16053-97-7

Upstream product

• 2411-83-8 methyl-2,3-dihydroxybenzoate 
• 932380-54-6 N-(benzyloxy)-2,3-dihydroxybenzamide 
• 74272-78-9 2,3-dibenzyloxybenzoic acid 
• 2169-27-9 Methyl 2,3-bis(benzyloxy)benzoate 

Downstream Products

• 904329-71-1 C₁₇H₁₉N₆O₁₀P 

Relevant academic research and scientific papers

Benzoic hydroxamate-based iron complexes as model compounds for humic substances: Synthesis, characterization and algal growth experiments

A series of monomeric and dimeric FeIII complexes bearing benzoic hydroxamates as O,O-chelates has been prepared and characterized by elemental analysis, IR spectroscopy, UV-Vis spectroscopy, electrospray ionization mass spectrometry (ESI-MS), cyclic voltammetry, EPR spectroscopy and for some examples by X-ray diffraction analysis. The stability of the synthesized complexes in pure water and seawater was monitored over 24 h by means of UV-Vis spectrometry. The ability to release iron from the synthesized model complexes has been investigated with algae growth experiments.

Inhibitors of the FEZ-1 metallo-β-lactamase

Metallo-β-lactamases (MBLs) catalyze the hydrolysis of β-lactams including penicillins, cephalosporins and carbapenems. Starting from benzohydroxamic acid (1) structure-activity studies led to the identification of selective inhibitors of the FEZ-1 MBL, e.g., 2,5-substituted benzophenone hydroxamic acid 17 has a Ki of 6.1 ± 0.7 μM against the FEZ-1 MBL but does not significantly inhibit the IMP-1, BcII, CphA or L1 MBLs.

Nanomolar inhibition of the enterobactin biosynthesis enzyme, EntE: Synthesis, substituent effects, and additivity

2,3-Dihydroxybenzohydroxamoyl adenylate (I) was prepared as a potential product analog inhibitor of EntE (EC# 2.7.7.58), a 2,3-dihydroxybenzoate AMP ligase from Escherichia coli that is required for the biosynthesis of enterobactin. This compound, obtained by the aqueous reaction of imidazole-activated adenosine 5′-phosphate and 2,3-dihydroxybenzohydroxamic acid, is a competitive inhibitor with a Ki value of 4.5 × 10-9 M. Deletion of the catecholic 3-OH group of (I), in compound (II), reduced inhibitory activity by a factor of 3.5, whereas, removal of both the 3-OH and 2-OH groups, in (III), reduced inhibitory activity by a factor of ～2000. Acetohydroxamoyl adenylate (IV), in which the entire catechol moiety of (I) is replaced by a hydrogen atom, gave {less-than or slanted equal to}10% inhibition at 6 × 10-4 M, indicating a reduction in affinity by more than 105. The binding free energy of (I) is nearly equivalent to the sum of the corresponding values for adenosine 5′-phosphate and 2,3-dihydroxybenzoate.

Protective solutions for organs

Described is a protective solution for avoiding ischemic, storage or ischemia/reperfusion to organs, or to isolated cell systems, or to tissue components after perfusion, surgery, transplantation, or cryopreservation and subsequent reperfusion, which contains alkali ions, and if need be also alkaline earth ions as the electrolyte, a buffer e.g. on a histidine derivation basis, as well as a polyol and/or a saccharide, has an osmolarity of about 290 mosm/l to about 350 mosm/l, as well as a pH value of about 6.8 to about 7.4, and to which hydroxamic acid, and/or one or more hydroxamic acid derivatives are added.

Method of treating hemoglobinopathies

A therapeutic process for treating anemias in primates, including man, particularly those anemias of genetic origin including sickle-cell anemia, which comprises administering to an anemic primate an amount of a polyhydroxy benzoic, mandelic or phenylacetic acid derivative as specified at a dose level sufficient to increase fetal hemoglobin.

HYDROXY BENZOHYDROXAMIC ACIDS AND BENZAMIDES

Di or trihydroxybenzohydroxamic acids or N-substituted benzamides, inhibitors or ribonucleotide reductase

Synthesis of hydroxy- and amino-substituted benzohydroxamic acids: Inhibition of ribonucleotide reductase and antitumor activity

Benzohydroxamic acids inhibit mammalian ribonucleotide reductase and exhibit antineoplastic activity in L1210 leukemic mice. Five new hydroxy- and amino-substituted benzohydroxamic acids (3,4- and 3,5-OH,3,4-NH2, 2,3,4-, and 3,4,5-OH) were prepared and tested along with 12 previously reported benzohydroxamic acids (BHA) for enzyme inhibition and antitumor activity. The most potent enzyme inhibitor in this series was 2,3,4-OH-BHA (ID50=3.5 μM), which is 140 times more potent than hydroxyurea, but its toxicity limited the antitumor activity to a 30% increase in life span of L1210 bearing mice at 125 (mg/kg) day ip for 8 days. The most effective antitumor agent in this series was 3,4-OH-BHA which prolonged the life span of L1210 bearing mice 103% at 600 (mg/kg)/day ip for 8 days.