Articles with "thermotoga maritima" as a keyword



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Tolrestat acts atypically as a competitive inhibitor of the thermostable aldo‐keto reductase Tm1743 from Thermotoga maritima

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Published in 2019 at "FEBS Letters"

DOI: 10.1002/1873-3468.13630

Abstract: Tolrestat and epalrestat have been characterized as noncompetitive inhibitors of aldo‐ketone reductase 1B1 (AKR1B1), a leading drug target for the treatment of type 2 diabetes complications. However, clinical applications are limited for most AKR1B1 inhibitors… read more here.

Keywords: reductase; thermotoga maritima; tm1743 thermotoga; tm1743 ... See more keywords
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Acetylornithine aminotransferase TM1785 performs multiple functions in the hyperthermophile Thermotoga maritima.

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Published in 2021 at "FEBS letters"

DOI: 10.1002/1873-3468.14222

Abstract: The hyperthermophilic bacterium Thermotoga maritima peptidoglycan contains unusual D-lysine alongside typical D-alanine and D-glutamate. We previously identified lysine racemase and threonine dehydratase, but knowledge of D-amino acid metabolism remains limited. Herein, we identified and characterized… read more here.

Keywords: aminotransferase; thermotoga maritima; aminotransferase tm1785; acetylornithine aminotransferase ... See more keywords
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High-temperature behavior of hyperthermostable Thermotoga maritima xylanase XYN10B after designed and evolved mutations.

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Published in 2022 at "Applied microbiology and biotechnology"

DOI: 10.1007/s00253-022-11823-3

Abstract: A hyperthermostable xylanase XYN10B from Thermotoga maritima (PDB code 1VBR, GenBank accession number KR078269) was subjected to site-directed and error-prone PCR mutagenesis. From the selected five mutants, the two site-directed mutants (F806H and F806V) showed… read more here.

Keywords: xylanase; xylanase xyn10b; temperature; thermotoga maritima ... See more keywords
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Synthesis of fucosylated oligosaccharides with α-l-fucosidase from Thermotoga maritima immobilized on Eupergit® CM

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Published in 2021 at "Extremophiles"

DOI: 10.1007/s00792-021-01230-3

Abstract: Fucosylated oligosaccharides present in human milk perform various biological functions that benefit infants’ health. These compounds can be also obtained by enzymatic synthesis. In this work, the effect of the immobilization of α- l -fucosidase… read more here.

Keywords: thermotoga maritima; fucosidase thermotoga; synthesis fucosylated; fucosylated oligosaccharides ... See more keywords
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Synthesis of a Fucosylated Trisaccharide Via Transglycosylation by α-l-Fucosidase from Thermotoga maritima

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Published in 2018 at "Applied Biochemistry and Biotechnology"

DOI: 10.1007/s12010-018-2771-x

Abstract: Fucosylated oligosaccharides, such as 2′-fucosyllactose in human milk, have important biological functions such as prebiotics and preventing infection. In this work, the effect of an acceptor substrate (lactose) and the donor substrate 4-nitrophenyl-α-l-fucopyranoside (pNP-Fuc) on… read more here.

Keywords: thermotoga maritima; fucosidase thermotoga; synthesis fucosylated; fucosylated trisaccharide ... See more keywords
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Engineering a switch-based biosensor for arginine using a Thermotoga maritima periplasmic binding protein.

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Published in 2017 at "Analytical biochemistry"

DOI: 10.1016/j.ab.2017.02.021

Abstract: The Thermotoga maritima arginine-binding protein (TmArgBP) has been modified to create a reagentless fluorescent protein biosensor. Two design methods for biosensor construction are compared: 1) solvent accessibility of environmentally-sensitive probes and 2) fluorescence deactivation due… read more here.

Keywords: protein; based biosensor; thermotoga maritima; arginine ... See more keywords
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Structural and biochemical characterization of FabK from Thermotoga maritima.

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Published in 2017 at "Biochemical and biophysical research communications"

DOI: 10.1016/j.bbrc.2016.11.141

Abstract: TM0800 from Thermotoga maritima is one of the hypothetical proteins with unknown function. The crystal structure determined at 2.3 Å resolution reveals a two domain structure: the N-terminal domain forming a barrel and the C-terminal forming… read more here.

Keywords: enzymatic activity; thermotoga; thermotoga maritima; fabk ... See more keywords
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Improving the catalytic activity of thermostable xylanase from Thermotoga maritima via mutagenesis of non-catalytic residues at glycone subsites.

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Published in 2020 at "Enzyme and microbial technology"

DOI: 10.1016/j.enzmictec.2020.109579

Abstract: Endo-β-1,4-xylanase from Thermotoga maritima, TmxB, is an industrially attractive enzyme due to its extreme thermostability. To improve its application value, four variants were designed on the basis of multiple sequence and three-dimensional structure alignments. Wild-type… read more here.

Keywords: non catalytic; thermotoga maritima; glycone subsites; xylanase thermotoga ... See more keywords
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Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima

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Published in 2023 at "Chemical Science"

DOI: 10.1039/d2sc06432d

Abstract: [FeFe] hydrogenases are exceptionally active catalysts for the interconversion of molecular hydrogen with protons and electrons. Their active site, the H-cluster, is composed of a [4Fe–4S] cluster covalently linked to a unique [2Fe] subcluster. These… read more here.

Keywords: thermotoga maritima; coordination; redox; sensory fefe ... See more keywords
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Structural Analysis of Redox-sensing Transcriptional Repressor Rex from Thermotoga maritima.

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Published in 2018 at "Scientific Reports"

DOI: 10.2210/pdb5zz6/pdb

Abstract: The cellular redox state of organisms continues to fluctuate during the metabolism. All organisms have various sensors that help detect and adapt to changes in the redox state. Nicotinamide adenine dinucleotides (NAD+/NADH), which are involved… read more here.

Keywords: nad nadh; thermotoga maritima; redox; rex thermotoga ... See more keywords
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Understanding the Positional Binding and Substrate Interaction of a Highly Thermostable GH10 Xylanase from Thermotoga maritima by Molecular Docking

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Published in 2018 at "Biomolecules"

DOI: 10.3390/biom8030064

Abstract: Glycoside hydrolase family 10 (GH10) xylanases are responsible for enzymatic cleavage of the internal glycosidic linkages of the xylan backbone, to generate xylooligosaccharides (XOS) and xyloses. The topologies of active-site cleft determine the substrate preferences… read more here.

Keywords: understanding positional; gh10; positional binding; thermotoga maritima ... See more keywords