scholarly journals Enzymatic activities associated with cell wall preparations from corn coleoptiles

1961 ◽  
Vol 36 (5) ◽  
pp. 605-610 ◽  
Author(s):  
A. Kivilaan ◽  
T. Cabrera Beaman ◽  
R. S. Bandurski
2006 ◽  
Vol 72 (11) ◽  
pp. 7003-7012 ◽  
Author(s):  
Yoh-ichi Shimma ◽  
Fumie Saito ◽  
Fumi Oosawa ◽  
Yoshifumi Jigami

ABSTRACT Fifty-one human glycosyltransferases were expressed in Saccharomyces cerevisiae as immobilized enzymes and were assayed for enzymatic activities. The stem and catalytic regions of sialyl-, fucosyl-, galactosyl-, N-acetylgalactosaminyl-, and N-acetylglucosaminyltransferases were fused with yeast cell wall Pir proteins, which anchor glycosyltransferases at the yeast cell wall glucan. More than 75% of expressed recombinant glycosyltransferases retained their enzymatic activities in the yeast cell wall fraction and will be used as a human glycosyltransferase library. In increasing the enzymatic activities of immobilized glycosyltransferases, several approaches were found to be effective. Additional expression of yeast protein disulfide isomerase increased the expression levels and activities of polypeptide N-acetylgalactosaminyltransferases and other glycosyltransferases. PIR3 and/or PIR4 was more effective than PIR1 as a cell wall anchor when the Pir-glycosyltransferase fusions were expressed under the control of the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter. Oligosaccharides such as Lewis x, Lewis y, and H antigen were successfully synthesized using this immobilized glycosyltransferase library, indicating that the Pir-fused glycosyltransferases are useful for the production of various human oligosaccharides.


1987 ◽  
Vol 127 (1-2) ◽  
pp. 11-22 ◽  
Author(s):  
Julio Llamazares ◽  
José L. Acebes ◽  
Ignacio Zarra

2003 ◽  
Vol 107 (4) ◽  
pp. 421-427 ◽  
Author(s):  
Gloria Innocenti ◽  
Roberta Roberti ◽  
Matteo Montanari ◽  
Eva Zakrisson

1995 ◽  
Vol 146 (5-6) ◽  
pp. 748-750 ◽  
Author(s):  
Jan Burczyk ◽  
Eckhard Loos

2018 ◽  
Vol 238 ◽  
pp. 325-332 ◽  
Author(s):  
Patricio Ramos ◽  
Carolina Parra-Palma ◽  
Carlos R. Figueroa ◽  
Paz E. Zuñiga ◽  
Felipe Valenzuela-Riffo ◽  
...  

OENO One ◽  
2003 ◽  
Vol 37 (1) ◽  
pp. 23
Author(s):  
Khalid Amrani Joutei ◽  
F. Ouazzani Chahdi ◽  
D. Bouya ◽  
Cédric Saucier ◽  
Yves Glories

<p style="text-align: justify;">Pectolytic enzymes act differently on the degradation of the cell wall of grape skin and on the libération of tannins. PG and PL degrade the pectin from the middle lamella and the primary wall which favours the liberation of granulate tannins present inside the vacuole only ones. Cellulase degrade the cellulose fibbers and allows the liberation of tannins bound to the cellular wall. These last ones being bound to cellulosic molecules.</p>


2018 ◽  
Vol 62 (1) ◽  
pp. 80-88 ◽  
Author(s):  
M. Moneo-Sanchez ◽  
L. Izquierdo ◽  
I. Martin ◽  
J. Hernandez-Nistal ◽  
L. Albornos ◽  
...  

Antibiotics ◽  
2018 ◽  
Vol 7 (3) ◽  
pp. 64 ◽  
Author(s):  
Krizia Pérez Medina ◽  
Joseph Dillard

The peptidoglycan cell wall that encloses the bacterial cell and provides structural support and protection is remodeled by multiple enzymes that synthesize and cleave the polymer during growth. This essential and dynamic structure has been targeted by multiple antibiotics to treat gonococcal infections. Up until now, antibiotics have been used against the biosynthetic machinery and the therapeutic potential of inhibiting enzymatic activities involved in peptidoglycan breakdown has not been explored. Given the major antibiotic resistance problems we currently face, it is crucial to identify other possible targets that are key to maintaining cell integrity and contribute to disease development. This article reviews peptidoglycan as an antibiotic target, how N. gonorrhoeae has developed resistance to currently available antibiotics, and the potential of continuing to target this essential structure to combat gonococcal infections by attacking alternative enzymatic activities involved in cell wall modification and metabolism.


Sign in / Sign up

Export Citation Format

Share Document