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

Foster, Alexander, Barnes, Nicole, Speight, Robert and 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: 73-82. doi:10.1016/j.molcatb.2011.09.001


Author Foster, Alexander
Barnes, Nicole
Speight, Robert
Keane, Mark A.
Title Identification, functional expression and kinetic analysis of two primary amine oxidases from Rhodococcus opacus
Journal name Journal of Molecular Catalysis B-Enzymatic   Check publisher's open access policy
ISSN 1381-1177
1873-3158
Publication date 2012-01
Year available 2012
Sub-type Article (original research)
DOI 10.1016/j.molcatb.2011.09.001
Volume 74
Issue 1-2
Start page 73
End page 82
Total pages 10
Place of publication Amsterdam, The Netherlands
Publisher Elsevier
Collection year 2013
Language eng
Formatted 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 upregulation, 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.
Keyword Amine oxidase
Rhodococcus opacus
Oxidase induction
Enzyme purification
Oxidative deamination kinetics
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Australian Institute for Bioengineering and Nanotechnology Publications
 
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Created: Thu, 12 Sep 2013, 09:34:30 EST by Cathy Fouhy on behalf of Aust Institute for Bioengineering & Nanotechnology