Lipase-catalysed condensation of fatty acids with hydroxylamine

Lipmann, Fritz; Tuttle, Lauren

doi:10.1016/0006-3002(50)90036-9

Cited by 103 publications

(24 citation statements)

References 12 publications

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“…Le P-aspartyl-phosphate est dose par la methode de mise en evidence des acyl-phosphates par l'hydroxylamine [9], l'hydroxamate de l'acide aspartique servant de substance &talon.…”

Section: Gradients De Glyckrolunclassified

La semi-aldehyde aspartique deshydrogenase chez Saccharomyces cerevisiae: proprietes et regulation

Surdin

1967

Eur J Biochem

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The synthesis of threonine and methionine in X. cerevisiae proceeds as follows :aspartic acid + aspartyl-phosphate + aspartic-semi-aldehydeThe aspartic-semi-aldehyde dehydrogenase (ASA dehydrogenase) catalyzes the second reaction. It has been purified from an extract of baker's yeast and has been obtained with a specific activity 250 times higher than in crude extracts. Its main properties are : (a) The optimum pH is 8.5 in both directions; (b) Its activity is enhanced 4 or 5 times in both directions by addition of bicarbonate to the reaction mixture. Evidence is presented that the bicarbonate is necessary for the reaction to proceed; (c) Its molecular weight estimated by filtration on Sephadex G-200 is about 140,000; (d) No feed-back inhibition by threonine or methionine has been found. An inhibition by cysteine and homocysteine (Kt = 1 x M) was found in the reverse reaction.The synthesis of ASA dehydrogenase is regulated by threonine intracellular concentration ; (e) By heating at 60" a t different pH's it is shown that ASA dehydrogenase exists in two forms. Two mechanisms are proposed: a depolymerisation, or a release of proton. As in the case of the ~-glyceraldehyde-3-phosphate dehydrogenase, the reaction catalyzed by ASA dehydrogenase can be separated into two parts : the oxidation and the phosphorylation. This mechanism is under investigation. Abrbviations non usudles. Semi-aldbhyde aspartique,

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“…Le P-aspartyl-phosphate est dose par la methode de mise en evidence des acyl-phosphates par l'hydroxylamine [9], l'hydroxamate de l'acide aspartique servant de substance &talon.…”

Section: Gradients De Glyckrolunclassified

La semi-aldehyde aspartique deshydrogenase chez Saccharomyces cerevisiae: proprietes et regulation

Surdin

1967

Eur J Biochem

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“…Acetyl-phosphatase activity was assayed by measuring the acetyl-phosphate concentration using the hydroxylamine protocol of Lipmann and Tuttle (19). The production of fructose in enzymatic reactions was determined using an enzyme-coupled assay with fructose dehydrogenase (F5152; Sigma), essentially as previously described (20).…”

Section: Methodsmentioning

confidence: 99%

Genome-wide Analysis of Substrate Specificities of the Escherichia coli Haloacid Dehalogenase-like Phosphatase Family

Kuznetsova

Proudfoot

González

et al. 2006

Journal of Biological Chemistry

262

323

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Most enzymes form families of paralogs whose members are related by sequence and catalyze similar reactions but have evolved specific biological functions. Comprehensive determination of the substrate specificities and selectivities of all metabolic enzymes in an organism is an essential step toward understanding the relationship between the proteome and the metabolome. By the most recent estimate, Escherichia coli possesses at least 1186 metabolic enzymes and 1005 metabolites (1). The most common functional group in the metabolome is phosphate; 35-40% of the metabolites contain a phosphate group (2). The pool of phosphorylated metabolites is controlled by the activity of diverse kinases and phosphatases, of which there are hundreds in the E. coli genome.

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“…45 105 One of the first reports on the enzymatic synthesis of hydroxamic acids from a sodium acyl salt and hydroxylamine was reported by Lipmann and Tuttle in 1950. 46 With the use of a hog liver esterase and the pancreas lipase Pancreatine Parke-Davis, the authors reported on the formation of hydroxamic acids in yields 110 typically around 10% after 60 minutes incubation time at 37 ºC at neutral pH. It was found that the two enzymes functioned optimally with carbon chains of different lengths; the hog liver esterase worked best with sodium octanoate, whereas the longer chain of sodium dodecanoate suited the pancrease lipase better.…”

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confidence: 99%

Catalytic amide formation from non-activated carboxylic acids and amines

et al. 2014

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The amide functionality is found in a wide variety of biological and synthetic structures such as proteins, polymers, pesticides and pharmaceuticals. Due to the fact that synthetic amides are still mainly produced by the aid of coupling reagents with poor atom-economy, the direct catalytic formation of amides from carboxylic acids and amines has become a field of emerging importance. A general, efficient and selective catalytic method for this transformation would meet well with the increasing criterias for green 10 chemistry. This review covers catalytic and synthetically relevant methods for direct condensation of carboxylic acids and amines. A comprehensive overview of homogeneous and heterogeneous catalytic methods is presented, covering biocatalysis, Lewis acid catalysts based on boron and metals as well an assortment of other types of catalysts.

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Lipase-catalysed condensation of fatty acids with hydroxylamine

Cited by 103 publications

References 12 publications

La semi-aldehyde aspartique deshydrogenase chez Saccharomyces cerevisiae: proprietes et regulation

La semi-aldehyde aspartique deshydrogenase chez Saccharomyces cerevisiae: proprietes et regulation

Genome-wide Analysis of Substrate Specificities of the Escherichia coli Haloacid Dehalogenase-like Phosphatase Family

Catalytic amide formation from non-activated carboxylic acids and amines

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