scholarly journals Analyzing the function of the insert region found between the α and β-subunits in the eukaryotic nitrile hydratase from Monosiga brevicollis

2018 ◽  
Vol 657 ◽  
pp. 1-7 ◽  
Author(s):  
Xinhang Yang ◽  
Brian Bennett ◽  
Richard C. Holz
Keyword(s):  
Nitrile Hydratase ◽  
Α And Β Subunits ◽  
Insert Region ◽  
Monosiga Brevicollis

scholarly journals A Nitrile Hydratase in the Eukaryote Monosiga brevicollis

PLoS ONE ◽  
2008 ◽  
Vol 3 (12) ◽  
pp. e3976 ◽  
Author(s):  
Konrad U. Foerstner ◽  
Tobias Doerks ◽  
Jean Muller ◽  
Jeroen Raes ◽  
Peer Bork
Keyword(s):  
Nitrile Hydratase ◽  
Monosiga Brevicollis

scholarly journals Pigmentiphaga sp. Strain D-2 Uses a Novel Amidase To Initiate the Catabolism of the Neonicotinoid Insecticide Acetamiprid

2020 ◽  
Vol 86 (6) ◽  
Author(s):  
Hongxing Yang ◽  
Shunli Hu ◽  
Xiang Wang ◽  
Shaochuang Chuang ◽  
Weibin Jia ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Nitrile Hydratase ◽  
Environmental Fate ◽  
Draft Genome ◽  
The Novel ◽  
Content Type ◽  
Neonicotinoid Insecticide ◽  
Α And Β Subunits ◽  
Hydrolysis Of ◽  
Considerable Concern

ABSTRACT Acetamiprid, a chloronicotinyl neonicotinoid insecticide, is among the most commonly used insecticides worldwide, and its environmental fate has caused considerable concern. The compound 1-(6-chloropyridin-3-yl)-N-methylmethanamine (IM 1-4) has been reported to be the main intermediate during acetamiprid catabolism in microorganisms, honeybees, and spinach. However, the molecular mechanism underlying the hydrolysis of acetamiprid to IM 1-4 has not yet been elucidated. In this study, a novel amidase (AceAB) that initially hydrolyzes the C-N bond of acetamiprid to generate IM 1-4 was purified and characterized from the acetamiprid-degrading strain Pigmentiphaga sp. strain D-2. Based on peptide profiling of the purified AceAB and the draft genome sequence of strain D-2, aceA (372 bp) and aceB (2,295 bp), encoding the α and β subunits of AceAB, respectively, were cloned and found to be necessary for acetamiprid hydrolysis in strain D-2. The characteristics of AceAB were also systematically investigated. Though AceA and AceB showed 35% to 56% identity to the α and β subunits of the N,N-dimethylformamidase from Paracoccus aminophilus, AceAB was specific for the hydrolysis of acetamiprid and showed no activities to N,N-dimethylformamide or its structural analogs. IMPORTANCE Acetamiprid, among the top neonicotinoid insecticides used worldwide, is one of the most important commercial insecticides. Due to its extensive use, the environmental fate of acetamiprid, especially its microbial degradation, has caused considerable concern. Although the catabolic pathways of acetamiprid in microorganisms have been extensively studied, the molecular mechanisms underlying acetamiprid biodegradation (except for a nitrile hydratase) remain largely unknown, and the enzyme responsible for the biotransformation of acetamiprid into its main intermediate, IM 1-4, have not yet been elucidated. The amidase AceAB and its encoding genes, aceA and aceB, characterized in this study, were found to be necessary and specific for the initial hydrolysis of the C-N bond of acetamiprid to generate IM 1-4 in Pigmentiphaga sp. strain D-2. The finding of the novel amidase AceAB will greatly enhance our understanding of the microbial catabolism of the widely used insecticide acetamiprid at the molecular level.

ON THE INTERACTION OF A VISCOELASTIC CYLINDRICAL PIPE WITH INNER UNIFORM COATING AND INSERTS WITH A COMPLEX PROFILE

2020 ◽  
Author(s):  
Kirill Kazakov
Keyword(s):  
Complex Shape ◽  
High Accuracy ◽  
Contact Stresses ◽  
Basis Functions ◽  
Complex Profile ◽  
Cylindrical Pipe ◽  
Interference Fit ◽  
Uniform Coating ◽  
Special Basis ◽  
Insert Region

This work is devoted to the formulation and construction of an analytical solution to the problem of contact between a cylindrical viscoelastic aging pipe with an internal thin coating and an insert having a complex shape placed inside the pipe with an interference fit. In practice, the presence of such coatings is required, for example, to protect the main structure from aggressive external or internal environments, for its electrical insulation, etc. The manufacturing process of the inner coating determines its possible heterogeneity (dependence of properties on coordinates). An insert placed inside a pipe can have a complex profile that has a rapidly changing function. Taking these features into account is important when analyzing the stress-strain state of pipes with an internal coating. Using an approach based on the use of special basis functions and the type of solution, a representation for the contact stresses in the pipe in the region of the rigid insert is obtained. This approach makes it possible to distinguish functions that describe the properties of the inner coating and the shape of the outer profile of the insert in the form of separate terms and factors in the expression for the contact stresses in the insert region. Therefore, in order to achieve high accuracy when carrying out calculations, it is sufficient to restrict ourselves to a relatively small number of terms

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

The Stability Enhancement of Nitrile Hydratase from Bordetella petrii by Swapping the C-terminal Domain of β subunit

2015 ◽  
Vol 178 (8) ◽  
pp. 1481-1487 ◽  
Author(s):  
Weifeng Sun ◽  
Longbao Zhu ◽  
Xianggui Chen ◽  
Lunjie Wu ◽  
Zhemin Zhou ◽  
...  
Keyword(s):  
Nitrile Hydratase ◽  
Β Subunit ◽  
Terminal Domain ◽  
The Stability ◽  
Stability Enhancement
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