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

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

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 acti...

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Bibliographic Details
Published in:Biochemical journal Vol. 394; no. Pt 3; pp. 665 - 674
Main Authors: Tirrell, Isaac M, Wall, Jennifer L, Daley, Christopher J, Denial, Sarah J, Tennis, Frances G, Galens, Kevin G, O'Handley, Suzanne F
Format: Journal Article
Language:English
Published: England Portland Press Ltd 15-03-2006
Subjects:
Adenosine Diphosphate - metabolism
Alcohols - metabolism
Amino Acid Sequence
Bacteria - enzymology
Carbohydrate Metabolism
Cloning, Molecular
Enzyme Stability
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Nudix Hydrolases
Paenibacillus thiaminolyticus
Phosphoric Monoester Hydrolases - chemistry
Phosphoric Monoester Hydrolases - classification
Phosphoric Monoester Hydrolases - genetics
Phosphoric Monoester Hydrolases - metabolism
Phosphorylation
Protein Structure, Tertiary
Pyrophosphatases - chemistry
Pyrophosphatases - classification
Pyrophosphatases - genetics
Pyrophosphatases - metabolism
Sequence Homology, Amino Acid
Substrate Specificity
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Summary: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.
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj20051172