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12-Aminododecanoic Acid

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Colin Scott – One of the best experts on this subject based on the ideXlab platform.

  • Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.
    Acta crystallographica. Section F Structural biology communications, 2017
    Co-Authors: Matthew Wilding, Colin Scott, Janet Newman, Thomas S. Peat

    Abstract:

    The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-Aminododecanoic Acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.

  • Summary
    , 2016
    Co-Authors: Pseudomonas Strain, Matthew Wilding, Ellen F. A. Walsh, Susan J, Colin Scott

    Abstract:

    A Pseudomonas species [Pseudomonas sp. strain amino alkanoate catabolism (AAC)] was identified that has the capacity to use 12-Aminododecanoic Acid, the constituent building block of homo-nylon-12, as a sole nitrogen source. Growth of Pseudomonas sp. strain AAC could also be sup-ported using a range of additional ω-amino alkanoates. This metabolic function was shown to be most probably dependent upon one or more transaminases (TAs). Fourteen genes encoding putative TAs were identified from the genome of Pseudomonas sp. AAC. Each of the 14 genes was cloned, 11 of which were successfully expressed in Escherichia coli and tested for activity against 12-Aminododecanoic Acid. In addition, physiological functions were proposed for 9 of the 14 TAs. Of the 14 proteins, activity was demonstrated in 9, and of note, 3 TAs were shown to be able to catalyse the transfer of the ω-amine from 12-Aminododecanoic Acid to pyruvate. Based on this study, three enzymes have been identified that are promising biocatalysts for the production of nylon and related polymers

  • A β-Alanine Catabolism Pathway Containing a Highly Promiscuous ω-Transaminase in the 12-Aminododecanate-Degrading Pseudomonas Sp. Strain AAC
    Applied and environmental microbiology, 2016
    Co-Authors: Matthew Wilding, Thomas S. Peat, Janet Newman, Colin Scott

    Abstract:

    We previously isolated the transaminase {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458 from Pseudomonas sp. strain AAC as a promising biocatalyst for the production of 12-Aminododecanoic Acid, a constituent building block of nylon-12. Here, we report the subsequent characterization of this transaminase. It exhibits activity with a broad substrate range which includes α-, β-, and ω-amino Acids, as well as α,ω-diamines and a number of other industrially relevant compounds. It is therefore a prospective candidate for the biosynthesis of a range of polyamide monomers. The crystal structure of {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458 revealed that the protein forms a dimer containing a large active site pocket and unusual phosphorylated histidine residues. To infer the physiological role of the transaminase, we expressed, purified, and characterized a dehydrogenase from the same operon, {“type”:”entrez-protein”,”attrs”:{“text”:”KES23460″,”term_id”:”664810530″,”term_text”:”KES23460″}}KES23460. Unlike the transaminase, the dehydrogenase was shown to be quite selective, catalyzing the oxidation of malonic Acid semialdehyde, formed from β-alanine transamination via {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458. In keeping with previous reports, the dehydrogenase was shown to catalyze both a coenzyme A (CoA)-dependent reaction to form acetyl-CoA and a significantly slower CoA-independent reaction to form acetate. These findings support the original functional assignment of {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458 as a β-alanine transaminase. However, a seemingly well-adapted active site and promiscuity toward unnatural compounds, such as 12-Aminododecanoic Acid, suggest that this enzyme could perform multiple functions for Pseudomonas sp. strain AAC.

    IMPORTANCE We describe the characterization of an industrially relevant transaminase able to metabolize 12-Aminododecanoic Acid, a constituent building block of the widely used polymer nylon-12, and we report the biochemical and structural characterization of the transaminase protein. A physiological role for this highly promiscuous enzyme is proposed based on the characterization of a related gene from the host organism. Molecular dynamics simulations were carried out to compare the conformational changes in the transaminase protein to better understand the determinants of specificity in the protein. This study makes a substantial contribution that is of interest to the broad biotechnology and enzymology communities, providing insights into the catalytic activity of an industrially relevant biocatalyst as well as the biological function of this operon.

Sasha Omanovic – One of the best experts on this subject based on the ideXlab platform.

  • the effect of electrolyte flow on the performance of 12 aminododecanoic Acid as a carbon steel corrosion inhibitor in co2 saturated hydrochloric Acid
    Corrosion Science, 2011
    Co-Authors: Saad Ghareba, Sasha Omanovic

    Abstract:

    Abstract The effect of flow and flow pattern of CO 2 -saturated HCl on the corrosion inhibition of carbon steel (CS) by 12-Aminododecanoic Acid (AA) was investigated in a square duct, rotating disk electrode (RDE), and jet impingement cell configuration. 3 mM AA provided high corrosion inhibition efficiency in the square duct and RDE configuration. However, in 1 mM AA the inhibition efficiency decreased with an increase in Re , due to desorption of AA from the CS surface. AA was found to poorly protect CS in the impingement-jet configuration at low Re , while at high Re , acceleration of CS corrosion was recorded.

  • 12 aminododecanoic Acid as a corrosion inhibitor for carbon steel
    Electrochimica Acta, 2011
    Co-Authors: Saad Ghareba, Sasha Omanovic

    Abstract:

    Abstract The inhibiting effect of 12-Aminododecanoic Acid (AA) on corrosion of carbon steel (CS) was investigated in hydrochloric Acid of different pH, temperatures and over a prolonged period of time, and also in some other selected corrosive solutions. It was found that AA inhibits both partial corrosion reactions, with a slightly stronger inhibition of the anodic corrosion reaction. The corrosion protection mechanism is by formation of a surface-adsorbed AA monolayer that offers a hydrophobic barrier to transport of solvated corrosive ions to the surface. A maximum inhibition efficiency of 98.8 ± 0.5% was achieved in 0.5 M HCl. The adsorption of AA onto the CS surface was described by the Langmuir adsorption isotherm. The corresponding standard Gibbs energy of adsorption was calculated to be −26 kJ mol −1 . Polarization modulation infrared reflection absorption spectroscopy measurements revealed that the adsorbed AA monolayer is amorphous, which is due to the high heterogeneity of the CS surface.

  • interaction of 12 aminododecanoic Acid with a carbon steel surface towards the development of green corrosion inhibitors
    Corrosion Science, 2010
    Co-Authors: Saad Ghareba, Sasha Omanovic

    Abstract:

    Abstract The inhibiting effect of 12-Aminododecanoic Acid (AA) on corrosion of carbon steel (CS) in CO2-saturated hydrochloric Acid was investigated. It was found that AA acts as a mixed-type inhibitor, yielding a maximum inhibition efficiency of 98.1 ± 0.1%. The mechanism of its corrosion inhibition is by formation of a self-assembled monolayer (SAM), which presents a tight hydrophobic barrier imposed by the (–CH2)11 chain. In-situ PM-IRRAS measurements revealed that the SAM is amorphous. The SAM formation process was found to be spontaneous and reversible. The corresponding standard Gibbs energy of AA adsorption on CS was calculated to be −28 kJ mol−1.

Matthew Wilding – One of the best experts on this subject based on the ideXlab platform.

  • Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.
    Acta crystallographica. Section F Structural biology communications, 2017
    Co-Authors: Matthew Wilding, Colin Scott, Janet Newman, Thomas S. Peat

    Abstract:

    The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-Aminododecanoic Acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.

  • Summary
    , 2016
    Co-Authors: Pseudomonas Strain, Matthew Wilding, Ellen F. A. Walsh, Susan J, Colin Scott

    Abstract:

    A Pseudomonas species [Pseudomonas sp. strain amino alkanoate catabolism (AAC)] was identified that has the capacity to use 12-Aminododecanoic Acid, the constituent building block of homo-nylon-12, as a sole nitrogen source. Growth of Pseudomonas sp. strain AAC could also be sup-ported using a range of additional ω-amino alkanoates. This metabolic function was shown to be most probably dependent upon one or more transaminases (TAs). Fourteen genes encoding putative TAs were identified from the genome of Pseudomonas sp. AAC. Each of the 14 genes was cloned, 11 of which were successfully expressed in Escherichia coli and tested for activity against 12-Aminododecanoic Acid. In addition, physiological functions were proposed for 9 of the 14 TAs. Of the 14 proteins, activity was demonstrated in 9, and of note, 3 TAs were shown to be able to catalyse the transfer of the ω-amine from 12-Aminododecanoic Acid to pyruvate. Based on this study, three enzymes have been identified that are promising biocatalysts for the production of nylon and related polymers

  • A β-Alanine Catabolism Pathway Containing a Highly Promiscuous ω-Transaminase in the 12-Aminododecanate-Degrading Pseudomonas Sp. Strain AAC
    Applied and environmental microbiology, 2016
    Co-Authors: Matthew Wilding, Thomas S. Peat, Janet Newman, Colin Scott

    Abstract:

    We previously isolated the transaminase {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458 from Pseudomonas sp. strain AAC as a promising biocatalyst for the production of 12-Aminododecanoic Acid, a constituent building block of nylon-12. Here, we report the subsequent characterization of this transaminase. It exhibits activity with a broad substrate range which includes α-, β-, and ω-amino Acids, as well as α,ω-diamines and a number of other industrially relevant compounds. It is therefore a prospective candidate for the biosynthesis of a range of polyamide monomers. The crystal structure of {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458 revealed that the protein forms a dimer containing a large active site pocket and unusual phosphorylated histidine residues. To infer the physiological role of the transaminase, we expressed, purified, and characterized a dehydrogenase from the same operon, {“type”:”entrez-protein”,”attrs”:{“text”:”KES23460″,”term_id”:”664810530″,”term_text”:”KES23460″}}KES23460. Unlike the transaminase, the dehydrogenase was shown to be quite selective, catalyzing the oxidation of malonic Acid semialdehyde, formed from β-alanine transamination via {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458. In keeping with previous reports, the dehydrogenase was shown to catalyze both a coenzyme A (CoA)-dependent reaction to form acetyl-CoA and a significantly slower CoA-independent reaction to form acetate. These findings support the original functional assignment of {“type”:”entrez-protein”,”attrs”:{“text”:”KES23458″,”term_id”:”664810528″,”term_text”:”KES23458″}}KES23458 as a β-alanine transaminase. However, a seemingly well-adapted active site and promiscuity toward unnatural compounds, such as 12-Aminododecanoic Acid, suggest that this enzyme could perform multiple functions for Pseudomonas sp. strain AAC.

    IMPORTANCE We describe the characterization of an industrially relevant transaminase able to metabolize 12-Aminododecanoic Acid, a constituent building block of the widely used polymer nylon-12, and we report the biochemical and structural characterization of the transaminase protein. A physiological role for this highly promiscuous enzyme is proposed based on the characterization of a related gene from the host organism. Molecular dynamics simulations were carried out to compare the conformational changes in the transaminase protein to better understand the determinants of specificity in the protein. This study makes a substantial contribution that is of interest to the broad biotechnology and enzymology communities, providing insights into the catalytic activity of an industrially relevant biocatalyst as well as the biological function of this operon.