Bissoli NS1.
- Clinical science (London, England : 1979).Clin Sci (Lond).2014 Aug;127(4):265-75. doi: 10.1042/CS20130553.
- Metformin is an antihyperglycaemic drug with pleiotropic effects that result in cardiovascular improvement. The aim of the present study was to evaluate the effects of metformin treatment on vascular dysfunction in ovariectomized rats. At 8 weeks of age, female Wistar rats were subjected to ovariect
- PMID 24521306
- Nitrite reduction and cardiovascular protection.
- Omar SA1, Webb AJ2.
- Journal of molecular and cellular cardiology.J Mol Cell Cardiol.2014 Aug;73C:57-69. doi: 10.1016/j.yjmcc.2014.01.012. Epub 2014 Jan 29.
- Inorganic nitrite, a metabolite of endogenously produced nitric oxide (NO) from NO synthases (NOS), provides the largest endocrine source of directly bioavailable NO. The conversion of nitrite to NO occurs mainly through enzymatic reduction, mediated by a range of proteins, including haem-globins, m
- PMID 24486197
Japanese Journal
- Heterologous expression of L-lysine α-oxidase from Scomber japonicus in Pichia pastoris and functional characterization of the recombinant enzyme
- Increased Expression of Osteopontin in the Degenerating Striatum of Rats Treated with Mitochondrial Toxin 3-Nitropropionic Acid: A Light and Electron Microscopy Study
- Increased Expression of Osteopontin in the Degenerating Striatum of Rats Treated with Mitochondrial Toxin 3-Nitropropionic Acid: A Light and Electron Microscopy Study
Related Links
- flavoproteinとは。意味や和訳。[名詞] 〔生化学〕 フラビンタンパク質，黄色タンパク：ビタミン B2(riboflavin)を含む複合タンパク質の総称；動物細胞中の酸化を促進する.[語源]1934 - 80万項目以上収録、例文・コロケーションが豊富な無料 ...
- flavoprotein [fla″vo-pro´tēn] a conjugated protein containing a flavin nucleotide. fla·vo·pro·tein (flā'vō-prō'tēn), A compound protein possessing a flavin as prosthetic group. Compare: flavoenzyme. flavoprotein (flā′vō-prō′tēn′, -tē-ĭn) n. Any of ...
Related Pictures
★リンクテーブル★
[★]
- 英
- flavoenzyme, flavin enzyme
- 同
- フラビンタンパク質 flavoprotein
- 関
- フラビン
[★]
- 英
- flavoprotein
- 関
- フラビンタンパク質、フラボプロテイン
[★]
- 英
- flavoprotein
- 関
- フラボタンパク質、フラビンタンパク質