Abstract
Abstract A second protein, the stimulator, has been identified as a necessary component for the in vitro incorporation of d-alanine into membrane teichoic acid of Lactobacillus casei (ATCC 7469). The incorporation activity is dependent on membrane fragments, ATP, d-alanine:membrane acceptor ligase (Reusch, V. M., Jr., and Neuhaus, F. C. (1971) J. Biol. Chem. 246, 6136), and the stimulator. The stimulator and the d-alanine:membrane acceptor ligase differ significantly with respect to exclusion volume on Sephadex G-100, chromatography on DEAE-cellulose, heat lability, and sensitivity to p-hydroxymercuribenzoate. It is proposed that the stimulator is the d-alanine-activating enzyme previously described by Baddiley and Neuhaus ((1960) Biochem. J. 75, 579). The stimulator and the d-alanine-activating enzyme co-elute on Sephadex G-100 and on DEAE-cellulose at pH 6.0 and pH 7.8. They are inactivated to the same extent by incubation at 45° and by incubation in the presence of p-hydroxymercuribenzoate. Under assay conditions in which the stimulator concentration is limiting with respect to ligase, the d-alanine incorporation system has a high specificity for ATP, shows product inhibition by pyrophosphate, and has a high Km for d-alanine. Each of these properties is also characteristic of the d-alanine-activation enzyme. A two-stage reaction sequence utilizing the activating enzyme and the ligase for the incorporation of d-alanine into membrane teichoic acid is suggested.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
