Disease relevance of poxB

• Complete cross-reactivity was found with antibodies directed against the pyruvate dehydrogenase complex from E. coli and electron micrographs of both enzyme complexes reveal identical structures [1].
• The gene was named poxB for Pseudomonas oxacillinase [2].
• Serum reactivity against bacterial pyruvate dehydrogenase: Increasing the specificity of anti-mitochondrial antibodies for the diagnosis of primary biliary cirrhosis [3].

High impact information on poxB

• A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct [4].
• Strain YYC202 (aceEF pfl poxB pps) generated 90 g/liter lactate in 16 h during the anaerobic phase (with a yield of 0.95 g/g and a productivity of 5.6 g/liter . h) [5].
• Pirin regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase e1 subunit and modulating pyruvate dehydrogenase activity [6].
• Genetic and biochemical analyses of the mutant revealed the downregulation of many TCA cycle enzymes, including citrate synthase, and the upregulation of the pyruvate dehydrogenase complex in both transcription and enzyme activities [7].
• Cloning and expression of poxB in Escherichia coli conferred beta-lactam resistance to the host [2].

Chemical compound and disease context of poxB

• Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex [8].

Biological context of poxB

• The results support the view that synthesis of the PDH complex is regulated from the pdhR promoter of a pdhR-aceEF-lpd operon [9].
• Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution [10].

Associations of poxB with chemical compounds

• VAL22 is a single mutant with an inactivated poxB gene that codes for pyruvate oxidase which converts pyruvate to acetate [11].
• Reassociation to a fully active complex molecule works with equal facility between the pyruvate dehydrogenase component and a dihydrolipoamide transacetylase: dihydrolipoamide dehydrogenase subcomplex from either organism in all possible combinations [1].

Enzymatic interactions of poxB

• VAL24 is a triple mutant with ldhA and pflB deleted and poxB inactivated [11].

Analytical, diagnostic and therapeutic context of poxB

• Protein pull-down and bacterial two-hybrid assays followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electrospray ionization-tandem mass spectrometry analyses showed the pyruvate dehydrogenase (PDH) E1 subunit as a component interacting with the pirin(Sm) gene [6].

References