Engineered Asparaginase from Erwinia chrysanthemi enhances asparagine hydrolase activity and diminishes enzyme immunoreactivity

2021 ◽  
Author(s):  
Iris Munhoz Costa ◽  
Débora Custódio Moura ◽  
Guilherme Meira Lima ◽  
Adalberto Pessoa ◽  
Camila Oresco dos Santos ◽  
...  
Keyword(s):  
Hydrolase Activity ◽  
Erwinia Chrysanthemi

scholarly journals PehN, a Polygalacturonase Homologue with a Low Hydrolase Activity, Is Coregulated with the Other Erwinia chrysanthemi Polygalacturonases

2002 ◽  
Vol 184 (10) ◽  
pp. 2664-2673 ◽  
Author(s):  
Nicole Hugouvieux-Cotte-Pattat ◽  
Vladimir E. Shevchik ◽  
William Nasser
Keyword(s):  
Rna Polymerase ◽  
Direct Interaction ◽  
Pectate Lyase ◽  
Soft Rot ◽  
Hydrolase Activity ◽  
Erwinia Chrysanthemi ◽  
Receptor Protein ◽  
Glycosyl Hydrolases ◽  
Pectate Lyases ◽  
Almost All

ABSTRACT Erwinia chrysanthemi 3937 secretes an arsenal of pectinolytic enzymes, including at least eight endo-pectate lyases encoded by pel genes, which play a major role in the soft-rot disease caused by this bacterium on various plants. E. chrysanthemi also produces some hydrolases that cleave pectin. Three adjacent hydrolase genes, pehV, pehW, and pehX, encoding exo-poly-α-d-galacturonosidases, have been characterized. These enzymes liberate digalacturonides from the nonreducing end of pectin. We report the identification of a novel gene, named pehN, encoding a protein homologous to the glycosyl hydrolases of family 28, which includes mainly polygalacturonases. PehN has a low hydrolase activity on polygalacturonate and on various pectins. PehN action favors the activity of the secreted endo-pectate lyases, mainly PelB and PelC, and that of the periplasmic exo-pectate lyase PelX. However, removal of the pehN gene does not significantly alter the virulence of E. chrysanthemi. Regulation of pehN transcription was analyzed by using gene fusions. Like other pectinase genes, pehN transcription is dependent on several environmental conditions. It is induced by pectic catabolic products and is affected by growth phase, catabolite repression, osmolarity, anaerobiosis, nitrogen starvation, and the presence of calcium ions. The transcription of pehN is modulated by the repressor KdgR, which controls almost all the steps of pectin catabolism, and by cyclic AMP receptor protein (CRP), the global activator of sugar catabolism. The regulator PecS, which represses the transcription of the pel genes but activates that of pehV, pehW, and pehX, also activates transcription of pehN. The three regulators KdgR, PecS, and CRP act by direct interaction with the pehN promoter region. The sequences involved in the binding of these three regulators and of RNA polymerase have been precisely defined. Analysis of the simultaneous binding of these proteins indicates that CRP and RNA polymerase bind cooperatively and that the binding of KdgR could prevent pehN transcription. In contrast, the activator effect of PecS is not linked to competition with KdgR or to cooperation with CRP or RNA polymerase. This effect probably results from competition between PecS and an unidentified repressor involved in peh regulation.

Changes of Lysosomal Hydrolase Activity in the Anterior Pituitary of Hens during Induced Molting

2002 ◽  
Vol 39 (1) ◽  
pp. 22-26 ◽  
Author(s):  
Vishwajit S. Chowdhury ◽  
Yukinori Yoshimura
Keyword(s):  
Anterior Pituitary ◽  
Hydrolase Activity ◽  
Lysosomal Hydrolase

scholarly journals Nostoc commune UTEX 584 gene expressing indole phosphate hydrolase activity in Escherichia coli.

1989 ◽  
Vol 171 (2) ◽  
pp. 708-713 ◽  
Author(s):  
W Q Xie ◽  
B A Whitton ◽  
J W Simon ◽  
K Jäger ◽  
D Reed ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Hydrolase Activity ◽  
Nostoc Commune ◽  
Gene Expressing

scholarly journals Monoacylmonoalkylglycerol as a substrate for diacylglycerol hydrolase activity in adipose tissue.

1978 ◽  
Vol 19 (5) ◽  
pp. 654-656
Author(s):  
H Tornqvist ◽  
P Björgell ◽  
L Krabisch ◽  
P Belfrage
Keyword(s):  
Adipose Tissue ◽  
Hydrolase Activity

scholarly journals Enzyme's Hydrolase Activity Hints at Root of Disease

2005 ◽  
Vol 280 (22) ◽  
pp. e99926
Keyword(s):  
Hydrolase Activity

scholarly journals Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity

Diabetologia ◽  
2006 ◽  
Vol 49 (7) ◽  
pp. 1629-1636 ◽  
Author(s):  
A. Mairal ◽  
D. Langin ◽  
P. Arner ◽  
J. Hoffstedt
Keyword(s):  
Hydrolase Activity ◽  
Adipose Triglyceride Lipase ◽  
Triglyceride Lipase

scholarly journals Retinyl palmitate hydrolase activity in normal rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4498-4503
Author(s):  
J.H. Prystowsky ◽  
J.E. Smith ◽  
D.S. Goodman
Keyword(s):  
Rat Liver ◽  
Retinyl Palmitate ◽  
Hydrolase Activity ◽  
Normal Rat
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