Two new phospholipase D isoforms of Loxosceles laeta: Cloning, heterologous expression, functional characterization, and potential biotechnological application

2011 ◽  
Vol 25 (6) ◽  
pp. 393-403 ◽  
Author(s):  
A Catalán ◽  
W Cortes ◽  
H Sagua ◽  
J González ◽  
J. E. Araya
Keyword(s):  
Heterologous Expression ◽  
Phospholipase D ◽  
Functional Characterization ◽  
Biotechnological Application ◽  
Loxosceles Laeta

scholarly journals Heterologous expression and functional characterization of a GH10 endoxylanase from Aspergillus fumigatus var. niveus with potential biotechnological application

2019 ◽  
Vol 24 ◽  
pp. e00382 ◽  
Author(s):  
Josman Velasco ◽  
Bianca Oliva ◽  
Evandro José Mulinari ◽  
Leidy Patricia Quintero ◽  
Awana da Silva Lima ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Aspergillus Fumigatus ◽  
Functional Characterization ◽  
Biotechnological Application

scholarly journals Molecular cloning, heterologous expression, and functional characterization of a cellulolytic enzyme (Cel PRII) from buffalo rumen metagenome

3 Biotech ◽  
2017 ◽  
Vol 7 (4) ◽  
Author(s):  
Ravi K. Shah ◽  
Amrutlal K. Patel ◽  
Deepti M. Davla ◽  
Ishan K. Parikh ◽  
Ramalingam B. Subramanian ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Molecular Cloning ◽  
Functional Characterization ◽  
Cellulolytic Enzyme ◽  
Rumen Metagenome ◽  
Buffalo Rumen

scholarly journals Heterologous Expression and Functional Characterization of Novel CYP2C9 Variants Identified in the Alaska Native People

2020 ◽  
Vol 374 (2) ◽  
pp. 233-240
Author(s):  
Matthew G. McDonald ◽  
Lindsay M. Henderson ◽  
Sutapa Ray ◽  
Catherine K. Yeung ◽  
Amanda L. Johnson ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Alaska Native ◽  
Functional Characterization ◽  
Native People

scholarly journals Functional Characterization of Corynebacterium alkanolyticum β-Xylosidase and Xyloside ABC Transporter in Corynebacterium glutamicum

2015 ◽  
Vol 81 (12) ◽  
pp. 4173-4183 ◽  
Author(s):  
Akira Watanabe ◽  
Kazumi Hiraga ◽  
Masako Suda ◽  
Hideaki Yukawa ◽  
Masayuki Inui
Keyword(s):  
Heterologous Expression ◽  
Corynebacterium Glutamicum ◽  
Abc Transporter ◽  
Binding Protein ◽  
Functional Characterization ◽  
Product Inhibition ◽  
Gene Encoding ◽  
Content Type ◽  
Industrial Strains ◽  
Efficient Fermentation

ABSTRACTTheCorynebacterium alkanolyticumxylEFGDgene cluster comprises thexylDgene that encodes an intracellular β-xylosidase next to thexylEFGoperon encoding a substrate-binding protein and two membrane permease proteins of a xyloside ABC transporter. Cloning of the cluster revealed a recombinant β-xylosidase of moderately high activity (turnover forp-nitrophenyl-β-d-xylopyranoside of 111 ± 4 s−1), weak α-l-arabinofuranosidase activity (turnover forp-nitrophenyl-α-l-arabinofuranoside of 5 ± 1 s−1), and high tolerance to product inhibition (Kifor xylose of 67.6 ± 2.6 mM). Heterologous expression of the entire cluster under the control of the strong constitutivetacpromoter in theCorynebacterium glutamicumxylose-fermenting strain X1 enabled the resultant strain X1EFGD to rapidly utilize not only xylooligosaccharides but also arabino-xylooligosaccharides. The ability to utilize arabino-xylooligosaccharides depended oncgR_2369, a gene encoding a multitask ATP-binding protein. Heterologous expression of the contiguousxylDgene in strain X1 led to strain X1D with 10-fold greater β-xylosidase activity than strain X1EFGD, albeit with a total loss of arabino-xylooligosaccharide utilization ability and only half the ability to utilize xylooligosaccharides. The findings suggest some inherent ability ofC. glutamicumto take up xylooligosaccharides, an ability that is enhanced by in the presence of a functionalxylEFG-encoded xyloside ABC transporter. The finding thatxylEFGimparts nonnative ability to take up arabino-xylooligosaccharides should be useful in constructing industrial strains with efficient fermentation of arabinoxylan, a major component of lignocellulosic biomass hydrolysates.

Functional characterization of a sex pheromone receptor in the pest moth Spodoptera littoralis by heterologous expression in Drosophila

2012 ◽  
Vol 36 (5) ◽  
pp. 2588-2596 ◽  
Author(s):  
Nicolas Montagné ◽  
Thomas Chertemps ◽  
Isabelle Brigaud ◽  
Adrien François ◽  
Marie-Christine François ◽  
...  
Keyword(s):  
Sex Pheromone ◽  
Heterologous Expression ◽  
Spodoptera Littoralis ◽  
Functional Characterization ◽  
Pheromone Receptor

scholarly journals A Lysine Substitute for K+

2002 ◽  
Vol 277 (51) ◽  
pp. 49651-49654 ◽  
Author(s):  
Georgiy A. Belogurov ◽  
Reijo Lahti
Keyword(s):  
Escherichia Coli ◽  
Heterologous Expression ◽  
Phylogenetic Analyses ◽  
Functional Characterization ◽  
Membrane Vesicles ◽  
Thermophilic Bacterium ◽  
Inorganic Pyrophosphatase ◽  
Inner Membrane ◽  
Carboxydothermus Hydrogenoformans

The H+proton-translocating inorganic pyrophosphatase (H+-PPase) family is composed of two phylogenetically distinct types of enzymes: K+-dependent and K+-independent. However, to date, the sequence criteria governing this dichotomy have remained unknown. In this study, we describe the heterologous expression and functional characterization of H+-PPase from the thermophilic bacteriumCarboxydothermus hydrogenoformans. Both PPi-hydrolyzing and PPi-energized H+translocation activities of the recombinant enzyme inEscherichia coliinner membrane vesicles are strictly K+-dependent. Here we deduce the K+requirement of all available H+-PPase sequences based on the K+dependence ofC. hydrogenoformansH+-PPase in conjunction with phylogenetic analyses. Our data reveal that K+-independent H+-PPases possess conserved Lys and Thr that are absent in K+-dependent H+-PPases. We further demonstrate that a A460K substitution inC. hydrogenoformansH+-PPase is sufficient to confer K+independence to both PPihydrolysis and PPi-energized H+translocation. In contrast, a A463T mutation does not affect the K+dependence of H+-PPase.

Tryptophan and aspartic acid residues present in the glycerophosphoryl diester phosphodiesterase (GDPD) domain of the Loxosceles laeta phospholipase D are essential for substrate recognition

Toxicon ◽  
2014 ◽  
Vol 81 ◽  
pp. 43-47 ◽  
Author(s):  
Alejandro Catalán ◽  
William Cortés ◽  
Christian Muñoz ◽  
Jorge E. Araya
Keyword(s):  
Aspartic Acid ◽  
Phospholipase D ◽  
Substrate Recognition ◽  
Loxosceles Laeta

scholarly journals Functional Characterization of Homo- and Heteromeric Channel Kinases TRPM6 and TRPM7

2006 ◽  
Vol 127 (5) ◽  
pp. 525-537 ◽  
Author(s):  
Mingjiang Li ◽  
Jianmin Jiang ◽  
Lixia Yue
Keyword(s):  
Heterologous Expression ◽  
Divalent Cation ◽  
Functional Characterization ◽  
Ph Sensitivity ◽  
Physiological Processes ◽  
Heteromeric Channel ◽  
Unitary Conductance ◽  
Cation Permeability

TRPM6 and TRPM7 are two known channel kinases that play important roles in various physiological processes, including Mg2+ homeostasis. Mutations in TRPM6 cause hereditary hypomagnesemia and secondary hypocalcemia (HSH). However, whether TRPM6 encodes functional channels is controversial. Here we demonstrate several signature features of TRPM6 that distinguish TRPM6 from TRPM7 and TRPM6/7 channels. We show that heterologous expression of TRPM6 but not the mutant TRPM6S141L produces functional channels with divalent cation permeability profile and pH sensitivity distinctive from those of TRPM7 channels and TRPM6/7 complexes. TRPM6 exhibits unique unitary conductance that is 2- and 1.5-fold bigger than that of TRPM7 and TRPM6/7. Moreover, micromolar levels of 2-aminoethoxydiphenyl borate (2-APB) maximally increase TRPM6 but significantly inhibit TRPM7 channel activities; whereas millimolar concentrations of 2-APB potentiate TRPM6/7 and TRPM7 channel activities. Furthermore, Mg2+ and Ca2+ entry through TRPM6 is enhanced three- to fourfold by 2-APB. Collectively, these results indicate that TRPM6 forms functional homomeric channels as well as heteromeric TRPM6/7 complexes. The unique characteristics of these three channel types, TRPM6, TRPM7, and TRPM6/7, suggest that they may play different roles in vivo.

Sequence, Heterologous Expression and Functional Characterization of a Novel Tryparedoxin from Crithidia fasciculata

1998 ◽  
Vol 379 (8-9) ◽  
Author(s):  
Marisa Montemartini ◽  
Henryk M. Kalisz ◽  
Michael Kiess ◽  
Everson Nogoceke ◽  
Mahavir Singh ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Functional Characterization ◽  
Crithidia Fasciculata
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