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

Foster, Alexander; Barnes, Nicole; Speight, Robert; Keane, Mark A.

doi:10.1016/j.molcatb.2011.09.001

Cited by 8 publications

(12 citation statements)

References 60 publications

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“…This finding was then applied to the metabolic engineering of microbes for the production of ethanolamine from glucose (patent application PCT/EP2007/055762; Foti et al, ). Ethanolamine is a small primary amine that can be oxidized to glycolaldehyde by ethanolamine oxidase activity, which has been detected in several organisms (Foster et al, ; Kulkarni and Hodgson, ; Narrod and Jakoby, ; Ota et al, ). Furthermore, as demonstrated previously, glycolaldehyde can be easily converted to EG (Liu et al, ).…”

Section: Introductionmentioning

confidence: 99%

Engineering a novel biosynthetic pathway in Escherichia coli for production of renewable ethylene glycol

Pereira

Zhang

Mey

et al. 2015

Biotech & Bioengineering

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Ethylene glycol (EG) is an important commodity chemical with broad industrial applications. It is presently produced from petroleum or natural gas feedstocks in processes requiring consumption of significant quantities of non-renewable resources. Here, we report a novel pathway for biosynthesis of EG from the renewable sugar glucose in metabolically engineered Escherichia coli. Serine-to-EG conversion was first achieved through a pathway comprising serine decarboxylase, ethanolamine oxidase, and glycolaldehyde reductase. Serine provision in E. coli was then enhanced by overexpression of the serine-biosynthesis pathway. The integration of these two parts into the complete EG-biosynthesis pathway in E. coli allowed for production of 4.1 g/L EG at a cumulative yield of 0.14 g-EG/g-glucose, establishing a foundation for a promising biotechnology.

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Section: Introductionmentioning

confidence: 99%

Engineering a novel biosynthetic pathway in Escherichia coli for production of renewable ethylene glycol

Pereira

Zhang

Mey

et al. 2015

Biotech & Bioengineering

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“…As nitrogen is the major limiting substrate for growth in nature, the underlying cellular stimulus for many transformations is the requirement for nitrogen assimilation and mineralisation. Such evolutionary pressures have lead to a diverse array of enzymes frequently with plasticity to act on chemically related substrates and periodically prevalent energy sources and essential nutrients . Full exploitation of Rhodococcus in bioremediation and biotechnology therefore requires a fundamental understanding of these processes from both a genomic and enzymatic perspective, and an appreciation of their role within the organism as part of the nitrogen cycle and associated regulatory aspects (repression and induction).…”

Section: Background and Overviewmentioning

confidence: 99%

“…They are established carcinogens with recorded incidences of human cancer linked to the industrial production and handling of amines . It is recognised that bio‐conversion of amines has a critical role to play in environmental remediation, treatment of livestock waste, wine, fish and meat spoilage, enantioselective synthesis of fine chemicals and pathogenesis and diagnosis . While bacteria can utilise amines through the action of amine dehydrogenases or catabolic routes found in Pseudomonas and Paracoccus denitrificans , deamination in Rhodococcus is normally promoted by amine oxidases.…”

Section: Aminesmentioning

confidence: 99%

“…Genomic analysis has revealed the presence of at least eight putative amine oxidases within Rhodococcus RHA1 and Rhodococcus opacus B4 . In contrast, there are two putative genes in the pathogenic ( Rhodococcus equi ) and marine ( Rhodococcus erythropolis ) varieties of the species .…”

Section: Aminesmentioning

confidence: 99%

“…can be linked to substrate specificity, facilitating effective amine utilisation at low available nitrogen concentration . Recent work has established three copper dependant oxidases in Rhodococcus opacus DSM 43250, induced by pre‐treatment with aliphatic monoamines, diamines and primary aromatic amines as sole nitrogen source . van Hellemond and co‐workers identified a homologue (92% identities) of a FAD dependant putrescine oxidase isolated from Rhodococcus erythropolis .…”

Section: Aminesmentioning

confidence: 99%

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The repertoire of nitrogen assimilation in Rhodococcus: catalysis, pathways and relevance in biotechnology and bioremediation

Foster

Barnes

Speight

et al. 2014

J of Chemical Tech & Biotech

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The Rhodococcus genus exhibits diverse enzymatic activity that can be exploited in the conversion of natural and anthropogenic nitrogenous compounds. This catalytic response provides a selective advantage in terms of available nutrients while also serving to remove otherwise harmful xenobiotics. This review provides a critical assessment of the literature on bioconversion of organonitrogen compounds with a consideration of applications in bioremediation and commercial biotechnology. By examining the major nitro-organic compounds (amino acids, amines, nitriles, amides and nitroaromatics) in turn, the considerable repertoire of Rhodococcus spp. is established. The available published enzyme reaction data is coupled with genomic characterisation to provide a molecular basis for Rhodococcus enzyme activity with an assessment of the cellular properties that aid substrate accessibility and ensure stability. The metabolic gene clusters associated with the observed reaction pathways are identified and future directions in enzyme optimisation and metabolic engineering are assessed.Alanine dehydrogenase (RHA1_ro01495, ald1, ald2) and aspartate ammonia lyase (aspA1, aspA2, aspA3), with corresponding transaminases, provide alternative ping-pong (bi-bi) systems. Specificity and cellular catalytic efficiency is extended by a number of genes encoding asparagine dehydrogenase, arginine, cysteine, histidine and serine ammonia lyase ( Table 2). The production of

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Syncephalastrum racemosum amine oxidase with high catalytic efficiency toward ethanolamine and its application in ethanolamine determination

Hirano

Chonan

Murayama

et al. 2015

Appl Microbiol Biotechnol

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Our screening study yielded a copper amine oxidase (SrAOX) from Syncephalastrum racemosum, which showed much higher affinity and catalytic efficiency toward ethanolamine (EA) than any other amine oxidase (AOX). Following purification of the enzyme to electrophoretic homogeneity from a cell-free extract, the maximum activity toward EA was detected at pH 7.2-7.5 and 45 °C. The SrAOX complementary DNA (cDNA) was composed of a 2052-bp open reading frame encoding a 683-amino acid protein with a molecular mass of 77,162 Da. The enzyme functions as a homodimer. The deduced amino acid sequence of SrAOX showed 55.3 % identity to Rhizopus delemar AOX and contains two consensus sequences of Cu-AOX, NYDY, and HHQH, suggesting SrAOX is a type 1 Cu-AOX (i.e., a topaquinone enzyme). Structural homology modeling showed that residues (112)ML(113), (141)FADTWG(146) M158, and N318 are unique, and T144 possibly characterizes the substrate specificity of SrAOX. The recombinant enzyme (rSrAOX) was produced using Escherichia coli. Steady-state kinetic analysis of rSrAOX activity toward EA (pH 7.5 and 45 °C) gave K m and k cat values of 0.848 ± 0.009 mM and 9.11 ± 0.13 s(-1), respectively. The standard curves were linear between 0.1 and 2 mM EA, and 10 μg mL(-1)-2.5 mg mL(-1) (15 μM-3.6 mM) phosphatidylethanolamine using Streptomyces chromofuscus phospholipase D, respectively, was sufficiently sensitive for clinical use.

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

Cited by 8 publications

References 60 publications

Engineering a novel biosynthetic pathway in Escherichia coli for production of renewable ethylene glycol

Engineering a novel biosynthetic pathway in Escherichia coli for production of renewable ethylene glycol

The repertoire of nitrogen assimilation in Rhodococcus: catalysis, pathways and relevance in biotechnology and bioremediation

Syncephalastrum racemosum amine oxidase with high catalytic efficiency toward ethanolamine and its application in ethanolamine determination

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