葉酸脱水素酵素、葉酸デヒドロゲナーゼ
WordNet
- determine the arrangement of (data) for storage and display (in computer science)
- the general appearance of a publication
- the organization of information according to preset specifications (usually for computer processing) (同)formatting, data format, data formatting
- set (printed matter) into a specific format; "Format this letter so it can be printed out" (同)arrange
- divide (a disk) into marked sectors so that it may store data; "Please format this disk before entering data!" (同)initialize, initialise
PrepTutorEJDIC
- (書籍の)体裁,型,判 / (ラジオ・テレビ番組などの)構成
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/06/11 17:01:07」(JST)
[Wiki en表示]
| Formate dehydrogenase N, transmembrane |
| Identifiers |
| Symbol |
Form-deh_trans |
| Pfam |
PF09163 |
| InterPro |
IPR015246 |
| SCOP |
1kqf |
| SUPERFAMILY |
1kqf |
| OPM superfamily |
3 |
| OPM protein |
1kqf |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.2.1.2) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1).[1]
Contents
- 1 Function
- 2 Molybdopterin, molybdenum and selenium dependence
- 3 Transmembrane domain
- 4 See also
- 5 References
- 6 External links
Function
NAD-dependent formate dehydrogenases are important in methylotrophic yeast and bacteria and are vital in the catabolism of C1 compounds such as methanol.[2] The cytochrome-dependent enzymes are more important in anaerobic metabolism in prokaryotes.[3] For example, in E. coli, the formate:ferricytochrome-b1 oxidoreductase is an intrinsic membrane protein with two subunits and is involved in anaerobic nitrate respiration.[4][5]
NAD-dependent reaction
Formate + NAD+ ↔ CO2 + NADH + H+
Cytochrome-dependent reaction
Formate + 2 ferricytochrome b1 ↔ CO2 + 2 ferrocytochrome b1 + 2 H+
Molybdopterin, molybdenum and selenium dependence
One of the enzymes in the oxidoreductase family that sometimes employ tungsten (bacterial formate dehydrogenase H) is known to use a selenium-molybdenum version of molybdopterin.[6]
Transmembrane domain
The transmembrane domain of the beta subunit of formate dehydrogenase consists of a single transmembrane helix. This domain acts as a transmembrane anchor, allowing the conduction of electrons within the protein.[7]
See also
- Formate dehydrogenase (cytochrome)
- Formate dehydrogenase (cytochrome-c-553)
- Formate dehydrogenase (NADP+)
- Microbial metabolism
References
- ^ Ferry JG (1990). "Formate dehydrogenase". FEMS Microbiol. Rev. 7 (3–4): 377–82. doi:10.1111/j.1574-6968.1990.tb04940.x. PMID 2094290.
- ^ Popov VO, Lamzin VS (1994). "NAD(+)-dependent formate dehydrogenase". Biochem. J. 301 (3): 625–43. PMC 1137035. PMID 8053888.
- ^ Jormakka M, Byrne B, Iwata S (2003). "Formate dehydrogenase--a versatile enzyme in changing environments". Curr. Opin. Struct. Biol. 13 (4): 418–23. doi:10.1016/S0959-440X(03)00098-8. PMID 12948771.
- ^ Graham A, Boxer DH (1981). "The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli". Biochem. J. 195 (3): 627–37. PMC 1162934. PMID 7032506.
- ^ Ruiz-Herrera J, DeMoss JA (1969). "Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction". J. Bacteriol. 99 (3): 720–9. PMC 250087. PMID 4905536.
- ^ Khangulov SV, Gladyshev VN, Dismukes GC, Stadtman TC (1998). "Selenium-Containing Formate Dehydrogenase H from Escherichia coli: A Molybdopterin Enzyme That Catalyzes Formate Oxidation without Oxygen Transfer". Biochemistry 37 (10): 3518–3528. doi:10.1021/bi972177k. PMID 9521673.
- ^ Jormakka M, Törnroth S, Byrne B, Iwata S (2002). "Molecular basis of proton motive force generation: structure of formate dehydrogenase-N". Science 295 (5561): 1863–1868. doi:10.1126/science.1068186. PMID 11884747.
External links
- ENZYME link for EC 1.2.2.1
- ENZYME link for EC 1.2.1.2
|
Metabolism: Citric acid cycle enzymes
|
|
| Cycle |
- Citrate synthase
- Aconitase
- Isocitrate dehydrogenase
- Oxoglutarate dehydrogenase
- Succinyl CoA synthetase
- Succinate dehydrogenase (SDHA)
- Fumarase
- Malate dehydrogenase and ETC
|
|
| Anaplerotic |
|
to acetyl-CoA
|
- Pyruvate dehydrogenase complex (E1, E2, E3)
- (regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase phosphatase)
|
|
|
to α-ketoglutaric acid
|
|
|
|
to succinyl-CoA
|
|
|
|
to oxaloacetate
|
- Pyruvate carboxylase
- Aspartate transaminase
|
|
|
Mitochondrial
electron transport chain/
oxidative phosphorylation |
|
Primary
|
- Complex I/NADH dehydrogenase
- Complex II/Succinate dehydrogenase
- Coenzyme Q
- Complex III/Coenzyme Q - cytochrome c reductase
- Cytochrome c
- Complex IV/Cytochrome c oxidase
- Coenzyme Q10 synthesis: COQ2
- COQ3
- COQ4
- COQ5
- COQ6
- COQ7
- COQ9
- COQ10A
- COQ10B
- PDSS1
- PDSS2
|
|
|
Other
|
- Alternative oxidase
- Electron-transferring-flavoprotein dehydrogenase
|
|
|
|
Metabolism, catabolism, anabolism
|
|
| General |
- Metabolic pathway
- Metabolic network
- Primary nutritional groups
|
|
Energy
metabolism |
| Aerobic respiration |
- Glycolysis → Pyruvate decarboxylation → Citric acid cycle → Oxidative phosphorylation (electron transport chain + ATP synthase)
|
|
| Anaerobic respiration |
- Electron acceptors are other than oxygen
|
|
| Fermentation |
- Glycolysis →
- Substrate-level phosphorylation
|
|
|
Specific
paths |
| Protein metabolism |
- Protein synthesis
- Catabolism
|
|
Carbohydrate metabolism
(carbohydrate catabolism
and anabolism) |
| Human |
- Glycolysis ⇄ Gluconeogenesis
|
|
- Glycogenolysis ⇄ Glycogenesis
|
|
- Pentose phosphate pathway
- Fructolysis
- Galactolysis
|
|
|
|
|
|
| Nonhuman |
- Photosynthesis
- Anoxygenic photosynthesis
- Chemosynthesis
- Carbon fixation
|
|
- Xylose metabolism
- Radiotrophism
|
|
|
|
Lipid metabolism
(lipolysis, lipogenesis) |
| Fatty acid metabolism |
- Fatty acid degradation (Beta oxidation)
- Fatty acid synthesis
|
|
| Other |
- Steroid metabolism
- Sphingolipid metabolism
- Eicosanoid metabolism
- Ketosis
- Reverse cholesterol transport
|
|
|
| Amino acid |
- Amino acid synthesis
- Urea cycle
|
|
Nucleotide
metabolism |
- Purine metabolism
- Nucleotide salvage
- Pyrimidine metabolism
|
|
| Other |
- Metal metabolism
- Ethanol metabolism
|
|
|
|
Aldehyde/oxo oxidoreductases (EC 1.2)
|
|
| 1.2.1: NAD or NADP |
- Aldehyde dehydrogenase
- Acetaldehyde dehydrogenase
- Long-chain-aldehyde dehydrogenase
|
|
| 1.2.2: cytochrome |
- Formate dehydrogenase (cytochrome)
|
|
| 1.2.3: oxygen |
|
|
| 1.2.4: disulfide |
- Oxoglutarate dehydrogenase complex
- Pyruvate dehydrogenase
- Branched-chain alpha-keto acid dehydrogenase complex
|
|
| 1.2.7: iron-sulfur protein |
|
|
|
Enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
UpToDate Contents
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English Journal
- The ionic liquid isopropylammonium formate as a mobile phase modifier to improve protein stability during reversed phase liquid chromatography.
- Zhou L, Danielson ND.SourceDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, United States. Electronic address: zhoul3@miamioh.edu.
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.J Chromatogr B Analyt Technol Biomed Life Sci.2013 Dec 1;940:112-20. doi: 10.1016/j.jchromb.2013.08.005. Epub 2013 Aug 8.
- The room temperature ionic liquid isopropylammonium formate (IPAF) is studied as a reversed phase HPLC mobile phase modifier for separation of native proteins using a polymeric column and the protein stability is compared to that using acetonitrile (MeCN) as the standard organic mobile phase modifie
- PMID 24141045
- C1 Metabolism in Corynebacterium glutamicum: an Endogenous Pathway for Oxidation of Methanol to Carbon Dioxide.
- Witthoff S, Mühlroth A, Marienhagen J, Bott M.SourceInstitute of Bio- and Geosciences, IBG-1: Biotechnology, Forschungszentrum Jülich, Jülich, Germany.
- Applied and environmental microbiology.Appl Environ Microbiol.2013 Nov;79(22):6974-83. doi: 10.1128/AEM.02705-13. Epub 2013 Sep 6.
- Methanol is considered an interesting carbon source in "bio-based" microbial production processes. Since Corynebacterium glutamicum is an important host in industrial biotechnology, in particular for amino acid production, we performed studies of the response of this organism to methanol. The C. glu
- PMID 24014532
- Metabolomic and proteomic insights into carbaryl catabolism by Burkholderia sp. C3 and degradation of ten N-methylcarbamates.
- Seo JS, Keum YS, Li QX.SourceDepartment of Molecular Biosciences and Bioengineering, University of Hawaii, 1955 East-West Road, Honolulu, HI, 96822, USA.
- Biodegradation.Biodegradation.2013 Nov;24(6):795-811. doi: 10.1007/s10532-013-9629-2. Epub 2013 Mar 5.
- Burkholderia sp. C3, an efficient polycyclic aromatic hydrocarbon degrader, can utilize nine of the ten N-methylcarbamate insecticides including carbaryl as a sole source of carbon. Rapid hydrolysis of carbaryl in C3 is followed by slow catabolism of the resulting 1-naphthol. This study focused on m
- PMID 23463356
Japanese Journal
- Overexpression of a putative transcription factor Gf.CRZ1 affects the expression of oxalate-degrading genes and causes morphological defects during mycelium formation in Grifola frondosa
- Sato Masayuki,Kurahashi Atsushi,Nishibori Kozo [他]
- Mycoscience : official journal of the Mycological Society of Japan 56(5), 516-522, 2015-09
- NAID 40020592398
- Discovery of the Reduced Form of Methylviologen Activating Formate Dehydrogenase in the Catalytic Conversion of Carbon Dioxide to Formic Acid
- Amao Yutaka,Ikeyama Shusaku
- Chemistry Letters 44(9), 1182-1184, 2015
- … The kinetic properties of the conversion of CO2 to formic acid with formate dehydrogenase (FDH) using dithionite-reduced methylviologen as an artificial coenzyme were studied. …
- NAID 130005096870
- Discovery of Reduced Form of Methylviologen Activating Formate Dehydrogenase in the Catalytic Conversion of Carbon Dioxide to Formic Acid
- Amao Yutaka,Ikeyama Shusaku
- Chemistry Letters advpub(0), 2015
- … The kinetic properties of the conversion of CO2 to formic acid with formate dehydrogenase (FDH) using dithionite-reduced methylviologen as an artificial co-enzyme were studied. …
- NAID 130005074614
Related Links
- のサプライヤーのリストを取得する Formate Dehydrogenase と同等の製品を ... IRIS Biotech GmbH ためのサプライヤです Formate Dehydrogenase. 我々としてもN-alpha-tert-Butyloxycarbonyl-O-benzyl-D-serinolを販売しています。
- Escherichia coli can perform two modes of formate metabolism. Under respiratory conditions, two periplasmically-located formate dehydrogenase isoenzymes couple formate oxidation to the generation of a transmembrane ...
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