Overexpression of the Saccharomyces cerevisiae MET17/MET25 gene in Escherichia coli and comparative characterization of the product with O-acetylserine · O-acetylhomoserine sulfhydrylase of the yeast

1994 ◽  
Vol 42 (1) ◽  
pp. 92-99 ◽  
Author(s):  
S. Yamagata ◽  
M. Isaji ◽  
K. Nakamura ◽  
S. Fujisaki ◽  
K. Doi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Comparative Characterization

scholarly journals Cloning and expression of Saccharomyces cerevisiae copper-metallothionein gene in Escherichia coli and characterization of the recombinant protein

1993 ◽  
Vol 212 (2) ◽  
pp. 521-528 ◽  
Author(s):  
Zehra SAYERS ◽  
Patricia BROUILLON ◽  
Constantin E. VORGIAS ◽  
Hans F. NOLTING ◽  
Christoph HERMES ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Recombinant Protein ◽  
Cloning And Expression ◽  
Metallothionein Gene

scholarly journals Characterization of a Maltase from an Early-Diverged Non-Conventional Yeast Blastobotrys adeninivorans

2019 ◽  
Vol 21 (1) ◽  
pp. 297 ◽  
Author(s):  
Triinu Visnapuu ◽  
Aivar Meldre ◽  
Kristina Põšnograjeva ◽  
Katrin Viigand ◽  
Karin Ernits ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Aspergillus Oryzae ◽  
Hydrolysis Product ◽  
Hydrolytic Activity ◽  
Glycoside Hydrolases ◽  
Arxula Adeninivorans ◽  
Sequence Identity ◽  
Diabetes Drug

Genome of an early-diverged yeast Blastobotrys (Arxula) adeninivorans (Ba) encodes 88 glycoside hydrolases (GHs) including two α-glucosidases of GH13 family. One of those, the rna_ARAD1D20130g-encoded protein (BaAG2; 581 aa) was overexpressed in Escherichia coli, purified and characterized. We showed that maltose, other maltose-like substrates (maltulose, turanose, maltotriose, melezitose, malto-oligosaccharides of DP 4‒7) and sucrose were hydrolyzed by BaAG2, whereas isomaltose and isomaltose-like substrates (palatinose, α-methylglucoside) were not, confirming that BaAG2 is a maltase. BaAG2 was competitively inhibited by a diabetes drug acarbose (Ki = 0.8 µM) and Tris (Ki = 70.5 µM). BaAG2 was competitively inhibited also by isomaltose-like sugars and a hydrolysis product—glucose. At high maltose concentrations, BaAG2 exhibited transglycosylating ability producing potentially prebiotic di- and trisaccharides. Atypically for yeast maltases, a low but clearly recordable exo-hydrolytic activity on amylose, amylopectin and glycogen was detected. Saccharomyces cerevisiae maltase MAL62, studied for comparison, had only minimal ability to hydrolyze these polymers, and its transglycosylating activity was about three times lower compared to BaAG2. Sequence identity of BaAG2 with other maltases was only moderate being the highest (51%) with the maltase MalT of Aspergillus oryzae.

Characterization of ubiquitin C-terminal hydrolase 1 (YUH1) from Saccharomyces cerevisiae expressed in recombinant Escherichia coli

2007 ◽  
Vol 56 (1) ◽  
pp. 20-26 ◽  
Author(s):  
Hyun-Ah Yu ◽  
Sung-Gun Kim ◽  
Eun-Jeong Kim ◽  
Woo-Jong Lee ◽  
Dae-Ok Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Recombinant Escherichia Coli

Expression, purification, and characterization of asparaginase II from Saccharomyces cerevisiae in Escherichia coli

2019 ◽  
Vol 159 ◽  
pp. 21-26 ◽  
Author(s):  
Wagner Lopes ◽  
Bárbara Adriana Ferreira dos Santos ◽  
André Luiz Franco Sampaio ◽  
Ana Paula Gregório Alves Fontão ◽  
Hilton Jorge Nascimento ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Purification And Characterization
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