scholarly journals Characterization of Two Hydrogen Peroxide Resistant Peroxidases from Rhodococcus opacus 1CP

2021 ◽  
Vol 11 (17) ◽  
pp. 7941
Author(s):  
Anna Christina R. Ngo ◽  
Catleen Conrad ◽  
Álvaro Gómez Baraibar ◽  
Anke Matura ◽  
Karl-Heinz van Pée ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Organic Synthesis ◽  
Broad Spectrum ◽  
Rhodococcus Opacus ◽  
High Tolerance ◽  
Abts Assay ◽  
Natural Function ◽  
Rhodococcus Opacus 1Cp

The dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such as azo dyes or anthraquinones make them excellent candidates for applications in bioremediation and organic synthesis. In this work, two novel DyP peroxidases from the organism Rhodococcus opacus 1CP (DypA and DypB) were cloned and expressed in Escherichia coli. The enzymes were purified and biochemically characterized. The activities of the two DyPs via 2,2′-azino-bis [3-ethylbenzthiazoline-6-sulphonic acid] (ABTS) assay and against Reactive Blue 5 were assessed and optimized. Results showed varying trends for DypA and DypB. Remarkably, these enzymes presented a particularly high tolerance towards H2O2, retaining its activities at about 10 mM H2O2 for DypA and about 4.9 mM H2O2 for DypB.

Characterization of the Maleylacetate Reductase MacA of Rhodococcus opacus 1CP and Evidence for the Presence of an Isofunctional Enzyme

1998 ◽  
Vol 180 (14) ◽  
pp. 3503-3508 ◽  
Author(s):  
Volker Seibert ◽  
Elena M. Kourbatova ◽  
Ludmila A. Golovleva ◽  
Michael Schlömann
Keyword(s):  
Aromatic Compounds ◽  
Gene Clusters ◽  
Reductive Dehalogenation ◽  
Rhodococcus Opacus ◽  
Reductase Gene ◽  
Rhodococcus Opacus 1Cp ◽  
Dienelactone Hydrolase ◽  
Maleylacetate Reductase ◽  
Intradiol Dioxygenase

ABSTRACT Maleylacetate reductases (EC 1.3.1.32 ) have been shown to contribute not only to the bacterial catabolism of some usual aromatic compounds like quinol or resorcinol but also to the degradation of aromatic compounds carrying unusual substituents, such as halogen atoms or nitro groups. Genes coding for maleylacetate reductases so far have been analyzed mainly in chloroaromatic compound-utilizing proteobacteria, in which they were found to belong to specialized gene clusters for the turnover of chlorocatechols or 5-chlorohydroxyquinol. We have now cloned the gene macA, which codes for one of apparently (at least) two maleylacetate reductases in the gram-positive, chlorophenol-degrading strain Rhodococcus opacus 1CP. Sequencing of macA showed the gene product to be relatively distantly related to its proteobacterial counterparts (ca. 42 to 44% identical positions). Nevertheless, like the known enzymes from proteobacteria, the cloned Rhodococcusmaleylacetate reductase was able to convert 2-chloromaleylacetate, an intermediate in the degradation of dichloroaromatic compounds, relatively fast and with reductive dehalogenation to maleylacetate. Among the genes ca. 3 kb up- and downstream of macA, none was found to code for an intradiol dioxygenase, a cycloisomerase, or a dienelactone hydrolase. Instead, the only gene which is likely to be cotranscribed with macA encodes a protein of the short-chain dehydrogenase/reductase family. Thus, the R. opacus maleylacetate reductase genemacA clearly is not part of a specialized chlorocatechol gene cluster.

CHARACTERIZATION OF KLEBSIELLA PNEUMONIAE AND ESCHERICHIA COLI STRAINS THAT PRODUCE CTX-M-2-TYPE BROAD SPECTRUM BETA-LACTAMASE ISOLATED FROM A CHILD WITH LEUKEMIA

2002 ◽  
Vol 21 (3) ◽  
pp. 260-262 ◽  
Author(s):  
Toshiya Ohkawa ◽  
Masao Yoshinaga ◽  
Naoaki Ikarimoto ◽  
Hiroaki Miyanohara ◽  
Koichiro Miyata ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Klebsiella Pneumoniae ◽  
Broad Spectrum ◽  
Beta Lactamase

Identification and characterization of novel broad-spectrum amino acid racemases from Escherichia coli and Bacillus subtilis

Amino Acids ◽  
2017 ◽  
Vol 49 (11) ◽  
pp. 1885-1894 ◽  
Author(s):  
Tetsuya Miyamoto ◽  
Masumi Katane ◽  
Yasuaki Saitoh ◽  
Masae Sekine ◽  
Hiroshi Homma
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Broad Spectrum ◽  
Identification And Characterization

scholarly journals Biochemical Characterization of CPS-1, a Subclass B3 Metallo-β-Lactamase from a Chryseobacterium piscium Soil Isolate

2015 ◽  
Vol 60 (3) ◽  
pp. 1869-1873 ◽  
Author(s):  
Dereje Dadi Gudeta ◽  
Simona Pollini ◽  
Jean-Denis Docquier ◽  
Valeria Bortolaia ◽  
Gian Maria Rossolini ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Broad Spectrum ◽  
Biochemical Characterization ◽  
Amino Acid Identity ◽  
Content Type ◽  
Acid Identity ◽  
Soil Isolate

CPS-1 is a subclass B3 metallo-β-lactamase from aChryseobacteriumpisciumisolate collected from soil, showing 68% amino acid identity to the GOB-1 enzyme. CPS-1 was overproduced inEscherichia coliRosetta (DE3), purified by chromatography, and biochemically characterized. This enzyme exhibits a broad-spectrum substrate profile, including penicillins, cephalosporins, and carbapenems, which overall resembles those of L1, GOB-1, and acquired subclass B3 enzymes AIM-1 and SMB-1.

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