How do hydrolases break chemical bonds?

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How do hydrolases break chemical bonds?

Hydrolases break chemical bonds through hydrolysis: they use a water molecule to cleave covalent bonds. In the enzyme’s active site, water is positioned so it acts as a nucleophile and attacks the bond (such as peptide, ester, glycosidic, or phosphodiester linkages). This creates a short-lived intermediate that is stabilized by the enzyme, and the bond splits to give two products, each incorporating a part of the water (typically an -OH on one fragment and an -H on the other). This is distinct from mechanisms that transfer electrons or groups without adding water, such as redox reactions or group transfers, so using water to sever bonds is the defining feature of hydrolases.

Hydrolases break chemical bonds through hydrolysis: they use a water molecule to cleave covalent bonds. In the enzyme’s active site, water is positioned so it acts as a nucleophile and attacks the bond (such as peptide, ester, glycosidic, or phosphodiester linkages). This creates a short-lived intermediate that is stabilized by the enzyme, and the bond splits to give two products, each incorporating a part of the water (typically an -OH on one fragment and an -H on the other). This is distinct from mechanisms that transfer electrons or groups without adding water, such as redox reactions or group transfers, so using water to sever bonds is the defining feature of hydrolases.

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