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Os [[autoanticorpo]]s contra a alfa-enolase están asociados coa rar síndrome chamada [[encefalopatía de Hashimoto]].<ref name="pmid15833368">{{cite journal |author=Fujii A, Yoneda M, Ito T, Yamamura O, Satomi S, Higa H, Kimura A, Suzuki M, Yamashita M, Yuasa T, Suzuki H, Kuriyama M |title=Autoantibodies against the amino terminal of alpha-enolase are a useful diagnostic marker of Hashimoto's encephalopathy |journal=[[J. Neuroimmunol.]] |volume=162 |issue=1–2 |pages=130–6 |year=2005 |month=May |pmid=15833368 |doi=10.1016/j.jneuroim.2005.02.004 |url=}}</ref>
 
==InhibitorsInhibidores ofda Enolaseenolase==
Sintetizáronse pequenas moléculas [[inhibidor encimático|inhibidoras]] da enolase como sondas químicas do mecanismo catalítico do encima. A máis potente destes é o fosfonoacetohidroxamato, que na súa forma non protonada ten afinidade pM polo encima. Ten unha semellanza estrutural co presunto intermediato catalítico entre o PEP e o 2-PG. Fixéronse intentos de usar este inhibidor como un fásrmaco anti-[[tripanosoma]], e máis recentemente, como un axente anticancro, especificamente, nos glioblastomas que son deficientes en enolase debido á deleción [[homocigoto|homocigótica]] do xene ENO1 como parte do [[locus]] 1p36.
Small molecule inhibitors of Enolase have been synthesized as chemical probes of the catalytic mechanism of the enzyme. The most potent of these is Phosphonoacetohydroxamate, which in its unprotonate form, has pM affinity for the enzyme. It has structural similarity to the presumed catalytic intermediate, between PEP and 2-PG. Attempts have been made to use this inhibitor as an anti-typanosome, and more recently, as an anti-cancer agent, specifically, in glioblastoma that are enolase-deficient due to homozygous deletion of the ENO1 gene as part of the 1p36 locus.
 
O [[Fluoridefluoruro]] isé aun known[[inhibición competitorencimática|competidor]] ofcoñecido enolase’sdo substratesubstrato da enolase 2-PG. O Thefluoruro fluorideforma isparte partdun ofcomplexo a complexco withmagnesio magnesiume ando phosphatefosfato, whichque bindsse inune theao activesitio siteactivo insteaden oflugar do 2-PG.<ref name="Hoorn" /> Beber Asauga such,fluorada drinkingproporciona [[waterun fluoridation|fluoridatednivel water]]de providesfluoruro fluorideque atinhibe a levelactividade thatda inhibitsenolase oraldas bacteria[[flora enolaseoral|bacterias activityda withoutboca]] harmingsen humans.causar dano Disruptionaos ofhumanos. theA bacteria’sinterrupción glycolyticda pathwayvía -glicolítica and,das thus,bacterias itsé normalunha metabolicprevención functioning - preventsda [[dental cariescarie]] from forming.<ref>{{cite journal |author=Centers For Disease Control |title=Populations receiving optimally fluoridated public drinking water—United States, 2000 |journal=MMWR Morb Mortal Wkly Rep. |volume=51 |issue=7 |pages=144–7 |year=2002 |month= February|pmid=11905481 |author1=Centers for Disease Control and Prevention (CDC) }}</ref><ref>{{cite journal |author=Hüther FJ, Psarros N, Duschner H |title=Isolation, characterization, and inhibition kinetics of enolase from Streptococcus rattus FA-1 |journal=Infect Immun. |volume=58 |issue=4 |pages=1043–7 |date=1 April 1990|pmid=2318530 |pmc=258580 |url=http://iai.asm.org/cgi/pmidlookup?view=long&pmid=2318530 }}</ref>▼
 
 
▲[[Fluoride]] is a known competitor of enolase’s substrate 2-PG. The fluoride is part of a complex with magnesium and phosphate, which binds in the active site instead of 2-PG.<ref name="Hoorn" /> As such, drinking [[water fluoridation|fluoridated water]] provides fluoride at a level that inhibits oral bacteria enolase activity without harming humans. Disruption of the bacteria’s glycolytic pathway - and, thus, its normal metabolic functioning - prevents [[dental caries]] from forming.<ref>{{cite journal |author=Centers For Disease Control |title=Populations receiving optimally fluoridated public drinking water—United States, 2000 |journal=MMWR Morb Mortal Wkly Rep. |volume=51 |issue=7 |pages=144–7 |year=2002 |month= February|pmid=11905481 |author1=Centers for Disease Control and Prevention (CDC) }}</ref><ref>{{cite journal |author=Hüther FJ, Psarros N, Duschner H |title=Isolation, characterization, and inhibition kinetics of enolase from Streptococcus rattus FA-1 |journal=Infect Immun. |volume=58 |issue=4 |pages=1043–7 |date=1 April 1990|pmid=2318530 |pmc=258580 |url=http://iai.asm.org/cgi/pmidlookup?view=long&pmid=2318530 }}</ref>
 
==Notas==
Traído desde «https://gl.wikipedia.org/wiki/Enolase»