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Synthesis of Benzohydroxamic Acid 3 The synthesis of compound 3 was achieved by reacting methyl benzoate 1 and hydroxylamine 2. Synthesis of Hydroxamates Using N, N1, NII–trimethoxy-N, NI, NII-trimethyl Phosphorus Triamides 5 Nui et al 31 reported the conversion of aromatic and aliphatic carboxylic acids, including sterically hindered substrates directly to hydroxamates using N, NI, NII-trimethoxy-N, NI, NII–trimethyl phosphorus triamide 5. On condensation of aromatic or aliphatic carboxylic acid 4 0.01M and compound 5 0.005M in toluene at 60 for 0.5 to 1 h, the hydroxamate 6 was obtained in excellent yield. Ester Synthesis of Hydroxamate Riva et al 32 reported the transformation of methyl or ethyl carboxylic esters into the corresponding hydroxamic acid. Protection of the commercially available hydro ester 22 with tertiary-butyldimethylsilyl chloride TBDMS-Cl gave silyl ester 23.

The broad biological activities of hydroxamates and the need to improve on their synthetic routes informed the review of their synthesis and biological applications. 5, 6 A number of synthetic routes are available for the preparation of hydroxamic acids, 7-12 but some are tedious, time consuming and costly as well. Colombo, An improved synthesis of the HDAC inhibitorn trichostatin A, Master s Theses and Doctoral Dissertations, Eastern Michigan University, 2009, 1-2. Keywords: Keyword Histone deacetylase inhibitors, Matrix metalloproteinase inhibitors, HIV, Hydroxamaates, Ribonucleoside diphosphate reductase Cite this paper: David I. The reasonable way of producing hydroxamic acid derivative is the reaction of hydroxylamine with acid chlorides or esters. 13 Hydroxamic acids are capable of inhibiting a variety of enzymes, including ureases, 14, 15 peroxidises 16, and matrix metalloproteinases. Hyper acetylation of histones increases the access of some transcription factors to nucleosomes thereby increasing RNA transcription. Histone deacetylase inhibitors HDI leads to hyper acetylation by blocking the function of histone deacetylase, therefore leaving the lysine amino acids acetylated from the histone acetyl transferase and ultimately increasing transcription.