Revision 54884
Added by Sandro La Bruzzo over 5 years ago
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<identifier xmlns="http://www.openarchives.org/OAI/2.0/">10.17035/d.2017.0033099548</identifier> |
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<identifier identifierType="DOI">10.17035/d.2017.0033099548</identifier> |
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<creators> |
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<creator> |
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<creatorName>Bitto, E.</creatorName>
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<creatorName>Hroch L</creatorName>
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</creator> |
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<creator> |
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<creatorName>Wesenberg, G.E.</creatorName>
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<creatorName>Hughes RL</creatorName>
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</creator> |
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<creator> |
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<creatorName>Phillips Jr., G.N.</creatorName>
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<creatorName>Williams T</creatorName>
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</creator> |
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<creator> |
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<creatorName>McCoy, J.G.</creatorName>
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<creatorName>Angelastro A</creatorName>
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</creator> |
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<creator> |
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<creatorName>Bingman, C.A.</creatorName>
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<creatorName>Loveridge EJ</creatorName>
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</creator> |
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</creators> |
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<titles> |
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<title>Crystal Structure of a dimetal phosphatase from Danio rerio LOC 393393</title>
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<title >Data underpinning "Reduction of Folate by Dihydrofolate Reductase from Thermotoga maritima"</title>
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</titles> |
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<publisher>Cardiff University</publisher> |
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<publicationYear>2017</publicationYear> |
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<subjects> |
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<subject schemeURI="http://www.rcuk.ac.uk/research/efficiency/researchadmin/harmonisation/" subjectScheme="">Biomolecules and biochemistry</subject> |
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<dates> |
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<date dateType="Collected">2006-12-12</date>
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<date dateType="Issued">2017</date>
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<resourceType resourceTypeGeneral="Dataset">Dataset</resourceType> |
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<language>English</language> |
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<resourceType resourceTypeGeneral="Dataset">chromatography & mass spectromoetry data</resourceType> |
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<alternateIdentifier alternateIdentifierType="DOI">https://doi.org/10.17035/d.2017.0033099548</alternateIdentifier> |
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<relatedIdentifier relatedIdentifierType="DOI" relationType="IsReferencedBy" >10.1021/acs.biochem.6b01268</relatedIdentifier> |
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<formats> |
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<format>.inf, .dat, .idx, .sts, .txt</format> |
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</formats> |
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<version>None</version> |
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<descriptions> |
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<description descriptionType="Abstract">We have shown that DHFR from the hyperthermophilic bacterium Thermotoga maritima is able to catalyse reduction of folate to tetrahydrofolate with a similar efficiency to reduction of dihydrofolate under saturating conditions. NMR and mass spectrometry experiments showed no evidence for production of free dihydrofolate during either the EcDHFR- or TmDHFR-catalysed reductions of folate, suggesting that both enzymes perform the two reduction steps without release of the partially reduced substrate. Herein we include underpinning liquid chromatography - mass spectrometry data.</description> |
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