YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily

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dc.contributor.author Tirrell, Isaac en_US
dc.contributor.author Wall, Jennifer en_US
dc.contributor.author Daley, Christopher en_US
dc.contributor.author Denial, Sarah en_US
dc.contributor.author Tennis, Frances en_US
dc.contributor.author Galens, Kevin en_US
dc.contributor.author O'Handley, Suzanne en_US
dc.date.accessioned 2006-07-19T19:52:06Z en_US
dc.date.available 2006-07-19T19:52:06Z en_US
dc.date.issued 2006-03-15 en_US
dc.identifier.citation Biochemical Journal 394N3 (2006) 665-674 en_US
dc.identifier.issn 1470-8728 en_US
dc.identifier.uri http://hdl.handle.net/1850/2205 en_US
dc.description Article may be found at: http://www.biochemj.org/bj/394/bj3940665.htm en_US
dc.description.abstract YZGD from Paenibacillus thiaminolyticus is a novel bifunctional enzyme with both PLPase (pyridoxal phosphatase) and Nudix (nucleoside diphosphate x) hydrolase activities. The PLPase activity is catalysed by the HAD (haloacid dehalogenase) superfamily motif of the enzyme, and the Nudix hydrolase activity is catalysed by the conserved Nudix signature sequence within a separate portion of the enzyme, as confirmed by site-directed mutagenesis. YZGD's phosphatase activity is very specific, with pyridoxal phosphate being the only natural substrate, while YZGD's Nudix activity is just the opposite, with YZGD being the most versatile Nudix hydrolase characterized to date. YZGD's Nudix substrates include the CDP-alcohols (CDP-ethanol, CDP-choline and CDP-glycerol), the ADP-coenzymes (NADH, NAD and FAD), ADP-sugars, TDP-glucose and, to a lesser extent, UDP- and GDP-sugars. Regardless of the Nudix substrate, one of the products is always a nucleoside monophosphate, suggesting a role in nucleotide salvage. Both the PLPase and Nudix hydrolase activities require a bivalent metal cation, but while PLPase activity is supported by Co2+, Mg2+, Zn2+ and Mn2+, the Nudix hydrolase activity is Mn2+-specific. YZGD's phosphatase activity is optimal at an acidic pH (pH 5), while YZGD's Nudix activities are optimal at an alkaline pH (pH 8.5). YZGD is the first enzyme reported to be a member of both the HAD and Nudix hydrolase superfamilies, the first PLPase to be recognized as a member of the HAD superfamily and the first Nudix hydrolase capable of hydrolysing ADP-x, CDP-x and TDP-x substrates with comparable substrate specificity. en_US
dc.format.extent 38490 bytes en_US
dc.format.mimetype application/pdf en_US
dc.language.iso en_US en_US
dc.publisher Portland Press: Biochemical Journal en_US
dc.subject ADP-coenzyme en_US
dc.subject Hydrolases en_US
dc.subject Nudix en_US
dc.title YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily en_US
dc.type Abstract en_US

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