Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Mario Klimacek"'
Publikováno v:
Biotechnology for Biofuels, Vol 14, Iss 1, Pp 1-15 (2021)
Abstract Background Cellodextrin phosphorylase (CdP; EC 2.4.1.49) catalyzes the iterative β-1,4-glycosylation of cellobiose using α-d-glucose 1-phosphate as the donor substrate. Cello-oligosaccharides (COS) with a degree of polymerization (DP) of u
Externí odkaz:
https://doaj.org/article/acac5fd0bdd446da8a24612858072cf5
Publikováno v:
Biotechnology for Biofuels
Biotechnology for Biofuels, Vol 14, Iss 1, Pp 1-15 (2021)
Biotechnology for Biofuels, Vol 14, Iss 1, Pp 1-15 (2021)
Background Cellodextrin phosphorylase (CdP; EC 2.4.1.49) catalyzes the iterative β-1,4-glycosylation of cellobiose using α-d-glucose 1-phosphate as the donor substrate. Cello-oligosaccharides (COS) with a degree of polymerization (DP) of up to 6 ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7fae386587df13396509629069d686e
https://doi.org/10.1186/s13068-021-01982-2
https://doi.org/10.1186/s13068-021-01982-2
Chemical group-transfer reactions by hydrolytic enzymes have considerable importance in biocatalytic synthesis and are exploited broadly in commercial-scale chemical production. Mechanistically, these reactions have in common the involvement of a cov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc44110e718201aac2a99b1ea77e888b
https://doi.org/10.22541/au.158896189.90644329
https://doi.org/10.22541/au.158896189.90644329
Publikováno v:
Bioresource Technology. 130:439-448
Spent sulfite liquor (SSL) is a by-product of pulp and paper manufacturing and is a promising substrate for second-generation bioethanol production. The Saccharomyces cerevisiae strain IBB10B05 presented herein for SSL fermentation was enabled to xyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bbee110bfc3f06b19bc2ee6dfc2cd8d
https://doi.org/10.1016/j.biortech.2012.11.115
https://doi.org/10.1016/j.biortech.2012.11.115
Publikováno v:
The Journal of Biological Chemistry
Background: The active site of mannitol 2-dehydrogenase from Pseudomonas fluorescens is connected with bulk solvent through a narrow protein channel. Glu292 adopts flexible positions down and up the channel. Results: Evidence linking motions of Glu29
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2adb0e7f821aecb96929cbd7d0b2245
http://europepmc.org/articles/PMC3307286
http://europepmc.org/articles/PMC3307286
Publikováno v:
FEBS Journal. 278:1264-1276
The human pathogenic fungus Aspergillus fumigatus accumulates large amounts of intracellular mannitol to enhance its resistance against defense strategies of the infected host. To explore their currently unknown roles in mannitol metabolism, we studi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f0839671c9215809f93730712ab9c292
https://doi.org/10.1111/j.1742-4658.2011.08047.x
https://doi.org/10.1111/j.1742-4658.2011.08047.x
Publikováno v:
Applied and Environmental Microbiology. 76:7566-7574
Little is known about how the general lack of efficiency with which recombinant Saccharomyces cerevisiae strains utilize xylose affects the yeast metabolome. Quantitative metabolomics was therefore performed for two xylose-fermenting S. cerevisiae st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c50a9aa067ca1cf693e9e1e8b885c94
https://doi.org/10.1128/aem.01787-10
https://doi.org/10.1128/aem.01787-10
Autor:
Mario Klimacek, Bernd Nidetzky
Publikováno v:
Journal of Biological Chemistry. 285:30644-30653
Directional preference in catalysis is often used to distinguish alcohol dehydrogenases from carbonyl reductases. However, the mechanistic basis underpinning this discrimination is weak. In mannitol 2-dehydrogenase from Pseudomonas fluorescens, stabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0a0745153f1919862f663deab788203
https://doi.org/10.1074/jbc.m110.108993
https://doi.org/10.1074/jbc.m110.108993
Publikováno v:
Biochemical Journal. 421:43-49
Despite their widely varying physiological functions in carbonyl metabolism, AKR2B5 ( Candida tenuis xylose reductase) and many related enzymes of the aldo-keto reductase protein superfamily utilise PQ (9,10-phenanthrenequinone) as a common in vitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b1d3f429c5f5c2ce56fbe4349a62bcc
https://doi.org/10.1042/bj20090128
https://doi.org/10.1042/bj20090128
Publikováno v:
FEBS Letters. 582:4095-4099
Substitution of active-site Tyr-51 by Ala (Y51A) disrupted the activity of Candida tenuis xylose reductase by six orders of magnitude. External bromide brought about unidirectional rate enhancement ( approximately 2x10(3)-fold at 300mM) for NAD(+)-de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::746c9b6501393e4ea7468bb700deba07
https://doi.org/10.1016/j.febslet.2008.11.003
https://doi.org/10.1016/j.febslet.2008.11.003