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dc.contributor.authorUthaiwan Suttisansaneeen_US
dc.contributor.authorYanhong Ranen_US
dc.contributor.authorKadia Y. Mullingsen_US
dc.contributor.authorNicole Sukdeoen_US
dc.contributor.authorJohn F. Honeken_US
dc.contributor.otherUniversity of Waterlooen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherJinan Universityen_US
dc.contributor.otherGreenLight Biosciencesen_US
dc.contributor.otherUniversity of Northern British Columbiaen_US
dc.date.accessioned2018-11-23T09:44:31Z-
dc.date.available2018-11-23T09:44:31Z-
dc.date.issued2015-04-01en_US
dc.identifier.citationMetallomics. Vol.7, No.4 (2015), 605-612en_US
dc.identifier.issn1756591Xen_US
dc.identifier.issn17565901en_US
dc.identifier.other2-s2.0-84927646710en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84927646710&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/35480-
dc.description.abstract© 2015 The Royal Society of Chemistry. Metabolically produced methylglyoxal is a cytotoxic compound that can lead to covalent modification of cellular DNA, RNA and protein. One pathway to detoxify this compound is via the glyoxalase enzyme system. The first enzyme of this detoxification system, glyoxalase I (GlxI), can be divided into two classes according to its metal activation profile, a Zn2+-activated class and a Ni2+-activated class. In order to elucidate some of the key structural features required for selective metal activation by these two classes of GlxI, deletional mutagenesis was utilized to remove, in a step-wise fashion, a key α-helix (residues 73-87) and two small loop regions (residues 99-103 and 111-114) from the Zn2+-activated Pseudomonas aeruginosa GlxI (GloA3) in order to mimic the smaller Ni2+-activated GlxI (GloA2) from the same organism. This approach was observed to clearly shift the metal activation profile of a Zn2+-activated class GlxI into a Ni2+-activated class GlxI enzyme. The α-helix structural component was found to contribute significantly toward GlxI metal specificity, while the two small loop regions were observed to play a more crucial role in the magnitude of the enzymatic activity. The current study should provide additional information on the fundamental relationship of protein structure to metal selectivity in these metalloenzymes.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84927646710&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemistryen_US
dc.subjectMaterials Scienceen_US
dc.titleModulating glyoxalase i metal selectivity by deletional mutagenesis: Underlying structural factors contributing to nickel activation profilesen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1039/c4mt00299gen_US
Appears in Collections:Scopus 2011-2015

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