Acyltransferase Activity of the Wide Spectrum Amidase of Brevibacterium sp. R312

Abstract

The wide spectrum amidase from Brevibacterium sp. R3 12, which can hydrolyse many amides to the corresponding acids, was shown to transfer the acyl groups of amides, acids and esters to hydroxylamine. The transfer rates of these reactions in cytoplasmic fractions were measured and compared. The K , and V,,, were determined for different substrates in the presence of hydroxylamine. The enzyme was also shown to transfer the acyl group of the amide analogue Nmethylacetamide to hydroxylamide and that of acetamide to the hydroxylamine analogue methyl hydrox ylamine.

Lipase and esterase-catalyzed acylation of hetero-substituted nitrogen nucleophiles in water and organic solvents

“…We note that the amidase-catalyzed hydroxylaminolysis of carboxylic amides has been known for a long time (Clarke, 1972;Jacobi and Fredericks, 1964); its kinetics have also been reported (Fournand et al, 1998a,b;Thiéry et al, 1986). The lipase-mediated synthesis of acyl hydrazides has briefly been described (Astorga et al, 1991(Astorga et al, , 1993Gotor et al, 1990); the reaction is also catalyzed by amidases (Fournand et al, 1998a;Kobayashi et al, 1999).…”

Synthesis and Characterization of Fatty Hydroxamic Acids from Triacylglycerides

“…Other uses include, synthesized a series of alkyloxybenzoyl hydroxamic acids and fatty acyl hydroxamic acids and found that some of these chemicals possessed antifungal activity [7][8][9] . Several studies were carried out for synthesis of hydroxamic acids from acids and esters with hydroxyl amine [10][11][12][13] . Servat et al (1990) reported that the synthesis of alkanohydroxamic acids (N-acyl hydroxylamines) by Rhizomucor miehei lipase -catalyzed hydroxylaminolysis of fatty acids and soybean methyl ester 14) .…”

Biotransformation of Acetamide to Acetohydroxamic Acid at Bench Scale Using Acyl Transferase Activity of Amidase of Geobacillus pallidus BTP-5x MTCC 9225

“…Like other purified and immobilized amidases, G. pallidus BTP-5x MTCC 9225 exhibit maximum acyl transferase activity at neutral pH [11][12][13][14][15][16]. The immobilized purified amidase of Rhodococcus sp.…”

“…R312 [6]. Optimum temperatures for acyl transferase activity in Rhodococcus erythropolis MP50 [14] and G. pallidus RAPc8 [17] were 30 and 50°C respectively. Maximum acetohydroxamic acid accumulation was reported with 1:2 ratios of acetamide and hydroxylamine and only 55-60% of conversion was reported [6].…”