Crystallization and preliminary X-ray analysis of a bacterial<scp>L</scp>-amino-acid oxidase from<i>Rhodococcus opacus</i>

Faust, Annette; Geueke, Birgit; Niefind, Karsten; Hummel, Werner; Schomburg, Dietmar

doi:10.1107/s1744309106005689

Cited by 5 publications

(3 citation statements)

References 28 publications

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“…36,61 Crystals were grown from solutions containing 100 mm Hepes (pH 7.8), 10% (v/v) 2-propanole and 10% (w/w) PEG 4000. All chemicals were obtained from Aldrich or Sigma.…”

Section: Methodsmentioning

confidence: 99%

The Structure of a Bacterial l-Amino Acid Oxidase from Rhodococcus opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation

Faust

Niefind

Hummel

et al. 2007

Journal of Molecular Biology

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“…36,61 Crystals were grown from solutions containing 100 mm Hepes (pH 7.8), 10% (v/v) 2-propanole and 10% (w/w) PEG 4000. All chemicals were obtained from Aldrich or Sigma.…”

Section: Methodsmentioning

confidence: 99%

The Structure of a Bacterial l-Amino Acid Oxidase from Rhodococcus opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation

Faust

Niefind

Hummel

et al. 2007

Journal of Molecular Biology

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“…The best characterized bacterial LAO is that expressed by Rhodococcus opacus which shows abroad substrate specificity. This enzyme has been expressed heterologously and its dimeric structure has been described [ 105 , 106 ]. LAOs are continuously being detected from diverse bacterial genera and different physiological functions have been proposed for them.…”

Section: L -Amino Acid Oxidasesmentioning

confidence: 99%

Finding New Enzymes from Bacterial Physiology: A Successful Approach Illustrated by the Detection of Novel Oxidases in Marinomonas mediterranea

2010

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The identification and study of marine microorganisms with unique physiological traits can be a very powerful tool discovering novel enzymes of possible biotechnological interest. This approach can complement the enormous amount of data concerning gene diversity in marine environments offered by metagenomic analysis, and can help to place the activities associated with those sequences in the context of microbial cellular metabolism and physiology. Accordingly, the detection and isolation of microorganisms that may be a good source of enzymes is of great importance. Marinomonas mediterranea, for example, has proven to be one such useful microorganism. This Gram-negative marine bacterium was first selected because of the unusually high amounts of melanins synthesized in media containing the amino acid l-tyrosine. The study of its molecular biology has allowed the cloning of several genes encoding oxidases of biotechnological interest, particularly in white and red biotechnology. Characterization of the operon encoding the tyrosinase responsible for melanin synthesis revealed that a second gene in that operon encodes a protein, PpoB2, which is involved in copper transfer to tyrosinase. This finding made PpoB2 the first protein in the COG5486 group to which a physiological role has been assigned. Another enzyme of interest described in M. mediterranea is a multicopper oxidase encoding a membrane-associated enzyme that shows oxidative activity on a wide range of substrates typical of both laccases and tyrosinases. Finally, an enzyme very specific for l-lysine, which oxidises this amino acid in epsilon position and that has received a new EC number (1.4.3.20), has also been described for M. mediterranea. Overall, the studies carried out on this bacterium illustrate the power of exploring the physiology of selected microorganisms to discover novel enzymes of biotechnological relevance.

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“…For example, it has been proposed that the alpha-keto acids generated after the deamination of amino acids can act as siderophores in some bacterial groups (10). By analogy with the physiological role of LAOs in eukaryotic microorganisms, it has been proposed that bacterial LAOs might also be involved in nitrogen and/or amino acid metabolism, although definitive evidence is lacking (13). Finally, it was recently described that an LAO is used by the lactic acid bacterium Streptococcus oligofermentans to generate hydrogen peroxide, which is involved in the process of microbial competition with the cariogenic Streptococcus mutans (42).…”

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confidence: 99%

Regulation of the Marinomonas mediterranea Antimicrobial Protein Lysine Oxidase by l -Lysine and the Sensor Histidine Kinase PpoS

Molina-Quintero

Lucas-Elı́o

Sánchez-Amat

2010

Appl Environ Microbiol

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Some Gram-negative bacteria express a novel enzyme with lysine--oxidase (LOD) activity (EC 1.4.3.20). The oxidation of L-Lys generates, among other products, hydrogen peroxide, which confers antimicrobial properties to this kind of enzyme and has been shown to be involved in cell death during biofilm development and differentiation. In addition to LOD, the melanogenic marine bacterium Marinomonas mediterranea, which forms part of the microbiota of the marine plant Posidonia oceanica, expresses two other oxidases of biotechnological interest, a multicopper oxidase, PpoA, with laccase activity and a tyrosinase named PpoB, which is responsible for melanin synthesis. By using both lacZ fusions with the lodAB promoter and quantitative reverse transcription-PCR (qRT-PCR), this study shows that the hybrid sensor histidine kinase PpoS regulates LOD activity at the transcriptional level. Although PpoS also regulates PpoA and PpoB, in this case, the regulatory effect cannot be attributed only to a transcriptional regulation. Further studies indicate that LOD activity is induced at the posttranscriptional level by L-Lys as well as by two structurally similar compounds, L-Arg and meso-2,6-diaminopimelic acid (DAP), neither of which is a substrate of the enzyme. The inducing effect of these compounds is specific for LOD activity since PpoA and PpoB are not affected by them. This study offers, for the first time, insights into the mechanisms regulating the synthesis of the antimicrobial protein lysine--oxidase in M. mediterranea, which could be important in the microbial colonization of the seagrass P. oceanica.

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Crystallization and preliminary X-ray analysis of a bacterialL-amino-acid oxidase fromRhodococcus opacus

Cited by 5 publications

References 28 publications

The Structure of a Bacterial l-Amino Acid Oxidase from Rhodococcus opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation

The Structure of a Bacterial l-Amino Acid Oxidase from Rhodococcus opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation

Finding New Enzymes from Bacterial Physiology: A Successful Approach Illustrated by the Detection of Novel Oxidases in Marinomonas mediterranea

Regulation of the Marinomonas mediterranea Antimicrobial Protein Lysine Oxidase by l -Lysine and the Sensor Histidine Kinase PpoS

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