High impact information on NSC 9807

• The equilibrium dissociation constants for calcium, substrate analogs, reaction products, and several competitive inhibitors bound to the enzyme at the interface were determined by monitoring the ligand-conferred protection of the active site histidine residue from alkylation by phenacyl bromide [1].
• Saturation kinetics with chloroacetophenone and bromoacetophenone indicated interaction at a specific site on the enzyme surface and gave a dissociation constant similar to that from steady-state kinetics, suggesting that the same processes were being observed by both methods and that the active site may be involved [2].
• Human liver aldehyde dehydrogenase isozymes E1 and E2 (EC 1.2.1.3) are both completely and irreversibly inactivated by bromoacetophenone (2-bromo-1-phenylethanone) [2].
• The cyclization of arylhydrazones of less reactive halides such as 2-chlorobenzaldehyde, as well as 2-bromoacetophenone and bromotetralone, has been achieved [3].
• An azido derivative of the oligomycin sensitivity conferring protein (OSCP) was prepared by alkylation with the bifunctional reagent p-azido phenacyl bromide [4].

Associations of NSC 9807 with other chemical compounds

• A series of 18 phenacyl bromide and iodoacetamide analogues have been synthesized and used to alkylate Met-398 situated in the S'1 binding site of carboxypeptidase Y [5].
• High-performance liquid chromatographic determination of cytosine-containing compounds by precolumn fluorescence derivatization with phenacyl bromide: application to antiviral nucleosides and nucleotides [6].
• An expeditious route to the two major metabolites of Zolpidem-and readily applicable to the synthesis of the drug-was established via a cyclization reaction between a 2-aminopyridine and a suitable alpha-bromoacetophenone [7].
• Another phospholipase A2 inhibitor 4-bromo phenacyl bromide was ineffective in vivo and in vitro alike, as well as the cyclooxygenase inhibitor indomethacin [8].

Gene context of NSC 9807

• Treatment of lecithin-cholesterol acyltransferase or B10-reacting phospholipases with phenacyl bromide, a reagent known to interact with the active site of phospholipase A2, inhibited both their esterolytic activity and their capacity to bind to B10 [9].
• Two photoactivable reagents were used: para azido phenacyl bromide (pAPA) which reacts with the SH of the ACP prosthetic group and the N-hydroxysuccinimide ester of 4-azido salicylic acid (NHS-ASA) which reacts with the amino groups of the protein [10].
• ((1977) Biochem. Biophys. Res. Commun. 74, 384-389) that phenacyl bromide reacts with a single reactive sulfhydryl group of aconitase, abolishing enzyme activity [11].

Analytical, diagnostic and therapeutic context of NSC 9807

• Twenty-two biologically relevant (6:0-22:6) saturated, monounsaturated and polyunsaturated fatty acids were separated by reversed-phase high-performance liquid chromatography after derivatization with phenacyl bromide [12].

References