scholarly journals Effects of urease inhibitors on enzymatic activities and fungal communities during the biosolids composting

RSC Advances ◽  
2021 ◽  
Vol 11 (60) ◽  
pp. 37667-37676
Author(s):  
Jishao Jiang ◽  
Yang Wang ◽  
Dou Yu ◽  
Jingyu Li ◽  
Jin Han ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activities ◽  
Fungal Communities ◽  
Urease Inhibitors ◽  
Nitrogen Conservation

Adding UI was effective for nitrogen conservation and the increase of enzyme activity during biosolid composting.

Enzymatic Activities of Mycelia in Mycorrhizal Fungal Communities

2005 ◽  
pp. 331-348
Author(s):  
John Cairney ◽  
Bj”rn Lindahl ◽  
Roger Finlay
Keyword(s):  
Enzymatic Activities ◽  
Fungal Communities

scholarly journals Ectomycorrhizal Fungal Communities and Enzymatic Activities Vary across an Ecotone between a Forest and Field

2015 ◽  
Vol 1 (2) ◽  
pp. 185-210 ◽  
Author(s):  
Megan Rúa ◽  
Becky Moore ◽  
Nicole Hergott ◽  
Lily Van ◽  
Colin Jackson ◽  
...  
Keyword(s):  
Enzymatic Activities ◽  
Fungal Communities

scholarly journals Parallel modulation of brush border myosin conformation and enzyme activity induced by monoclonal antibodies.

1989 ◽  
Vol 109 (2) ◽  
pp. 549-556 ◽  
Author(s):  
S Citi ◽  
R A Cross ◽  
C R Bagshaw ◽  
J Kendrick-Jones
Keyword(s):  
Enzyme Activity ◽  
Monoclonal Antibodies ◽  
Ionic Strength ◽  
Brush Border ◽  
Active Sites ◽  
High Ionic Strength ◽  
Enzymatic Activities ◽  
Filament Assembly ◽  
Order Of Magnitude ◽  
Low Ionic Strength

Monoclonal antibodies binding to distinct epitopes on the tail of brush border myosin were used to modulate the conformation and state of assembly of this myosin. BM1 binds 1:3 of the distance from the tip of the tail to the head and prevents the extended-tail (6S) monomer from folding into the assembly-incompetent folded-tail (10S) state, whereas BM4 binds to the tip of the myosin tail, and induces the myosin to fold into the 10S state. Thus, at physiological ionic strength BM1 promotes and BM4 blocks the assembly of the myosin into filaments. Using BM1 and BM4 together, we were able to prevent both folding and filament assembly, thus locking myosin molecules in the extended-tail 6S monomer conformation at low ionic strength where they normally assemble into filaments. Using these myosin-antibody complexes, we were able to investigate independently the effects of folding of the myosin tail and assembly into filaments on the myosin MgATPase. The enzymatic activities were measured from the fluorescent profiles during the turnover of the ATP analogue formycin triphosphate (FTP). Extended-tail (6S) myosin molecules had an FTPase activity of 1-5 X 10(-3) s-1, either at high ionic strength as a monomer alone or when complexed with antibody, or at low ionic strength as filaments or when maintained as extended-tail monomers by the binding of BM1 and BM4. Folding of the molecules into the 10S state reduced this rate by an order of magnitude, effectively trapping the products of FTP hydrolysis in the active sites.

scholarly journals Diversity and Enzyme Activity of Ectomycorrhizal Fungal Communities Following Nitrogen Fertilization in an Urban-Adjacent Pine Plantation

Forests ◽  
2018 ◽  
Vol 9 (3) ◽  
pp. 99 ◽  
Author(s):  
Chen Ning ◽  
Gregory Mueller ◽  
Louise Egerton-Warburton ◽  
Andrew Wilson ◽  
Wende Yan ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Nitrogen Fertilization ◽  
Fungal Communities ◽  
Pine Plantation

Chondroitin 4-O-sulfotransferase-1 regulates the chain length of chondroitin sulfate in co-operation with chondroitin N-acetylgalactosaminyltransferase-2

2011 ◽  
Vol 434 (2) ◽  
pp. 321-331 ◽  
Author(s):  
Tomomi Izumikawa ◽  
Yuka Okuura ◽  
Toshiyasu Koike ◽  
Naoki Sakoda ◽  
Hiroshi Kitagawa
Keyword(s):  
Enzyme Activity ◽  
Chondroitin Sulfate ◽  
Chain Length ◽  
Critical Role ◽  
Enzymatic Activities ◽  
Cell Mutant ◽  
Expression Levels ◽  
L Cells ◽  
L Cell ◽  
Mutant Cells

Previously, we demonstrated that sog9 cells, a murine L cell mutant, are deficient in the expression of C4ST (chondroitin 4-O-sulfotransferase)-1 and that they synthesize fewer and shorter CS (chondroitin sulfate) chains. These results suggested that C4ST-1 regulates not only 4-O-sulfation of CS, but also the length and amount of CS chains; however, the mechanism remains unclear. In the present study, we have demonstrated that C4ST-1 regulates the chain length and amount of CS in co-operation with ChGn-2 (chondroitin N-acetylgalactosaminyltransferase 2). Overexpression of ChGn-2 increased the length and amount of CS chains in L cells, but not in sog9 mutant cells. Knockdown of ChGn-2 resulted in a decrease in the amount of CS in L cells in a manner proportional to ChGn-2 expression levels, whereas the introduction of mutated C4ST-1 or ChGn-2 lacking enzyme activity failed to increase the amount of CS. Furthermore, the non-reducing terminal 4-O-sulfation of N-acetylgalactosamine residues facilitated the elongation of CS chains by chondroitin polymerase consisting of chondroitin synthase-1 and chondroitin-polymerizing factor. Overall, these results suggest that the chain length of CS is regulated by C4ST-1 and ChGn-2 and that the enzymatic activities of these proteins play a critical role in CS elongation.

scholarly journals Copper ion altered association network among multi-genes and enzyme activity of laccase in Ganoderma lucidum

2018 ◽  
Author(s):  
Xincong Kang ◽  
Yuewen Chen ◽  
Sien Yan ◽  
Luman Zeng ◽  
Xuehui Liu ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Gene Family ◽  
Ganoderma Lucidum ◽  
Laccase Activity ◽  
Copper Ion ◽  
Interaction Network ◽  
Enzymatic Activities ◽  
Functional Genes ◽  
Polyphenol Oxidases ◽  
Laccase Genes

Background: Laccases, copper-based polyphenol oxidases, played vital roles in lignin and humus degradation as well as fruiting body formation and stress response. Sixteen putative laccase genes (Lacc1-Lacc16) were reported in the genome of white-rot fungus Ganoderma lucidum. Members in this multi-gene family usually had close inter-relationships and may vary in the roles contributing to functions. Identifying the interactions among multiple genes and thus the conjoined consequence to an activity was essential for systematically unraveling the molecular mechanisms of laccase and improving laccase activity. Methods: In this study, multivariate statistical analysis was applied to track the relationship between thetranscriptional level of laccase genes and the total enzymatic activities. We outlined and compared the interaction networks among the transcriptional levels of 16 laccase genes and associations with the total enzymatic activities with or without copper ion (Cu 2+ ). Results: A multi-gene interaction network among the sixteen genes and laccase activity was constructed to figure out the changes induced by Cu 2+ . The interaction network showed that the enzyme activity was the result of interactions among genes, and these interactions might vary with the presence of Cu 2+ , subsequently leading to the alteration of enzyme activity. Some genes always kept relation with enzyme activity (positive or negative, Lacc13, Lacc10), some were irrelevant (Lacc1, Lacc6), while another some were inconsistent (Lacc3, Lacc8, Lacc14 and Lacc15). Discussion: Network-based methods were applied to identify key functional genes and to outline associations among genes and phenotype in laccase multi-gene family. This is an exploratory strategy to describe the transcriptional complexity of laccase and its relevant responses to Cu 2+ stress. The identified key functional genes associated with laccase activity (e.g. Lacc10, Lacc13) and the associations among genes and activity will benefit for the regulation of enzyme activity.

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