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  2. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    However, additional molecular interactions may render the amide form less stable; the amino group is expelled instead, resulting in an ester (Ser/Thr) or thioester (Cys) bond in place of the peptide bond. This chemical reaction is called an N-O acyl shift. The ester/thioester bond can be resolved in several ways:

  3. Butyrylcholinesterase - Wikipedia

    en.wikipedia.org/wiki/Butyrylcholinesterase

    590 12038 Ensembl ENSG00000114200 ENSMUSG00000027792 UniProt P06276 Q03311 RefSeq (mRNA) NM_000055 NM_009738 RefSeq (protein) NP_000046 NP_033868 Location (UCSC) Chr 3: 165.77 – 165.84 Mb Chr 3: 73.54 – 73.62 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Butyrylcholinesterase (HGNC symbol BCHE ; EC 3.1.1.8), also known as BChE, BuChE, BuChase, pseudocholinesterase, or plasma ...

  4. Ligase - Wikipedia

    en.wikipedia.org/wiki/Ligase

    In biochemistry, a ligase is an enzyme that can catalyze the joining of two molecules by forming a new chemical bond.This is typically via hydrolysis of a small pendant chemical group on one of the molecules, typically resulting in the formation of new C-O, C-S, or C-N bonds.

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein domains. The two shown protein structures share a common domain (maroon), the PH domain, which is involved in phosphatidylinositol (3,4,5)-trisphosphate binding. Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds.

  6. Hydrolase - Wikipedia

    en.wikipedia.org/wiki/Hydrolase

    Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase , which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid . [ 1 ]

  7. Carboxylesterase 1 - Wikipedia

    en.wikipedia.org/wiki/Carboxylesterase_1

    Carboxylesterase 1 is a serine esterase and member of a large multigene carboxylesterase family. It is also part of the alpha/beta fold hydrolase family. [7] These enzymes are responsible for the hydrolysis of ester- and amide-bond-containing xenobiotics and drugs such as cocaine and heroin.

  8. Dipeptide - Wikipedia

    en.wikipedia.org/wiki/Dipeptide

    The two modified amino acids are then combined in the presence of a coupling agent, which facilitates formation of the amide bond: RCH(NHP)CO 2 H + R'CH(NH 2)CO 2 CH 3 → RCH(NHP)C(O) NH(CHR')CO 2 CH 3 + H 2 O. Subsequent to this coupling reaction, the amine protecting group P and the ester are converted to the free amine and carboxylic acid ...

  9. Thioester - Wikipedia

    en.wikipedia.org/wiki/Thioester

    Eventually, [these] thioesters could have served to usher in ATP through its ability to support the formation of bonds between phosphate groups. However, due to the high free energy change of thioester's hydrolysis and correspondingly their low equilibrium constants, it is unlikely that these compounds could have accumulated abiotically to any ...