2019
DOI: 10.1016/j.ibiod.2018.12.005
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Substrate specificities of aromatic ring-hydroxylating oxygenases of an uncultured gammaproteobacterium from chronically-polluted subantarctic sediments

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Cited by 13 publications
(5 citation statements)
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“…This suggests that whilst enzymes capable of the hydrolysis of PET, PETases, are generally present in relatively low abundances [ 19 ], the enzymes involved in the metabolisation of PET degradation sub-products may be more widely distributed in the marine environment. Whilst we tend to assign enzymes to very specific substrates, it is not new that some oxygenases may display a broader substrate specificity [ 65 ], especially those with larger catalytic pockets [ 66 ]. The enzymes identified in this study are, hence, excellent candidates for further substrate specificity evaluation.…”
Section: Discussionmentioning
confidence: 99%
“…This suggests that whilst enzymes capable of the hydrolysis of PET, PETases, are generally present in relatively low abundances [ 19 ], the enzymes involved in the metabolisation of PET degradation sub-products may be more widely distributed in the marine environment. Whilst we tend to assign enzymes to very specific substrates, it is not new that some oxygenases may display a broader substrate specificity [ 65 ], especially those with larger catalytic pockets [ 66 ]. The enzymes identified in this study are, hence, excellent candidates for further substrate specificity evaluation.…”
Section: Discussionmentioning
confidence: 99%
“…Additionally, Khara et al [48] showed that the αand β-subunit structures of Rieske oxygenase can affect the substrate specificity of the enzyme, and reported that the specificity relies on the properties of the catalytic subunit, specifically, the volume, size and shape. In addition, many factors influence enzymatic reactions, including the structure of the catalytic center, entry and exit channels of substrates, and the physicochemical properties of size, geometry and hydrophobicity of the ligands [49]. Furthermore, the unique loop structure linking the αand βsubunits in Rieske oxygenase plays a significant role in maintaining its structural stability and catalytic activity, and is important for NADPH binding and screening substrates [50].…”
Section: Discussionmentioning
confidence: 99%
“…This suggests that while enzymes capable of the hydrolysis of PET, PETases, are generally present in relatively low abundances [19], the enzymes involved in the metabolisation of PET degradation sub-products may be more widely distributed in the marine environment. While we tend to assign enzymes to very speci c substrates, it is not new that some oxygenases may display a broader substrate speci city [60], especially those with larger catalytic pockets [61]. The enzymes identi ed in this study are, hence, excellent candidates for further substrate speci city evaluation.…”
Section: Discussionmentioning
confidence: 90%