gyaR Protein, Thermoanaerobacter ethanolicus (His, StrepⅡ)

GyaR Proteinas, an alcohol dehydrogenase, efficiently oxidizes primary long-chain alcohols, with pentan-1-ol as the optimal substrate in vitro. It displays versatile dehydrogenase activity on alcohols like propanol, hexanol, and ethanol, highlighting its potential in diverse metabolic pathways by catalyzing the oxidation of various primary alcohols. gyaR Protein, Thermoanaerobacter ethanolicus (His, Strep) is the recombinant gyaR protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

GyaR, identified as an alcohol dehydrogenase, exhibits enzymatic activity against primary long-chain alcohols. While pentan-1-ol serves as the optimal substrate in vitro, GyaR displays efficient dehydrogenase activity on a range of alcohols, including propanol, hexanol, and ethanol. This versatility underscores the enzyme's capability to catalyze the oxidation of various primary alcohols, emphasizing its potential role in diverse metabolic pathways.

Others

E. coli

N-StrepⅡ;N-6*His

Q9F282 (W2-F399)

/

Partial

WETKINPNKVFELRCKNTTYFGIGSIKKIKDILEVLKNKGINNVILVTGKGSYKASGAWDVVKPALETLGFKYSLYDKVGPNPTVDMIDEAAKIGRETGAKAVIGIGGGSPIDTAKSVAVLLEYTDKNARELYEQKFIPEKAAPIIAINLTHGTGTEVDRFAVATIPEKNYKPAIAYDCLYPMYAIDDPSLMTKLDKKQTIAVTIDALNHVTEAATTLVASPYSVLMAKETVRLIVRYLPAAVNDPENLVARYYLLYASALAGISFDNGLLHLTHALEHPLSAVKPEIAHGLGLGAILPAVVKAIYPSVAEVLAEVYSPIVPGLKGLPAEAEYVAKKVEEWLFKVGCTQKLSDFGFTKEDIPTLVRLAKTTPSLDGLLSNAPVEATEAVIAKIYEESF

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.