Substrate Hydrophobic Groups and the Maximal Rate of Enzyme Reactions
Author:
- Barend H. J. HofsteeBHBarend H. J. Hofstee
- 1 January 1967
- journal article
- Published by Springer Nature in Nature
- Vol. 213 (5071) , 42-44
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- The Primary Specificity of α-Chymotrypsin. Acylated Amino Acid Esters with Normal Alkyl Side Chains1Journal of the American Chemical Society, 1965
- SOME ASPECTS OF THE SPECIFICITY OF FATTY ACID ESTERASESJournal of Histochemistry & Cytochemistry, 1964
- Thermodynamics of the Solution ProcessJournal of Biological Chemistry, 1963
- The Relationship of Enzyme Inhibitory Activity to the Structure of n-Alkylphosphonate and Phenylalkylphosphonate Esters*Biochemistry, 1963
- Steric Course and Specificity of α-Chymotrypsin-catalyzed Reactions. IIJournal of the American Chemical Society, 1962
- Synthesis of some esters of hippuric acid, and their hydrolysis by α-chymotrypsinArchives of Biochemistry and Biophysics, 1962
- Kinetics of chymotrypsin with a homologous series of n-fatty acid esters as substratesBiochimica et Biophysica Acta, 1959
- Fatty acid esters as substrates for trypsin and chymotrypsinBiochimica et Biophysica Acta, 1957
- SPECIFICITY OF ESTERASESJournal of Biological Chemistry, 1954
- SPECIFICITY OF ESTERASESJournal of Biological Chemistry, 1952