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  2. Hydrolysis - Wikipedia

    en.wikipedia.org/wiki/Hydrolysis

    Hydrolysis (/ h aɪ ˈ d r ɒ l ɪ s ɪ s /; from Ancient Greek hydro- 'water' and lysis 'to unbind') is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution , elimination , and solvation reactions in which water is the nucleophile .

  3. Hydrolase - Wikipedia

    en.wikipedia.org/wiki/Hydrolase

    Acetic acid is an important metabolite in the body and a critical intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleotides. [2]

  4. Phosphatase - Wikipedia

    en.wikipedia.org/wiki/Phosphatase

    The general reaction catalyzed by a phosphatase enzyme. Phosphatases catalyze the hydrolysis of a phosphomonoester, removing a phosphate moiety from the substrate. Water is split in the reaction, with the -OH group attaching to the phosphate ion, and the H+ protonating the hydroxyl group of the other product. The net result of the reaction is ...

  5. Esterase - Wikipedia

    en.wikipedia.org/wiki/Esterase

    In biochemistry, an esterase is a class of enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis (and as such, it is a type of hydrolase). A wide range of different esterases exist that differ in their substrate specificity, their protein structure, and their biological function.

  6. GTPase - Wikipedia

    en.wikipedia.org/wiki/GTPase

    Hydrolysis of GTP bound to an (active) G domain-GTPase leads to deactivation of the signaling/timer function of the enzyme. [2] [3] The hydrolysis of the third (γ) phosphate of GTP to create guanosine diphosphate (GDP) and P i, inorganic phosphate, occurs by the S N 2 mechanism (see nucleophilic substitution) via a pentacoordinate transition state and is dependent on the presence of a ...

  7. Carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase

    Carboxypeptidases hydrolyze peptides at the first amide or polypeptide bond on the C-terminal end of the chain. Carboxypeptidases act by replacing the substrate water with a carbonyl (C=O) group. The carboxypeptidase A hydrolysis reaction has two mechanistic hypotheses, via a nucleophilic water and via an anhydride.

  8. Glycoside hydrolase - Wikipedia

    en.wikipedia.org/wiki/Glycoside_hydrolase

    Glycoside hydrolases can also be classified according to the stereochemical outcome of the hydrolysis reaction: thus they can be classified as either retaining or inverting enzymes. [6] Glycoside hydrolases can also be classified as exo or endo acting, dependent upon whether they act at the (usually non-reducing) end or in the middle ...

  9. ATP hydrolysis - Wikipedia

    en.wikipedia.org/wiki/ATP_hydrolysis

    Structure of ATP Structure of ADP Four possible resonance structures for inorganic phosphate. ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in the high-energy phosphoanhydride bonds in adenosine triphosphate (ATP) is released after splitting these bonds, for example in muscles, by producing work in the form of mechanical energy.