Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil.
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The characterized E. coli homolog establishes an NADH-dependent iron-sulfur flavoenzyme architecture for bacterial heteromeric DPD.
"dihydropyrimidine dehydrogenase is the first member of a novel NADH-dependent subclass of iron-sulfur flavoenzymes"
Pseudomonas putida PydR, a RutR-like transcriptional regulator, represses the dihydropyrimidine dehydrogenase gene in the pyrimidine reductive catabolic pathway.
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The paper identifies pydX and pydA as tandem KT2440 DPD genes.
"The putative DPD genes, pydX and pydA, are tandemly arranged in the Pseudomonas putida genome."
Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
UniProt record for pydX (Q88FQ1)
Manual evidence notes for pydX
OpenScientist deep research report for pydX