ChemInform Abstract: Investigations on the Enzyme Specificity of Clostripain: A New Efficient Biocatalyst for the Synthesis of Peptide Isosteres.

ChemInform ◽  
2010 ◽  
Vol 31 (24) ◽  
pp. no-no
Author(s):  
Robert Guenther ◽  
Anja Stein ◽  
Frank Bordusa
Keyword(s):  
Enzyme Specificity ◽  
Peptide Isosteres

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.

Reversing enzyme specificity

Nature ◽  
1989 ◽  
Vol 339 (6226) ◽  
pp. 580-581 ◽  
Author(s):  
Thomas L. Poulos
Keyword(s):  
Enzyme Specificity

Lid domain plasticity and lipid flexibility modulate enzyme specificity in human monoacylglycerol lipase

2017 ◽  
Vol 1862 (5) ◽  
pp. 441-451 ◽  
Author(s):  
Laura Riccardi ◽  
Jose M. Arencibia ◽  
Luca Bono ◽  
Andrea Armirotti ◽  
Stefania Girotto ◽  
...  
Keyword(s):  
Enzyme Specificity ◽  
Monoacylglycerol Lipase ◽  
Lid Domain

scholarly journals Mi2β Shows Chromatin Enzyme Specificity by Erasing a DNase I-hypersensitive Site Established by ACF

2009 ◽  
Vol 284 (12) ◽  
pp. 7533-7541 ◽  
Author(s):  
Haruhiko Ishii ◽  
Hansen Du ◽  
Zhaoqing Zhang ◽  
Angus Henderson ◽  
Ranjan Sen ◽  
...  
Keyword(s):  
Dnase I ◽  
Enzyme Specificity ◽  
Hypersensitive Site ◽  
Dnase I Hypersensitive Site

scholarly journals The Methionine 549 and Leucine 552 Residues of Friedelin Synthase from Maytenus ilicifolia Are Important for Substrate Binding Specificity

Molecules ◽  
2021 ◽  
Vol 26 (22) ◽  
pp. 6806
Author(s):  
Bruna F. Mazzeu ◽  
Tatiana M. Souza-Moreira ◽  
Andrew A. Oliveira ◽  
Melissa Remlinger ◽  
Lidiane G. Felippe ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biological Activities ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Enzyme Specificity ◽  
Amino Acid Residues ◽  
Loss Of Function ◽  
Pentacyclic Triterpene ◽  
Oxidosqualene Cyclases ◽  
Maytenus Ilicifolia

Friedelin, a pentacyclic triterpene found in the leaves of the Celastraceae species, demonstrates numerous biological activities and is a precursor of quinonemethide triterpenes, which are promising antitumoral agents. Friedelin is biosynthesized from the cyclization of 2,3-oxidosqualene, involving a series of rearrangements to form a ketone by deprotonation of the hydroxylated intermediate, without the aid of an oxidoreductase enzyme. Mutagenesis studies among oxidosqualene cyclases (OSCs) have demonstrated the influence of amino acid residues on rearrangements during substrate cyclization: loss of catalytic activity, stabilization, rearrangement control or specificity changing. In the present study, friedelin synthase from Maytenus ilicifolia (Celastraceae) was expressed heterologously in Saccharomyces cerevisiae. Site-directed mutagenesis studies were performed by replacing phenylalanine with tryptophan at position 473 (Phe473Trp), methionine with serine at position 549 (Met549Ser) and leucine with phenylalanine at position 552 (Leu552Phe). Mutation Phe473Trp led to a total loss of function; mutants Met549Ser and Leu552Phe interfered with the enzyme specificity leading to enhanced friedelin production, in addition to α-amyrin and β-amyrin. Hence, these data showed that methionine 549 and leucine 552 are important residues for the function of this synthase.

Sign in / Sign up

Export Citation Format

Share Document