Home
Resources
Publications
Hydrolysis of 4-nitrophenyl Acetate Catalyzed by Carbonic Anhydrase III From Bovine Skeletal Muscle

Hydrolysis of 4-nitrophenyl Acetate Catalyzed by Carbonic Anhydrase III From Bovine Skeletal Muscle

C K Tu, H G Thomas, G C Wynns, D N Silverman

J Biol Chem. 1986 Aug 5;261(22):10100-3.

PMID: 3090030

Abstract:

We report three experiments which show that the hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle occurs at a site on the enzyme different than the active site for CO2 hydration. This is in contrast with isozymes I and II of carbonic anhydrase for which the sites of 4-nitrophenyl acetate hydrolysis and CO2 hydration are the same. The pH profile of kcat/Km for hydrolysis of 4-nitrophenyl acetate was roughly described by the ionization of a group with pKa 6.5, whereas kcat/Km for CO2 hydration catalyzed by isozyme III was independent of pH in the range of pH 6.0-8.5. The apoenzyme of carbonic anhydrase III, which is inactive in the catalytic hydration of CO2, was found to be as active in the hydrolysis of 4-nitrophenyl acetate as native isozyme III. Concentrations of N-3 and OCN- and the sulfonamides methazolamide and chlorzolamide which inhibited CO2 hydration did not affect catalytic hydrolysis of 4-nitrophenyl acetate by carbonic anhydrase III.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP830035	4-Nitrophenyl acetate		830-03-5	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: