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The Modification Of Tyrosine
Published in Roger L. Lundblad, Chemical Reagents for Protein Modification, 2020
Tyrosyl residues in proteins are also modified by reaction with cyanuric fluoride (Figure 4).24,25 The reaction proceeds at alkaline pH (9.1) via modification of the phenolic hydroxyl group with a change in the spectral properties of tyrosine. The phenolic hydroxyl groups must be ionized (phenoxide ion) for reaction with cyanuric fluoride. The modification of tyrosyl residues in elastase26 and yeast hexokinase27 with cyanuric fluoride has been reported.
The Modification of Tyrosine
Published in Roger L. Lundblad, Claudia M. Noyes, Chemical Reagents for Protein Modification, 1984
Roger L. Lundblad, Claudia M. Noyes
Tyrosyl residues in proteins are also modified by reaction with cyanuric fluoride (Figure 4).26,27 The reaction proceeds at alkaline pH (9.1) via modification of the phenolic hydroxyl group with a change in the spectral properties of tyrosine. The phenolic hydroxyl groups must be ionized (phenoxide ion) for reaction with cyanuric fluoride. The modification of tyrosyl residues in elastase28 and yeast hexokinase29 with cyanuric fluoride has been reported.
The Modification of Tyrosine
Published in Roger L. Lundblad, Claudia M. Noyes, Chemical Reagents for Protein Modification, 1984
Roger L. Lundblad, Claudia M. Noyes
Tyrosyl residues in proteins are also modified by reaction with cyanuric fluoride (Figure 4).26,27 The reaction proceeds at alkaline pH (9.1) via modification of the phenolic hydroxyl group with a change in the spectral properties of tyrosine. The phenolic hydroxyl groups must be ionized (phenoxide ion) for reaction with cyanuric fluoride. The modification of tyrosyl residues in elastase28 and yeast hexokinase29 with cyanuric fluoride has been reported.
Antibacterial carbonic anhydrase inhibitors: an update on the recent literature
Published in Expert Opinion on Therapeutic Patents, 2020
Claudiu T. Supuran, Clemente Capasso
A series of diazenylbenzenesulfonamides obtained from sulfanilamide or metanilamide by diazotization followed by coupling with phenols or amines resulted in micromolar inhibitors of mtCA1, with prontosil being the best inhibitor KIs of 126 nM [125]. Most sulfonamides exhibited KI values in the range of 1–10 µM [126]. Still, several derivatives, including sulfanilyl-sulfonamides acetazolamide, methazolamide, dichlorophenamide, dorzolamide, brinzolamide, benzolamide, and the sulfamate topiramate, exhibited submicromolar inhibition (KI values of 0.481–0.905 µM) [126]. The best inhibitors were 3-bromosulfanilamide and indisulam (KI values of 97–186 nM) [126]. A series of fluorine-containing 1,3,5-triazinyl sulfonamide derivatives obtained from cyanuric fluoride, sulfanilamide/4-aminoethyl benzenesulfonamide, and incorporating amino, amino alcohol and amino acid moieties showed excellent inhibition, with KI values in the nanomolar or submicromolar range not only against mtCA 1, but also against the others β-CAs (mtCA 2 and mtCA 3) identified in the genome of M. tuberculosis [89].