From protease to decarboxylase: the molecular metamorphosis of phosphatidylserine decarboxylase

Choi, J.-Y., Duraisingh, M. T., Marti, M. , Ben Mamoun, C. and Voelker, D. R. (2015) From protease to decarboxylase: the molecular metamorphosis of phosphatidylserine decarboxylase. Journal of Biological Chemistry, 290(17), pp. 10972-10980. (doi:10.1074/jbc.M115.642413) (PMID:25724650) (PMCID:PMC4409258)

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Abstract

Background: Phosphatidylserine decarboxylase (PSD) undergoes an autoendoproteolytic cleavage but the mechanism has not been defined.

Results: PSD proenzyme processing occurs by a canonical serine protease mechanism catalyzed by a conserved aspartate-histidine-serine triad.

Conclusion: PSD proenzyme executes a proteolytic reaction in cis that creates the active site of the decarboxylase.

Significance: The mechanism of autoendoproteolyic processing of PSDs across phyla has been elucidated.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Marti, Professor Matthias
Authors: Choi, J.-Y., Duraisingh, M. T., Marti, M., Ben Mamoun, C., and Voelker, D. R.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
ISSN (Online):1083-351X
Published Online:26 February 2015
Copyright Holders:Copyright © 2015 The American Society for Biochemistry and Molecular Biology, Inc.
First Published:First published in Journal of Biological Chemistry 290(17):10972-10980
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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