The bioremediator glycerophosphodiesterase employs a non-processive mechanism for hydrolysis.
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Hadler, Kieran S; Grahan, Lawrence R; Ollis, David; Schenk, Gerhard
Description
Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a binuclear metallohydrolase that catalyzes the breakdown of a broad range of phosphate ester substrates, and it is of interest for its potential application in the destruction of organophosphate nerve agents and pesticides. The reaction mechanism of GpdQ has been proposed to involve a nucleophilic attack by a terminally bound hydroxide molecule. The hydroxide species bridging the two metal ions is suggested to activate the...[Show more]
dc.contributor.author | Hadler, Kieran S | |
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dc.contributor.author | Grahan, Lawrence R | |
dc.contributor.author | Ollis, David | |
dc.contributor.author | Schenk, Gerhard | |
dc.date.accessioned | 2015-12-07T22:24:47Z | |
dc.identifier.issn | 0162-0134 | |
dc.identifier.uri | http://hdl.handle.net/1885/20984 | |
dc.description.abstract | Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes is a binuclear metallohydrolase that catalyzes the breakdown of a broad range of phosphate ester substrates, and it is of interest for its potential application in the destruction of organophosphate nerve agents and pesticides. The reaction mechanism of GpdQ has been proposed to involve a nucleophilic attack by a terminally bound hydroxide molecule. The hydroxide species bridging the two metal ions is suggested to activate the nucleophile, thus favoring a sequential rather than a processive mechanism of action. Here, the hydrolysis of the two ester bonds in the substrate bis(para-nitrophenyl) phosphate (bpNPP) is probed using 31P NMR. The kinetic rates measured compare well with those determined spectrophotometrically. Furthermore, the data indicate that the diester bonds are cleaved in two separate (non-processive) reactions, indicating that only a single nucleophile (the terminal hydroxide molecule) is likely to be employed as a nucleophile for GpdQ. | |
dc.publisher | Elsevier | |
dc.source | Journal of Inorganic Biochemistry | |
dc.subject | Keywords: glycerophosphodiesterase; hydroxide; metal ion; nucleophile; phosphodiesterase; unclassified drug; article; catalysis; chemical bond; Enterobacter aerogenes; hydrolysis; nonhuman; phosphorus nuclear magnetic resonance; reaction analysis; spectrophotometry 31P NMR; Binuclear metallohydrolases; Processive mechanism; Reaction mechanism; Sequential mechanism | |
dc.title | The bioremediator glycerophosphodiesterase employs a non-processive mechanism for hydrolysis. | |
dc.type | Journal article | |
local.description.notes | Imported from ARIES | |
local.identifier.citationvolume | 104 | |
dc.date.issued | 2010 | |
local.identifier.absfor | 060112 - Structural Biology (incl. Macromolecular Modelling) | |
local.identifier.ariespublication | u2544221xPUB15 | |
local.type.status | Published Version | |
local.contributor.affiliation | Hadler, Kieran S, University of Queensland | |
local.contributor.affiliation | Grahan, Lawrence R, University of Queensland | |
local.contributor.affiliation | Ollis, David, College of Physical and Mathematical Sciences, ANU | |
local.contributor.affiliation | Schenk, Gerhard, University of Queensland | |
local.description.embargo | 2037-12-31 | |
local.bibliographicCitation.issue | 2 | |
local.bibliographicCitation.startpage | 211 | |
local.bibliographicCitation.lastpage | 213 | |
local.identifier.doi | 10.1016/j.jinorgbio.2009.10.012 | |
dc.date.updated | 2016-02-24T09:51:22Z | |
local.identifier.scopusID | 2-s2.0-71849093760 | |
local.identifier.thomsonID | 000273448100016 | |
Collections | ANU Research Publications |
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