Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.2.1.7 (BAL)
 1,977 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Interactions of dithiols with p-aminophenyldichloroarsine (APA) and with Torpedo nicotinic receptors were studied using two approaches. First, the stability of dithiol-APA complexes in solution was studied based on quenching thiol reactions with dithiobis-(nitrobenzoic acid). A peptide corresponding to a portion of the Torpedo alpha-subunit and various 1,2-dithiols such as 2,3-dimercaptopropanesulfonic acid (DMPS), 2,3-dimercaptosuccinic acid formed stable complexes with APA, while 1,4-dithiols, such as dithiothreitol (DTT) and 2,5 dimercapto-N,N,N'N'-tetradipamide (DTA) did not. The Kd of APA association with DTT in Tris buffer is 2 microM. These data suggest that APA has greater affinity for reduced nicotinic receptors than for either DTT or DTA, a prediction that was experimentally confirmed, since these reagents do not reverse the effects of APA on nicotinic receptors. Second, application of DMPS and BAL, but not 2,3-dimercaptosuccinic acid, to DTT-treated receptors both reversed the effects of APA-receptor complexes and prevented alkylation by bromoacetylcholine, suggesting that DMPS and BAL "oxidize" reduced nicotinic receptors. The presence of air is required for this "oxidizing" effect, but no clear mechanism was discovered, since prevention of formation of the reactive oxygen species superoxide, hydrogen peroxide, or hydroxyl radicals failed to block oxidation. These data suggest that oxygen reacts with dithiols to produce unknown reactive species that directly oxidize reduced nicotinic receptors, although other interpretations are still possible.
 ...
PMID:Interactions of dithiols with p-aminophenyldichloroarsine and nicotinic acetylcholine receptors. 805 Nov 36

The thiamin-diphosphate-dependent enzyme benzaldehyde lyase is a very import catalyst for chemoenzymatic synthesis catalyzing the formation and cleavage of (R)-hydroxy ketones. We have studied the stability of the recombinant enzyme and some enzyme variants with respect to pH, temperature, buffer salt, cofactors and organic cosolvents. Stability of BAL in chemoenzymatic synthesis requires the addition of cofactors to the buffer. Reaction temperature should not exceed 37 degrees C. The enzyme is stable between pH 6 and 8, with pH 8 being the pH-optimum of both the lyase and the ligase reaction. Potassium phosphate and Tris were identified as optimal reaction buffers and the addition of 20 vol% DMSO is useful to enhance both the solubility of aromatic substrates and products and the stability of BAL. The initial broad product range of BAL-catalyzed reactions has been enlarged to include highly substituted hydroxybutyrophenones and aliphatic acyloins.
 ...
PMID:Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C-C bond formation. 1707 94