Substrate specificity of solvent viscosity effects in carboxypeptidase A catalyzed peptide hydrolysis
โ Scribed by Dimitrij E. Khoshtariya; Jan Meldtoft Hammerstad-Pedersen; Jens Ulstrup
- Book ID
- 113268581
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 369 KB
- Volume
- 1076
- Category
- Article
- ISSN
- 0167-4838
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๐ SIMILAR VOLUMES
N-benzoyl-L-phenylalanyl-L-phenylalanine is an excellent peptide substrate for carboxypeptidase A; at 30ยฐC and pH 7.5, K m is 2.6 ร 10 -5 M while k cat is 177 s -1 (k cat /K m = 6.8 ร 10 6 M -1 s -1 ). Indole-3-acetic acid is a noncompetitive or mixed inhibitor towards the peptide and toward hippury
Results of a previous study on the hydrolysis of \(O\)-( \(\alpha\)-acylamino-cinnamoyl)-L- \(\beta\)-phenyllactates \(E 1\) and \(\mathbf{E} 2\) catalyzed by carboxypeptidase \(A(C P A)\) supported the anhydride mechanism for the action of CPA. Since these esters are hydrolyzed very slowly by CPA,