scholarly journals Comparative Studies on Retroviral Proteases: Substrate Specificity

Viruses ◽  
2010 ◽  
Vol 2 (1) ◽  
pp. 147-165 ◽  
Author(s):  
József Tözsér
Keyword(s):  
Substrate Specificity ◽  
Comparative Studies ◽  
Retroviral Proteases

scholarly journals Comparative studies on O-acetylhomoserine sulfhydrylase: physiological role and characterization of the Aspergillus nidulans enzyme.

1993 ◽  
Vol 40 (3) ◽  
pp. 421-428 ◽  
Author(s):  
J Brzywczy ◽  
S Yamagata ◽  
A Paszewski
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Substrate Specificity ◽  
Aspergillus Nidulans ◽  
Comparative Studies ◽  
Alternative Pathway ◽  
Physiological Role ◽  
Oligomeric Protein ◽  
Cysteine Synthesis ◽  
Sulfhydryl Compounds

O-acetylhomoserine sulfhydrylase (OAH SHLase) from Aspergillus nidulans is an oligomeric protein with a broad substrate specificity with regard to sulfhydryl compounds. As its Saccharomyces cerevisiae counterpart the enzyme also reacts with O-acetylserine and is inhibited by carbonyl reagents but not by antiserum raised against the yeast enzyme. In contrast to Saccharomyces cerevisiae the enzyme is not essential for Aspergillus nidulans as indicated by the completely prototrophic phenotype of OAH SHLase-negative mutants. Its major physiological role in Aspergillus nidulans seems to be recycling of the thiomethyl group of methylthio-adenosine but it is also a constituent of the alternative pathway of cysteine synthesis.

scholarly journals Comparative Studies on the Substrate Specificity of Avian Myeloblastosis Virus Proteinase and Lentiviral Proteinases

1996 ◽  
Vol 271 (12) ◽  
pp. 6781-6788 ◽  
Author(s):  
József Tözsér ◽  
Péter Bagossi ◽  
Irene T. Weber ◽  
Terry D. Copeland ◽  
Stephen Oroszlan
Keyword(s):  
Substrate Specificity ◽  
Comparative Studies ◽  
Avian Myeloblastosis Virus

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.

Further Comparative Studies on Ascites in Liver and Heart Disease

1950 ◽  
Vol 16 (1) ◽  
pp. 91-103 ◽  
Author(s):  
John A. Layne ◽  
F.R. Schemm ◽  
W.W. Hurst
Keyword(s):  
Heart Disease ◽  
Comparative Studies
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