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

2015 ◽  
Vol 17 (9) ◽  
pp. 500-505 ◽  
Author(s):  
Hao C. Nguyen ◽  
Min Wang ◽  
Andrew Salsburg ◽  
Bryan Knuckley
Keyword(s):  
Substrate Specificity ◽  
Screening Assay

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

2014 ◽  
Vol 463 ◽  
pp. 23-30 ◽  
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

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

Molecules ◽  
2018 ◽  
Vol 23 (1) ◽  
pp. 164 ◽  
Author(s):  
Tom Ewing ◽  
Aster van Noord ◽  
Caroline Paul ◽  
Willem van Berkel
Keyword(s):  
Substrate Specificity ◽  
Xylenol Orange ◽  
Screening Assay ◽  
Phenol Oxidases

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

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
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.

11-dehydro-thromboxane B2 enzyme immuno assay, a suitable screening assay for aspirin use?

2001 ◽  
Vol 120 (5) ◽  
pp. A596-A596
Author(s):  
M LEERDAM ◽  
F HUDIG ◽  
W ROOIJEN ◽  
E SLAATS ◽  
A GERAEDTS ◽  
...  
Keyword(s):  
Thromboxane B2 ◽  
Screening Assay ◽  
Immuno Assay ◽  
Enzyme Immuno Assay

Substrate Specificity of Leukocyte and Platelet Elastases

1978 ◽  
Vol 39 (03) ◽  
pp. 785-786 ◽  
Author(s):  
Y Legrand ◽  
J Caen ◽  
L Robert
Keyword(s):  
Substrate Specificity

PRKACA mutations in adrenal Cushing can alter substrate specificity

2017 ◽  
Author(s):  
Kerstin Bathon ◽  
Isabel Weigand ◽  
Jens T Vanselow ◽  
Cristina L Ronchi ◽  
Dalmazi Guido Di ◽  
...  
Keyword(s):  
Substrate Specificity

Human Neuraminidases Have Reduced Activity Towards Modified Sialic Acids on Glycoproteins

2020 ◽  
Author(s):  
Carmanah D. Hunter ◽  
Elizabeth Porter ◽  
Christopher Cairo
Keyword(s):  
Substrate Specificity ◽  
General Trend ◽  
Sialic Acids ◽  
Enzyme Specificity ◽  
Naturally Occurring ◽  
Bovine Submaxillary Mucin ◽  
Reduced Activity

This work investigated the substrate specificity of hNEU enzymes for a glycoprotein substrate (bovine submaxillary mucin) containing 9-<i>O</i>-acetylated and Neu5Gc residues. Using this model substrate, we observe a general trend for hNEU tolerance of Neu5Ac>Neu5Gc>>>Neu5,9Ac<sub>2</sub>, consistent with our previous results with glycolipid substrates. These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity.

Bioinformatics-Guided Discovery of Citrulline 4-Hydroxylase from GE81112 Biosynthesis and Rational Engineering of Its Substrate Specificity

2019 ◽  
Author(s):  
Christian Zwick ◽  
Max Sosa ◽  
Hans Renata
Keyword(s):  
Substrate Specificity ◽  
Guided Discovery ◽  
Rational Engineering

We functionally characterize a nonheme dioxygenase from GE81112 biosynthesis and identify it as a citrulline hydroxylase. A bioinformatics guided engineering was performed to alter the substrate specificity of the enzyme.

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