Skip to main content

Oxidoreductase








Oxidoreductase


From Wikipedia, the free encyclopedia

Jump to navigation
Jump to search


In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP or NAD+ as cofactors.[1][2] Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix. [3].




Contents






  • 1 Reactions


  • 2 Nomenclature


  • 3 Classification


  • 4 See also


  • 5 References


  • 6 External links





Reactions[edit]


For example, an enzyme that catalyzed this reaction would be an oxidoreductase:


A– + B → A + B–

In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor).


In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:


Pi + glyceraldehyde-3-phosphate + NAD+ → NADH + H+ + 1,3-bisphosphoglycerate

In this reaction, NAD+ is the oxidant (electron acceptor), and glyceraldehyde-3-phosphate is the reductant (electron donor).



Nomenclature[edit]


Proper names of oxidoreductases are formed as "donor:acceptor oxidoreductase"; however, other names are much more common. The common name is "donor dehydrogenase" when possible, such as glyceraldehyde-3-phosphate dehydrogenase for the second reaction above. Common names are also sometimes formed as "acceptor reductase", such as NAD+ reductase. "Donor oxidase" is a special case where O2 is the acceptor.



Classification[edit]


Oxidoreductases are classified as EC 1 in the EC number classification of enzymes. Oxidoreductases can be further classified into 22 subclasses:




  • EC 1.1 includes oxidoreductases that act on the CH-OH group of donors (alcohol oxidoreductases)


  • EC 1.2 includes oxidoreductases that act on the aldehyde or oxo group of donors


  • EC 1.3 includes oxidoreductases that act on the CH-CH group of donors (CH-CH oxidoreductases)


  • EC 1.4 includes oxidoreductases that act on the CH-NH2 group of donors (Amino acid oxidoreductases, Monoamine oxidase)


  • EC 1.5 includes oxidoreductases that act on CH-NH group of donors


  • EC 1.6 includes oxidoreductases that act on NADH or NADPH


  • EC 1.7 includes oxidoreductases that act on other nitrogenous compounds as donors


  • EC 1.8 includes oxidoreductases that act on a sulfur group of donors


  • EC 1.9 includes oxidoreductases that act on a heme group of donors


  • EC 1.10 includes oxidoreductases that act on diphenols and related substances as donors


  • EC 1.11 includes oxidoreductases that act on peroxide as an acceptor (peroxidases)


  • EC 1.12 includes oxidoreductases that act on hydrogen as donors


  • EC 1.13 includes oxidoreductases that act on single donors with incorporation of molecular oxygen (oxygenases)


  • EC 1.14 includes oxidoreductases that act on paired donors with incorporation of molecular oxygen


  • EC 1.15 includes oxidoreductases that act on superoxide radicals as acceptors


  • EC 1.16 includes oxidoreductases that oxidize metal ions


  • EC 1.17 includes oxidoreductases that act on CH or CH2 groups


  • EC 1.18 includes oxidoreductases that act on iron-sulfur proteins as donors


  • EC 1.19 includes oxidoreductases that act on reduced flavodoxin as a donor


  • EC 1.20 includes oxidoreductases that act on phosphorus or arsenic in donors


  • EC 1.21 includes oxidoreductases that act on X-H and Y-H to form an X-Y bond


  • EC 1.97 includes other oxidoreductases



See also[edit]



  • Hydroxylase

  • List of enzymes



References[edit]





  1. ^ Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 ed.). Wiley-Interscience. ISBN 0471205036..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  2. ^ Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third ed.). USA: Oxford University Press. ISBN 019850229X.


  3. ^ Superfamilies of single-pass transmembrane oxidoreductases in Membranome database




External links[edit]



  • EC 1 Introduction from the Department of Chemistry at Queen Mary, University of London


























Retrieved from "https://en.wikipedia.org/w/index.php?title=Oxidoreductase&oldid=854752303"





Navigation menu


























(window.RLQ=window.RLQ||).push(function(){mw.config.set({"wgPageParseReport":{"limitreport":{"cputime":"0.312","walltime":"0.391","ppvisitednodes":{"value":1244,"limit":1000000},"ppgeneratednodes":{"value":0,"limit":1500000},"postexpandincludesize":{"value":234022,"limit":2097152},"templateargumentsize":{"value":78,"limit":2097152},"expansiondepth":{"value":7,"limit":40},"expensivefunctioncount":{"value":0,"limit":500},"unstrip-depth":{"value":1,"limit":20},"unstrip-size":{"value":6100,"limit":5000000},"entityaccesscount":{"value":0,"limit":400},"timingprofile":["100.00% 223.708 1 -total"," 49.21% 110.083 1 Template:Oxidoreductases"," 40.49% 90.576 1 Template:Reflist"," 34.90% 78.065 2 Template:Cite_book"," 31.43% 70.321 16 Template:Navbox"," 7.44% 16.646 1 Template:Alcohol_oxidoreductases"," 7.11% 15.901 1 Template:Portal_bar"," 3.72% 8.326 1 Template:Hydrogen_oxidoreductases"," 3.41% 7.631 1 Template:Other_oxidoreductases"," 3.37% 7.531 1 Template:Sulfur_oxidoreductases"]},"scribunto":{"limitreport-timeusage":{"value":"0.115","limit":"10.000"},"limitreport-memusage":{"value":3435396,"limit":52428800}},"cachereport":{"origin":"mw1323","timestamp":"20181023210003","ttl":1900800,"transientcontent":false}}});mw.config.set({"wgBackendResponseTime":95,"wgHostname":"mw1270"});});
-

Popular posts from this blog

Full-time equivalent

Image
Full-time equivalent From Wikipedia, the free encyclopedia Jump to navigation Jump to search Full-time equivalent ( FTE ) or whole time equivalent ( WTE ) is a unit that indicates the workload of an employed person (or student) in a way that makes workloads or class loads comparable [1] across various contexts. FTE is often used to measure a worker's or student's involvement in a project, or to track cost reductions in an organization. An FTE of 1.0 is equivalent to a full-time worker or student, while an FTE of 0.5 signals half of a full work or school load. [2] Contents 1 U.S. Federal Government 2 In education 2.1 Example 3 Notes 4 References U.S. Federal Government [ edit ] In the U.S. Federal Government, FTE is defined by the Government Accountability Office (GAO) as the number of total hours worked divided by the maximum number of compensable hours in a full-time schedule as
Read more

Bicuculline

Image
Bicuculline From Wikipedia, the free encyclopedia Jump to navigation Jump to search Bicuculline Clinical data ATC code none Identifiers IUPAC name (6 R )-​6-​[(5 S )-​6-​methyl-​5,​6,​7,​8-​tetrahydro​[1,3]dioxolo​[4,5- g ]​isoquinolin-​5-​yl]​furo[3,4- e ]​[1,3]​benzodioxol-​8(6 H )-​one CAS Number 485-49-4   Y PubChem CID 10237 IUPHAR/BPS 2312 ChemSpider 9820   Y UNII Y37615DVKC ChEBI CHEBI:3092   N ChEMBL ChEMBL417990   N ECHA InfoCard 100.006.927 Chemical and physical data Formula C 20 H 17 N O 6 Molar mass 367.352 g/mol 3D model (JSmol) Interactive image Melting point 215 °C (419 °F) SMILES O=C1O[C@H](c3c1c2OCOc2cc3)[C@@H]5c4cc6OCOc6cc4CCN5C InChI InChI=1S/C20H17NO6/c1-21-5-4-10-6-14-15(25-8-24-14)7-12(10)17(21)18-11-2-3-13-19(26-9-23-13)16(11)20(22)27-18/h2-3,6-7,17-18H,4-5,8-9H2,1H3/t17-,18+/m0/s1   Y Key:IYGYMKDQCDOMRE-ZWKOTPCHSA-N
Read more

さくらももこ

Image
さくら ももこ 本名 非公開 [1] 生誕 ( 1965-05-08 ) 1965年5月8日 日本・静岡県清水市 （現・静岡市清水区） 死没 ( 2018-08-15 ) 2018年8月15日（53歳没） 日本・東京都目黒区 国籍 日本 職業 漫画家 エッセイスト 作詞家 活動期間 1984年 - 2018年 ジャンル 少女漫画 青年漫画 児童漫画 代表作 『ちびまる子ちゃん』 『コジコジ』 受賞 1989年：第13回講談社漫画賞少女部門 （『ちびまる子ちゃん』） 1990年：第32回日本レコード大賞 （『おどるポンポコリン』作詞） 公式サイト さくらプロダクション テンプレートを表示 さくら ももこ （1965年5月8日 - 2018年8月15日 [2] ）は、日本の漫画家、エッセイスト、作詞家、脚本家。また、自身の少女時代をモデルとした代表作のコミック『ちびまる子ちゃん』の主人公の名前でもある。静岡県清水市（現・静岡市清水区）出身。血液型はA型。身長159cm。一男の母親。 代表作のコミック『ちびまる子ちゃん』の単行本の売上は累計3000万部を超える。また、エッセイストとしても独特の視点と語り口で人気が高く、初期エッセイ集三部作『もものかんづめ』『さるのこしかけ』『たいのおかしら』はいずれもミリオンセラーを記録。 目次 1 経歴 2 人物・交遊関係 3 主な作品 3.1 漫画 3.2 エッセイ 3.3 作詞 3.4 詩集 3.5 雑誌・ムック本 3.6 翻訳 3.7 絵本、ドラマ脚本他 3.8 ラジオ出演 3.9 その他 4 関係人物 4.1 アシスタント 4.2 さくらももこを演じた人物 5 脚注 5.1 注釈 5.2 出典 6 外部リンク 経歴 年譜形式の経歴は推奨されていません 。人物の伝記は流れのあるまとまった文章で記述し、年譜は補助的な使用にとどめてください。 （ 2018年8月 ） 清水市立（当時）入江小学校
Read more