Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.23.17 (
PCE
)
1,301
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Cell-free extracts of Clostridium bifermentans DPH-1 catalyzed tetrachloroethylene (
PCE
) dechlorination.
PCE
degradation was stimulated by addition of a variety of electron donors. Ethanol (0.61 mM) was the most effective electron donor for
PCE
dechlorination. Maximum activity was recorded at 30 degrees C and pH 7.5. Addition of
NADH
as a cofactor stimulated enzymatic activity but the activity was not stimulated by addition of metal ions. When the cell-free enzyme extract was incubated in the presence of titanium citrate as a reducing agent, the dehalogenase was rapidly inactivated by propyl iodide (0.5 mM). The activity of propyliodide-reacted enzyme was restored by illumination with a 250 W lamp. The dehalogenase activity was also inhibited by cyanide. The substrate spectrum of activity included trichloroethylene (TCE), cis-1,2-dichloroethylene (cDCE), trans-dichloroethylene, 1,1-dichloroethylene, 1,2-dichloroethane, and 1,1,2-trichloroethane. The highest rate of degradation of the chlorinated aliphatic compounds was achieved with
PCE
, and
PCE
was principally degraded via TCE to cDCE. Results indicate that the dehalogenase could play a vital role in the breakdown of
PCE
as well as a variety of other chlorinated aliphatic compounds.
...
PMID:In vitro dehalogenation of tetrachloroethylene (PCE) by cell-free extracts of Clostridium bifermentans DPH-1. 1133 32
