hidrolaz

Hidrolaz is the term used in several languages for hydrolases, a broad class of enzymes that catalyze the hydrolytic cleavage of chemical bonds by incorporating water. In enzymology, hydrolases (EC class 3) break bonds by adding water, producing smaller molecules. They participate in digestion, metabolism, development, and cellular turnover. Hydrolases act on various substrates, including esters, glycosidic bonds, phosphodiester bonds, and peptide bonds. Classic examples include proteases that hydrolyze proteins, lipases that hydrolyze fats, amylases that act on carbohydrates, nucleases that cleave nucleic acids, and phosphatases that remove phosphate groups.

Mechanism and structure: Most hydrolases use a catalytic mechanism that involves a nucleophilic attack and general acid-base catalysis, often via a catalytic triad such as serine-histidine-aspartate in serine hydrolases. Some are metal-dependent, using ions like zinc, calcium, or manganese to polarize water or stabilize intermediates. Substrate specificity ranges from broad to highly selective, reflecting adaptations to cellular roles or environmental niches.

Biological relevance: Hydrolases are essential for digestion in animals, decomposition of biomolecules in soils, recycling of nucleotides, and various regulatory pathways. They are common targets in pharmacology and are widely exploited in industry for biocatalysis, laundry detergents, biomass conversion, and bioremediation.

Classification: Hydrolases belong to EC class 3 and are grouped into major subclasses such as esterases, glycosidases, phosphatases, amidases, peptidases, and nucleases. This grouping reflects differences in substrates and reaction types rather than a single uniform mechanism.

See also: Hydrolase; Enzyme Commission; Protease; Lipase.