Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0378-1097(01)00393-7
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dc.titleIdentification of amino acid residues essential for catalytic activity of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867
dc.contributor.authorChua, C.H.
dc.contributor.authorFeng, Y.
dc.contributor.authorYeo, C.C.
dc.contributor.authorPoh, C.L.
dc.contributor.authorKhoo, H.E.
dc.date.accessioned2012-03-28T06:05:50Z
dc.date.available2012-03-28T06:05:50Z
dc.date.issued2001
dc.identifier.citationChua, C.H., Feng, Y., Yeo, C.C., Poh, C.L., Khoo, H.E. (2001). Identification of amino acid residues essential for catalytic activity of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867. FEMS Microbiology Letters 204 (1) : 141-146. ScholarBank@NUS Repository. https://doi.org/10.1016/S0378-1097(01)00393-7
dc.identifier.issn03781097
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/31468
dc.description.abstractGentisate 1,2-dioxygenase (GDO, EC 1.13.11.4) is a ring cleavage enzyme that utilizes gentisate as a substrate yielding maleylpyruvate as the ring fission product. Mutant GDOs were generated by both random mutagenesis and site-directed mutagenesis of the gene cloned from Pseudomonas alcaligenes NCIB 9867. Alignment of known GDO sequences indicated the presence of a conserved central core region. Mutations generated within this central core resulted in the complete loss of enzyme activity whereas mutations in the flanking regions yielded GDOs with enzyme activities that were reduced by up to 78%. Site-directed mutagenesis was also performed on a pair of highly conserved HRH and HXH motifs found within this core region. Conversion of these His residues to Asp resulted in the complete loss of catalytic activity. Mutagenesis within the core region could have affected quaternary structure formation as well as cofactor binding. A mutant enzyme with increased catalytic activities was also characterized. © 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0378-1097(01)00393-7
dc.sourceScopus
dc.subjectCatalytic activity
dc.subjectGentisate 1,2-dioxygenase
dc.subjectMutagenesis
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1016/S0378-1097(01)00393-7
dc.description.sourcetitleFEMS Microbiology Letters
dc.description.volume204
dc.description.issue1
dc.description.page141-146
dc.description.codenFMLED
dc.identifier.isiut000172003700025
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