On Malyl-coenzyme A Synthetase
- 1 December 1964
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 56 (6) , 545-551
- https://doi.org/10.1093/oxfordjournals.jbchem.a128032
Abstract
Malyl-CoA synthetase (L-malate: CoA ligase (ADP)) which specifically catalyzed the malyl-CoA formation from L-malate and CoA in the expense of ATP was isolated and partially purified from cell-free extracts of Rhodopseudomonas spheroides. The enzyme also catalyzed a rapid ATP-Pi exchange which was strictly dependent upon the presence of L-malatc and CoA. Also Mg++ was required for these reactions. Reversibility of the reaction of malyl-CoA synthesis was established by employing ADP, Pi and chemically synthesized DL-malyl-CoA which has been proved to have the hydroxyl group at βpostion.Keywords
This publication has 2 references indexed in Scilit:
- The synthesis of porphyrins and bacteriochlorophyll in cell suspensions of Rhodopseudomonas spheroidesBiochemical Journal, 1956
- STUDIES ON THE MECHANISM OF THE REACTION CATALYZED BY THE PHOSPHORYLATING ENZYMEJournal of Biological Chemistry, 1955