Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase |
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| Authors: | RATNER S ROCHOVANSKY O |
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| Affiliation: | 1. Faculty of Arts and Social Sciences, University of Technology Sydney, 15 Broadway, Ultimo, NSW 2007, Australia;2. Resources, Environment and Development Group, Crawford School of Public Policy, The Australian National University, Canberra, ACT, Australia;1. Institute of Chemistry, State University of Moldova, 3 Academiei str., MD-2028, Chisinau, Republic of Moldova;2. Department of Pharmacy, University of Naples “Federico II”, Via Montesano 49, 80131 Naples, Italy;3. Consiglio Nazionale delle Ricerche (CNR), Istituto di Chimica Biomolecolare (ICB), Via Campi Flegrei 34, 80078 Pozzuoli Na, Italy;4. Department of Biology, University of Naples “Federico II”, Via Cintia, 21, 80126 Naples, Italy;1. School of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin 150001, PR China;2. State Key Laboratory of Advanced Welding and Joining, Harbin Institute of Technology, Harbin 150001, PR China |
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| Abstract: | A transamidinase which catalyzes the reversible reaction, l-arginine + glycine guanidinoacetic acid + l-ornithine, has been obtained from hog kidney and purified about 80-fold. Ornithine exerts a strong product inhibition which influences the reaction rates; conditions are given for obtaining initial rates.The velocity of the forward reaction is six times faster than the reverse reaction, and the equilibrium constant has been found to have a value of 1.1. The position of equilibrium indicates that the “energy level” of the CN bonds in arginine are the same for all other guanidino amino acids.A weak hydrolytic activity toward arginine appears to be associated with the enzyme, as well as the ability to utilize l-homoarginine as amidine donor at a relatively low rate. A number of other properties of the enzyme are described. |
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