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thioester การใช้

ประโยคมือถือ
  • The intermediate that attacks the incoming thioester substrate.
  • The challenge lies in the preparation of the necessary unprotected peptide-thioester building block.
  • This enzyme belongs to the family of hydrolases, specifically the class of thioester lyases.
  • This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds.
  • First, a prenyl lipid anchor is attached to the cysteine through a thioester linkage.
  • Upon cleavage of the LPXTG motif, Sortase forms a thioester intermediate with the engineered molecule.
  • The absence of this domain means that the exposed thioester bond of active TEP1 is unstable.
  • They use the coenzyme A-thioester of ( r )-hydroxy fatty acids as substrates.
  • This highly stereoselective chiral inversion is mediated by the FLX-S-Acyl-CoA thioester.
  • During the second step, Atg8 is transferred to Atg3 assuming the same type of thioester bondage.
  • The energy needed for this oxidation is conserved in the formation of a thioester bond of succinyl CoA.
  • Deprotonation encourages the reformation of the carbonyl group in the thioester intermediate and ejection of the hydride ion.
  • Although this secondary ubiquitin is similarly adenylated, it does not form the same thioester complex described previously.
  • Cleavage into the cut form is followed by a change in protein structure which exposes the thioester bond.
  • Finally, in the extein the ester or thioester bond is rearranged to form a normal peptide bond.
  • Similarly, a recombinant protein containing an N-terminal Cys can be reacted with a synthetic polypeptide thioester.
  • The most common form of native chemical ligation uses a peptide thioester that reacts with a terminal cysteine residue.
  • The energy from ATP and diphosphate hydrolysis drives the formation of this reactive thioester, and subsequent steps are thermoneutral.
  • "' Methylmalonyl-CoA "'is the thioester consisting of coenzyme A linked to methylmalonic acid.
  • The thiolase superfamily enzymes catalyse the carbon carbon-bond formation via a thioester-dependent Claisen condensation reaction mechanism.
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