Identification, functional expression and kinetic analysis of two primary amine oxidases from Rhodococcus opacus

Foster, Alexander, Barnes, Nicole, Speight, Robert, & Keane, Mark A. (2012) Identification, functional expression and kinetic analysis of two primary amine oxidases from Rhodococcus opacus. Journal of Molecular Catalysis B: Enzymatic, 74(1-2), pp. 73-82.

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Abstract

Two native copper-containing amine oxidases (EC 1.4.3.21) have been isolated from Rhodococcus opacus and reveal phenotypic plasticity and catalytic activity with respect to structurally diverse natural and synthetic amines. Altering the amine growth substrate has enabled tailored and targeted oxidase upreg-ulation, which with subsequent treatment by precipitation, ion exchange and gel filtration, achieved a 90–150 fold purification. MALDI-TOF mass spectrometric and genomic analysis has indicated multiple gene activation with complex biodegradation pathways and regulatory mechanisms. Additional post-purification characterisation has drawn on the use of carbonyl reagent and chelating agent inhibitors. Michaelis–Menten kinetics for common aliphatic and aromatic amine substrates and several structural analogues demonstrated a broad specificity and high affinity with Michaelis constants (K M) ranging from 0.1 to 0.9 mM for C 1 –C 5 aliphatic mono-amines and <0.2 mM for a range of aromatic amines. Potential exploitation of the enzymatic versatility of the two isolated oxidases in biosensing and bioprocessing is discussed.

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7 citations in Scopus
7 citations in Web of Science®
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ID Code: 70400
Item Type: Journal Article
Refereed: Yes
DOI: 10.1016/j.molcatb.2011.09.001
ISSN: 13811177
Divisions: Current > Schools > School of Chemistry, Physics & Mechanical Engineering
Current > QUT Faculties and Divisions > Science & Engineering Faculty
Copyright Owner: Wiley
Deposited On: 22 Apr 2014 05:04
Last Modified: 26 Jun 2014 03:29

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