Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.8.1.4 (diaphorase)
 2,754 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Streptococcus pneumoniae strains lacking the enzyme dihydrolipoamide dehydrogenase (DLDH) show markedly reduced ability to grow on raffinose and stachyose as sole carbon sources. Import of these sugars occurs through the previously characterized raffinose ATP-binding cassette (ABC) transport system, encoded by the raf operon, that lacks the necessary ATP-binding protein. In this study, we identified the raffinose ATP-binding protein RafK and showed that it was directly involved in raffinose and stachyose import. RafK carries a C-terminal regulatory domain present in a subset of ATP-binding proteins that has been involved in both direct regulation of transporter activity (inducer exclusion) and transcription of transporter genes. Pneumococci lacking RafK showed a 50- to 80-fold reduction in expression of the raf operon genes aga (alpha-galactosidase) and rafEFG (raffinose substrate binding and permease genes), and both glucose and sucrose inhibited raffinose uptake through inducer exclusion. Like RafK, the presence of DLDH also activated the expression of raf operon genes, as DLDH-negative pneumococci showed a significantly decreased expression of aga and rafEFG, but DLDH did not regulate rafK or the putative regulatory genes rafR and rafS. DLDH also bound directly to RafK both in vitro and in vivo, indicating the possibility that DLDH regulates raffinose transport by a direct interaction with the regulatory domain of the transporter. Finally, although not as attenuated as DLDH-negative bacteria, pneumococci lacking RafK were significantly outcompeted by wild-type bacteria in colonization experiments of murine lung and nasopharynx, indicating a role for raffinose and stachyose transport in vivo.
 ...
PMID:Role of dihydrolipoamide dehydrogenase in regulation of raffinose transport in Streptococcus pneumoniae. 2160 35

The investigation of BDE-209 degradation by Microbacterium Y2 under different condition was conducted. Cell membrane permeability, cell surface hydrophobicity (CSH), membrane potential (MP) and reactive oxygen species (ROS) production were altered under BDE-209 stress. Eleven debrominated congeners were identified, suggesting that BDE-209 biodegradation by Microbacterium Y2 was dominantly a successive debromination process. Proteome analysis showed that the overexpression of haloacid dehalogenases, glutathione S-transferases (GSTs) and ATP-binding cassette (ABC) transporters might occupy important roles in BDE-209 biotransformation. Meanwhile, heat shock proteins (HSPs), ribonuclease E, oligoribonuclease (Orn) and ribosomal protein were activated to counter the BDE-209 toxicity. The up-regulated pyruvate dehydrogenase E1 component beta subunit and dihydrolipoamide dehydrogenase suggested that the pyruvate metabolism pathway was activated. Bioaugmentation of BDE-209 polluted water-sediments system with Microbacterium Y2 could efficiently improve BDE-209 removal. The detection of total 16S rRNA genes in treatment system suggested that Microbacterium (25.6 %), Luteimonas (14.3 %), Methylovorus (12.6 %), Hyphomicrobium (9.2 %) were the dominant genera and PICRUSt results further revealed that the diminution of BDE-209 was owed to cooperation between the introduced bacteria and aboriginal ones.
 ...
PMID:Proteomic mechanism of decabromodiphenyl ether (BDE-209) biodegradation by Microbacterium Y2 and its potential in remediation of BDE-209 contaminated water-sediment system. 3180 41