4857-75-4

Basic information

• Product Name: 1,2,4-triacetoxy-5-tert-butylbenzene
• Synonyms: 1,2,4-triacetoxy-5-tert-butylbenzene
• CAS NO: 4857-75-4
• Molecular Weight: 308.331
• Mol File: 4857-75-4.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: 1,2,4-triacetoxy-5-tert-butylbenzene(CAS DataBase Reference)
• NIST Chemistry Reference: 1,2,4-triacetoxy-5-tert-butylbenzene(4857-75-4)
• EPA Substance Registry System: 1,2,4-triacetoxy-5-tert-butylbenzene(4857-75-4)

Safety Data

• Hazardous Substances Data: 4857-75-4(Hazardous Substances Data)

Upstream product

• 88-58-4 2,5-bis(1,1-dimethylethyl)-1,4-benzenediol 
• 98-29-3 4-tert-Butylcatechol 
• 533-73-3 1,2,4-Trihydroxybenzene 
• 4857-70-9 2-tert-butyl-5-hydroxy-1,4-benzoquinone 
• 108-24-7 acetic anhydride 
• 4857-74-3 5-tert-butyl-1,2,4-trihydroxybenzene 
• 2460-77-7 2,5-di-tert-butyl-p-benzoquinone 

Relevant articles and documents

Mechanism-based cofactor derivatization of a copper amine oxidase by a branched primary amine recruits the oxidase activity of the enzyme to turn inactivator into substrate

The copper amine oxidases (CAOs) have evolved to catalyze oxidative deamination of unbranched primary amines to aldehydes. We report that a branched primary amine bearing an aromatization-prone moiety, ethyl 4-amino-4,5- dihydrothiophene-2-carboxylate (1), is recognized enantioselectively (S ? R) by bovine plasma amine oxidase (BPAO) both as a temporary inactivator and as a substrate. Substrate activity results from an O2-dependent turnover of the covalently modified enzyme, with release of 4-aminothiophene-2- carboxylate (2) as ultimate product. Interaction of (S)-1 with BPAO occurs within the enzyme active site with a dissociation constant of 0.76 μM. Evidence from kinetic and spectroscopic studies, and HPLC analysis of stoichiometric reactions of BPAO with (S)-1, combined with a model study using a quinone cofactor mimic, establishes that the enzyme metabolizes 1 according to a transamination mechanism. Following the initial isomerization of substrate Schiff base to product Schiff base, a facile aromatization of the latter results in a metastable N-aryl derivative of the reduced cofactor aminoresorcinol, which is catalytically inactive. The latter derivative is then slowly oxidized by O2, apparently facilitated partially by the active-site Cu(II), to form a quinonimine of the native cofactor that releases 2 upon hydrolysis or transimination with substrate amine. Preferential metabolism of (S)-1 is consistent with the preferential removal of the pro-S α-proton in metabolism of benzylamine by BPAO. This study represents the first report of product identification in metabolism of a branched primary amine by a copper amine oxidase and suggests a novel type of reversible mechanism-based (covalent) inhibition where inhibition lifetime can be fine-tuned independently of inhibition potency.