Part IV intermediate metabolismLipase-catalysed condensation of fatty acids with hydroxylamine
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Cited by (34)
Multienzymatic Synthesis of γ-Lactam Building Blocks from Unsaturated Esters and Hydroxylamine
2023, European Journal of Organic ChemistryGenome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family
2006, Journal of Biological ChemistryCitation Excerpt :Enzymatic Screens and Assays—General phosphatase screens with p-nitrophenyl phosphate (pNPP) as substrate and natural substrate phosphatase screens with 80 phosphorylated compounds from Sigma (supplemental Table 1) were performed as previously described (18). 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).
Biochemical characterization of the Pseudomonas putida 3-hydroxyacyl ACP:CoA transacylase, which diverts intermediates of fatty acid de novo biosynthesis
2002, Journal of Biological ChemistryCitation Excerpt :The purified (R,S)-3-hydroxydecanoyl-CoA was analyzed by HPLC, and its concentration was determined by hydroxylamine treatment, which causes a release of bound CoA. The concentration of free CoA before and after hydroxylamine treatment (17) was analyzed by the Ellman method (18). Since various enzymes involved in PHA biosynthesis are localized at the PHA-granule surface, we investigated the subcellular localization of PhaG inP.
Study of the acyl transfer activity of a recombinant amidase overproduced in an Escherichia coli strain. Application for short-chain hydroxamic acid and acid hydrazide synthesis
1998, Journal of Molecular Catalysis - B EnzymaticLarge-scale synthesis of coenzyme A esters
1997, Methods in EnzymologyA rapid method for the synthesis of methylmalonyl-coenzyme A and other CoA-esters
1993, Analytical Biochemistry
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I am happy for the opportunity to express with this contribution my gratitude and increasingly realized indebtedness to Professor Otto Meyerhof and his laboratory for what I imbibed there during my apprenticeship from 1927–1930.
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Present address: Department of Chemistry, University of Nebraska.