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Literature DB >> 962855

A steady-state kinetic study of the reaction catalysed by the secondary-amine mono-oxygenase of Pseudomonas aminovorans.

Abstract

1. Secondary-amine mono-oxygenase (proposed EC group 1.14.99.-) was partially purified from trimethylamine-grown Pseudomonas aminovorans by (NH4)2SO4 fractionation, gel filtration, hydrophobic chromatography on 5-aminopentylamino-Sepharose, and affinity chromatography on Sepharose-bound NADH. 2. Some problems in the affinity-chromatography step are discussed. 3. A steady-state kinetic analysis varying substrate, oxygen and electron-donor concentrations was performed, which, over the concentration range studied, gave a series of families of approximately parallel double-reciprocal plots. From secondary and tertiary plots, Michaelis constants of 0.160 mM, 0.086 mM and 0.121 mM were obtained for dimethylamine, NADPH and oxygen respectively. 4. Product-inhibition studies supported the postulated Hexa Uni Ping Pong (triple-transfer) reaction mechanism.

Entities: Chemical Species

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Year: 1976 PMID： 962855 PMCID： PMC1163831 DOI： 10.1042/bj1570197

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

18 in total

1. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.

Authors: W W CLELAND
Journal: Biochim Biophys Acta Date: 1963-01-08

2. Protein measurement with the Folin phenol reagent.

Authors: O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal: J Biol Chem Date: 1951-11 Impact factor: 5.157

3. Primary amines as uncouplers of electron transport from hydroxylation in the secondary-amine mono-oxygenase system of Pseudomonas aminovorans.

Authors: T R Jarman; P J Large
Journal: Biochem Biophys Res Commun Date: 1972-11-01 Impact factor: 3.575

8. Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein.

Authors: R R Eady; T R Jarman; P J Large
Journal: Biochem J Date: 1971-11 Impact factor: 3.857

9. Microbial oxidation of amines. Partial purification of a trimethylamine mono-oxygenase from Pseudomonas aminovorans and its role in growth on trimethylamine.

Authors: C A Boulton; M J Crabbe; P J Large
Journal: Biochem J Date: 1974-05 Impact factor: 3.857

10. Affinity chromatography of nicotinamide-adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide.

Authors: S Barry; P O'Carra
Journal: Biochem J Date: 1973-12 Impact factor: 3.857

2 in total

1. The dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila. Comparison with dye-linked methanol dehydrogenases.

Authors: C W Bamforth; J R Quayle
Journal: Biochem J Date: 1978-03-01 Impact factor: 3.857

2. Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source.

Authors: G W Haywood; P J Large
Journal: Biochem J Date: 1981-10-01 Impact factor: 3.857