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Title: Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1

Abstract

The Gram-negative bacteriumSphingomonas wittichiiRW1 is notable for its ability to metabolize a variety of aromatic hydrocarbons. Not surprisingly, theS. wittichiigenome contains a number of putative aromatic hydrocarbon-degrading gene clusters. One of these includes an enzyme of unknown function, Swit_4259, which belongs to the acetoacetate decarboxylase-like superfamily (ADCSF). Here, it is reported that Swit_4259 is a small (28.8 kDa) tetrameric ADCSF enzyme that, unlike the prototypical members of the superfamily, does not have acetoacetate decarboxylase activity. Structural characterization shows that the tertiary structure of Swit_4259 is nearly identical to that of the true decarboxylases, but there are important differences in the fine structure of the Swit_4259 active site that lead to a divergence in function. In addition, it is shown that while it is a poor substrate, Swit_4259 can catalyze the hydration of 2-oxo-hex-3-enedioate to yield 2-oxo-4-hydroxyhexanedioate. It is also demonstrated that Swit_4259 has pyruvate aldolase-dehydratase activity, a feature that is common to all of the family V ADCSF enzymes studied to date. The enzymatic activity, together with the genomic context, suggests that Swit_4259 may be a hydratase with a role in the metabolism of an as-yet-unknown hydrocarbon. These data have implications for engineering bioremediation pathways to degrade specific pollutants, asmore » well as structure–function relationships within the ADCSF in general.« less

Authors:
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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Science Foundation (NSF)
OSTI Identifier:
1410117
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F, Structural Biology Communications
Additional Journal Information:
Journal Volume: 73; Journal Issue: 12; Journal ID: ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Mydy, Lisa S., Mashhadi, Zahra, Knight, T. William, Fenske, Tyler, Hagemann, Trevor, Hoppe, Robert W., Han, Lanlan, Miller, Todd R., Schwabacher, Alan W., and Silvaggi, Nicholas R. Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1. United States: N. p., 2017. Web. doi:10.1107/S2053230X17015862.
Mydy, Lisa S., Mashhadi, Zahra, Knight, T. William, Fenske, Tyler, Hagemann, Trevor, Hoppe, Robert W., Han, Lanlan, Miller, Todd R., Schwabacher, Alan W., & Silvaggi, Nicholas R. Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1. United States. doi:10.1107/S2053230X17015862.
Mydy, Lisa S., Mashhadi, Zahra, Knight, T. William, Fenske, Tyler, Hagemann, Trevor, Hoppe, Robert W., Han, Lanlan, Miller, Todd R., Schwabacher, Alan W., and Silvaggi, Nicholas R. Tue . "Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1". United States. doi:10.1107/S2053230X17015862.
@article{osti_1410117,
title = {Swit_4259, an acetoacetate decarboxylase-like enzyme from Sphingomonas wittichii RW1},
author = {Mydy, Lisa S. and Mashhadi, Zahra and Knight, T. William and Fenske, Tyler and Hagemann, Trevor and Hoppe, Robert W. and Han, Lanlan and Miller, Todd R. and Schwabacher, Alan W. and Silvaggi, Nicholas R.},
abstractNote = {The Gram-negative bacteriumSphingomonas wittichiiRW1 is notable for its ability to metabolize a variety of aromatic hydrocarbons. Not surprisingly, theS. wittichiigenome contains a number of putative aromatic hydrocarbon-degrading gene clusters. One of these includes an enzyme of unknown function, Swit_4259, which belongs to the acetoacetate decarboxylase-like superfamily (ADCSF). Here, it is reported that Swit_4259 is a small (28.8 kDa) tetrameric ADCSF enzyme that, unlike the prototypical members of the superfamily, does not have acetoacetate decarboxylase activity. Structural characterization shows that the tertiary structure of Swit_4259 is nearly identical to that of the true decarboxylases, but there are important differences in the fine structure of the Swit_4259 active site that lead to a divergence in function. In addition, it is shown that while it is a poor substrate, Swit_4259 can catalyze the hydration of 2-oxo-hex-3-enedioate to yield 2-oxo-4-hydroxyhexanedioate. It is also demonstrated that Swit_4259 has pyruvate aldolase-dehydratase activity, a feature that is common to all of the family V ADCSF enzymes studied to date. The enzymatic activity, together with the genomic context, suggests that Swit_4259 may be a hydratase with a role in the metabolism of an as-yet-unknown hydrocarbon. These data have implications for engineering bioremediation pathways to degrade specific pollutants, as well as structure–function relationships within the ADCSF in general.},
doi = {10.1107/S2053230X17015862},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
issn = {2053-230X},
number = 12,
volume = 73,
place = {United States},
year = {2017},
month = {11}
}