High impact information on NSC2527

• O6-Benzylguanine acts by virtue of its ability to serve as a substrate for the AGT forming S-benzylcysteine at the cysteine acceptor site [1].
• The Vmax for S-benzyl-L-cysteine sulfoxide formation by kidney microsomes was nearly 3-fold greater than the rate measured with liver microsomes [2].
• Further characterization and purification of the flavin-dependent S-benzyl-L-cysteine S-oxidase activities of rat liver and kidney microsomes [3].
• Further evidence for FMO1 being the major FMO isoform involved in S-benzyl-L-cysteine sulfoxidation was obtained from kinetic studies with cDNA-expressed rabbit FMOs [4].
• Isolated hepatocytes rapidly accumulated S-benzylcysteine by a carrier-mediated mechanism and metabolized it to the N-acetylcysteine conjugate [5].

Biological context of NSC2527

• We succeeded in showing that OK cells absorb S-benzyl-L-cysteine via an active transport system which is inhibitable by phenylalanine [6].

Gene context of NSC2527

• From placental extracts two activity peaks (CAS I and II) hydrolysing S-benzyl L-cysteine paranitroanilide were separated on DEAE Sephacel [7].
• Formation of a dehydroalanyl residue from S-benzylcysteine upon HF cleavage of a [Sar1, Cys8]-angiotensin II peptide resin [8].
• The multiple forms of S-benzyl-L-cysteine-beta-naphthylamide hydrolase (oxytocinase) in human pregnancy sera demonstrated by the method of isoelectric fractionation [9].

References