Publications by authors named "Anthony J Zmuda"

Article Synopsis
  • Metformin is a widely used diabetes medication that often remains unremoved in wastewater, leading to environmental pollution and potential toxicity in freshwater systems.
  • Researchers identified specific Pseudomonads bacteria that can break down metformin and biguanide as their nitrogen sources, revealing a promising method for bioremediation.
  • Genetic studies revealed key enzymes involved in this breakdown, including a Ni-dependent hydrolase and an aminohydrolase, suggesting Pseudomonads have evolved new capabilities to convert these pollutants into less harmful substances like guanylurea.
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A prevalent side-reaction of succinate dehydrogenase oxidizes malate to enol-oxaloacetate (OAA), a metabolically inactive form of OAA that is a strong inhibitor of succinate dehydrogenase. We purified from cow heart mitochondria an enzyme (OAT1) with OAA tautomerase (OAT) activity that converts enol-OAA to the physiological keto-OAA form, and determined that it belongs to the highly conserved and previously uncharacterized Fumarylacetoacetate_hydrolase_domain-containing protein family. From all three domains of life, heterologously expressed proteins were shown to have strong OAT activity, and ablating the OAT1 homolog caused significant growth defects.

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At least a quarter of the protein-encoding genes in plant genomes are predicted to encode enzymes for which no physiological function is known. Determining functions for these uncharacterized enzymes is key to understanding plant metabolism. Functional characterization typically requires expression and purification of recombinant enzymes to be used in enzyme assays and/or for protein structure elucidation studies.

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