| 词条 | Formate dehydrogenase |
| 释义 |
| Symbol = Form-deh_trans | Name = Formate dehydrogenase N, transmembrane | image = | width = | caption = | Pfam= PF09163 | InterPro= IPR015246 | SMART= | Prosite = | SCOP = 1kqf | TCDB = | OPM family= 3 | OPM protein= 1kqf | PDB={{PDB3|1kqf}}B:246-289 {{PDB3|1kqg}}B:246-289 }}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] FunctionNAD-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 reactionFormate + NAD+ {{eqm}} CO2 + NADH + H+ Cytochrome-dependent reactionFormate + 2 ferricytochrome b1 {{eqm}} CO2 + 2 ferrocytochrome b1 + 2 H+ Molybdopterin, molybdenum and selenium dependenceOne 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 domainThe 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
References1. ^{{cite journal | vauthors = Ferry JG | title = Formate dehydrogenase | journal = FEMS Microbiol. Rev. | volume = 7 | issue = 3–4 | pages = 377–82 | year = 1990 | pmid = 2094290 | doi=10.1111/j.1574-6968.1990.tb04940.x}} 2. ^{{cite journal | vauthors = Popov VO, Lamzin VS | title = NAD(+)-dependent formate dehydrogenase | journal = Biochem. J. | volume = 301 | issue = 3 | pages = 625–43 | year = 1994 | pmid = 8053888 | pmc = 1137035 }} 3. ^{{cite journal | vauthors = Jormakka M, Byrne B, Iwata S | title = Formate dehydrogenase--a versatile enzyme in changing environments | journal = Curr. Opin. Struct. Biol. | volume = 13 | issue = 4 | pages = 418–23 | year = 2003 | pmid = 12948771 | doi = 10.1016/S0959-440X(03)00098-8 }} 4. ^{{cite journal | vauthors = Graham A, Boxer DH | title = The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli | journal = Biochem. J. | volume = 195 | issue = 3 | pages = 627–37 | year = 1981 | pmid = 7032506 | pmc = 1162934 }} 5. ^{{cite journal | vauthors = Ruiz-Herrera J, DeMoss JA | title = Nitrate reductase complex of Escherichia coli K-12: participation of specific formate dehydrogenase and cytochrome b1 components in nitrate reduction | journal = J. Bacteriol. | volume = 99 | issue = 3 | pages = 720–9 | year = 1969 | pmid = 4905536 | pmc = 250087 }} 6. ^{{cite journal | vauthors = Khangulov SV, Gladyshev VN, Dismukes GC, Stadtman TC | title = Selenium-Containing Formate Dehydrogenase H from Escherichia coli: A Molybdopterin Enzyme That Catalyzes Formate Oxidation without Oxygen Transfer | journal = Biochemistry | volume = 37 | issue = 10 | pages = 3518–3528 | year = 1998 | pmid = 9521673 | doi = 10.1021/bi972177k }} 7. ^{{cite journal | vauthors = Jormakka M, Törnroth S, Byrne B, Iwata S | title = Molecular basis of proton motive force generation: structure of formate dehydrogenase-N | journal = Science | volume = 295 | issue = 5561 | pages = 1863–1868 | year = 2002 | pmid = 11884747 | doi = 10.1126/science.1068186 }} External links
4 : Cellular respiration|Metabolism|EC 1.2.2|EC 1.2.1 |
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