Structure and functional characterization of pyruvate decarboxylase from Gluconacetobacter diazotrophicus

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dc.contributor.authorvan Zyl, Leonardo Joaquim
dc.contributor.authorSchubert, Wolf-Dieter
dc.contributor.authorTuffin, Marla I.
dc.contributor.authorCowan, Donald A.
dc.date.accessioned2016-10-12T15:07:46Z
dc.date.available2016-10-12T15:07:46Z
dc.date.issued2014
dc.description.abstractBACKGROUND: Bacterial pyruvate decarboxylases (PDC) are rare. Their role in ethanol production and in bacterially mediated ethanologenic processes has, however, ensured a continued and growing interest. PDCs from Zymomonas mobilis (ZmPDC), Zymobacter palmae (ZpPDC) and Sarcina ventriculi (SvPDC) have been characterized and ZmPDC has been produced successfully in a range of heterologous hosts. PDCs from the Acetobacteraceae and their role in metabolism have not been characterized to the same extent. Examples include Gluconobacter oxydans (GoPDC), G. diazotrophicus (GdPDC) and Acetobacter pasteutrianus (ApPDC). All of these organisms are of commercial importance. RESULTS: This study reports the kinetic characterization and the crystal structure of a PDC from Gluconacetobacter diazotrophicus (GdPDC). Enzyme kinetic analysis indicates a high affinity for pyruvate (KM 0.06 mM at pH 5), high catalytic efficiencies, pHopt of 5.5 and Topt at 45 degrees C. The enzyme is not thermostable (T of 18 minutes at 60 degrees C) and the calculated number of bonds between monomers and dimers do not give clear indications for the relatively lower thermostability compared to other PDCs. The structure is highly similar to those described for Z. mobilis (ZmPDC) and A. pasteurianus PDC (ApPDC) with a rmsd value of 0.57 A for C? when comparing GdPDC to that of ApPDC. Indole-3-pyruvate does not serve as a substrate for the enzyme. Structural differences occur in two loci, involving the regions Thr341 to Thr352 and Asn499 to Asp503. CONCLUSIONS: This is the first study of the PDC from G. diazotrophicus (PAL5) and lays the groundwork for future research into its role in this endosymbiont. The crystal structure of GdPDC indicates the enzyme to be evolutionarily closely related to homologues from Z. mobilis and A. pasteurianus and suggests strong selective pressure to keep the enzyme characteristics in a narrow range. The pH optimum together with reduced thermostability likely reflect the host organisms niche and conditions under which these properties have been naturally selected for. The lack of activity on indole-3-pyruvate excludes this decarboxylase as the enzyme responsible for indole acetic acid production in G. diazotrophicus.en_US
dc.description.accreditationISIen_US
dc.identifier.citationvan Zyl et al. (2014). Structure and functional characterization of pyruvate decarboxylase from Gluconacetobacter diazotrophicus. BMC Structural Biology, 14: 21
dc.identifier.issn1472-6807
dc.identifier.urihttp://hdl.handle.net/10566/2444
dc.identifier.urihttp://dx.doi.org/10.1186/s12900-014-0021-1
dc.language.isoenen_US
dc.privacy.showsubmitterFALSE
dc.publisherBioMed Central
dc.rightsCopyright van Zyl et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0).
dc.source.urihttp://dx.doi.org/10.1186/s12900-014-0021-1
dc.status.ispeerreviewedTRUE
dc.subjectBacterial pyruvate decarboxylases (PDC)en_US
dc.subjectEthanol productionen_US
dc.subjectGluconacetobacter diazotrophicusen_US
dc.titleStructure and functional characterization of pyruvate decarboxylase from Gluconacetobacter diazotrophicusen_US
dc.typeArticleen_US

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