Hydrolases enzymes

Procion Rubine MX-B, Procion Yellow H-A, and Turquoise MX-G. These dyes have found use over the last few decades in the purification of a broad range of proteins and enzymes, including albumin, decarboxylases, glycolytic enzymes, hydrolases, lyases, nucleases, oxidoreductases, synthetases, and transferases [77,78], The first use of dye-ligand affinity chromatography was described by Staal et al. in 1971 [79], Since that time, it has become an extremely popular tool for enzyme and protein purification, with hundreds of such compounds having been isolated by this technique [3-6,76-79],... 

SNAKE VENOM ENZYMES HYDROLASES THAT PRODUCE TOXIC EFFECTS... 

Caco-2 cells form tight junctions and express many of the brush border enzymes (hydrolases) that are found in the normal small intestine, for example, alkaline phosphatase, sucrase, and amino peptidases [26-29]. Cytochrome P450 (CYP450) isoenzymes and some phase II enzymes (e.g., glutathione-S-transferases, sulfotrans-ferase, and glucuronidase) have been identified [29-33] in these cells however, the level of CYP expression (e.g., CYP3A4) is low in the original cells under standard cell culture conditions [34]. 

Of the six main classes of enzymes, hydrolases, oxidoreductases and transferases have been the three most useful in kinetic resolution. Among the hydrolases, lipases are extensively used. The molecular machinery of lipases consists of a catalytic triad of the amino acids serine, histidine, and aspartic (or glutamic) acid. The enzyme first transfers the acyl group of an ester to the hydroxyl group of the serine residue to form the acylated enzyme. The acyl group is subsequently transferred to an external nucleophile with the return of the enzyme to its pre-acylated state to start the process again. A variety of nucleophiles can participate in this process water results in hydrolysis, an amine results in amidation, an alcohol results in esterification or transesterification, and hydrogen peroxide results in the formation of perac-id. Another reason which favored the relatively wide applicability of lipases in enzymatic... 

Goto et al. 1998). None of them probably reflects properly the enzyme activity over the real substrate, so it will be a matter of judgment and experience to select the most pertinent assay with respect to the actual use of the enzyme. Hydrolases are currently assayed with respect to their hydrolytic activities however, the increasing use of hydrolases to perform reactions of synthesis in non-aqueous media make this type of assay not quite adequate to evaluate the synthetic potential of such enzymes. For instance, the protease subtilisin has been used as a catalyst for a trans-esterification reaction that produces thiophenol as one of the products (Han et al. 2004) in this case, a method based on a reaction leading to a fluorescent adduct of thiophenol is a good system to assess the transesterification potential of such proteases and is to be preferred to a conventional protease assay based on the hydrolysis of a protein (Gupta et al. 1999 Priolo et al. 2000) or a model peptide (Klein et al. 1989). 

Thus, for example, hydrolytically effective enzymes (hydrolases) are distinguished from decarboxylating enzymes (decarboxylases), etc. ... 

W. is a reactant in enzyme (hydrolase)-catalysed hydrolytic cleavage of macromolecules (proteins, carbohydrates, fats), representing the first stage in the biological degradation of these substances. W. is formed metabolically by the operation of the respiratory chain (Thble 3) (respiratory W.), and is the substrate of photosynthesis. 

---