A Xylenol Orange-Based Screening Assay for the Substrate Specificity of Flavin-Dependent para-Phenol Oxidases

Tom Ewing; Aster van Noord; Caroline Paul; Willem van Berkel

doi:10.3390/molecules23010164

A Xylenol Orange-Based Screening Assay for the Substrate Specificity of Flavin-Dependent para-Phenol Oxidases

Molecules ◽

10.3390/molecules23010164 ◽

2018 ◽

Vol 23 (1) ◽

pp. 164 ◽

Cited By ~ 7

Author(s):

Tom Ewing ◽

Aster van Noord ◽

Caroline Paul ◽

Willem van Berkel

Keyword(s):

Substrate Specificity ◽

Xylenol Orange ◽

Screening Assay ◽

Phenol Oxidases

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Colorimetric method for enzymatic screening assay of ATP using Fe(III)-xylenol orange complex formation

Analytical and Bioanalytical Chemistry ◽

10.1007/s00216-008-2334-z ◽

2008 ◽

Vol 392 (5) ◽

pp. 987-994 ◽

Cited By ~ 11

Author(s):

Akihiko Ishida ◽

Yasuko Yamada ◽

Tamio Kamidate

Keyword(s):

Complex Formation ◽

Xylenol Orange ◽

Colorimetric Method ◽

Screening Assay

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Continuous colorimetric screening assay for detection of d-amino acid aminotransferase mutants displaying altered substrate specificity

Analytical Biochemistry ◽

10.1016/j.ab.2014.06.006 ◽

2014 ◽

Vol 463 ◽

pp. 23-30 ◽

Cited By ~ 11

Author(s):

Janet E.B. Barber ◽

Adam M. Damry ◽

Guido F. Calderini ◽

Curtis J.W. Walton ◽

Roberto A. Chica

Keyword(s):

Amino Acid ◽

Substrate Specificity ◽

Screening Assay

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Development of a Plate-Based Screening Assay to Investigate the Substrate Specificity of the PRMT Family of Enzymes

ACS Combinatorial Science ◽

10.1021/acscombsci.5b00070 ◽

2015 ◽

Vol 17 (9) ◽

pp. 500-505 ◽

Cited By ~ 7

Author(s):

Hao C. Nguyen ◽

Min Wang ◽

Andrew Salsburg ◽

Bryan Knuckley

Keyword(s):

Substrate Specificity ◽

Screening Assay

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Overview of Recent Advances in Immobilisation Techniques for Phenol Oxidases in Solution

Catalysts ◽

10.3390/catal10050467 ◽

2020 ◽

Vol 10 (5) ◽

pp. 467

Author(s):

Thandanani Ndlovu ◽

Sidy Ba ◽

Soraya P Malinga

Keyword(s):

Substrate Specificity ◽

Large Scale ◽

Future Directions ◽

Enzyme Immobilisation ◽

Broad Substrate Specificity ◽

Structural Modifications ◽

Advantages And Disadvantages ◽

Phenol Oxidases ◽

The Past ◽

Bioremediation Processes

Over the past two decades, phenol oxidases, particularly laccases and tyrosinases, have been extensively used for the removal of numerous pollutants in wastewaters due to their broad substrate specificity and their ability to use readily accessible molecular oxygen as the essential cofactor. As for other enzymes, immobilisation of laccases and tyrosinases has been shown to improve the performance and efficiency of the biocatalysts in solution. Several reviews have addressed the enzyme immobilisation techniques and the application of phenol oxidases to decontaminate wastewaters. This paper offers an overview of the recent publications, mainly from 2012 onwards, on the various immobilisation techniques applied to laccases and tyrosinases to induce and/or increase the performance of the biocatalysts. In this paper, the emphasis is on the efficiencies achieved, in terms of structural modifications, stability and resistance to extreme conditions (pH, temperature, inhibitors, etc.), reactivity, reusability, and broad substrate specificity, particularly for application in bioremediation processes. The advantages and disadvantages of several enzyme immobilisation techniques are also discussed. The relevance and effectiveness of the immobilisation techniques with respect to wastewater decontamination are critically assessed. A perspective on the future directions for large-scale application of the phenol oxidases in immobilised forms is provided.

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Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

Biochemical Society Symposium ◽

10.1042/bss0700039 ◽

2003 ◽

Vol 70 ◽

pp. 39-52 ◽

Cited By ~ 54

Author(s):

Roy A. Black ◽

John R. Doedens ◽

Rajeev Mahimkar ◽

Richard Johnson ◽

Lin Guo ◽

...

Keyword(s):

Substrate Specificity ◽

Recent Work ◽

Tumour Necrosis Factor ◽

Tumour Necrosis ◽

Transforming Growth Factor ◽

Intrinsic Activity ◽

Converting Enzyme ◽

Tumour Necrosis Factor Α ◽

Factor Α ◽

Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

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