Angebote zu "Enzymatic" (20 Treffer)

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Selenoprotein
34,00 € *
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In molecular biology a selenoprotein is any protein that includes a selenocysteine (Se-Cys) amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Se-Cys. Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Se-Cys residues, which are split into two domains, a longer N-terminal domain that contains 1 Se-Cys, and a shorter C-terminal domain that contains 9 Se-Cys. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive Selenium atom throughout the body.

Anbieter: Dodax
Stand: 28.01.2020
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Computer Modeling of Enzyme Catalysis and Inhib...
50,40 € *
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Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes , and were also investigated in the context of PKC- inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC- were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC.

Anbieter: Dodax AT
Stand: 28.01.2020
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Computer Modeling of Enzyme Catalysis and Inhib...
49,00 € *
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Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes , and were also investigated in the context of PKC- inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC- were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC.

Anbieter: Dodax
Stand: 28.01.2020
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Using Mass Spectrometry for Biochemical Studies...
103,72 € *
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This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from trans-AT Polyketide Synthases (PKSs). Using a combination of electrospray ionisation-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, the specificity of a range of KS domains from the bacillaene and psymberin PKSs have been succsessfully studied with regard to the initial acylation step of KS-catalysis.In addition, the ability to alter the substrate tolerance of KS domains by simple point mutations in the active site has been demonstrated. A series of acyl-ACPs have been synthesised using a novel methodology and employed to probe the substrate specificity of both KS domains and the previously uncharcterised acyl hydrolase domain, PedC.KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. The findings in this thesis provide important insights into mechanisms of KS specificity and show that mutagenesis can be used to expand the repertoire of acceptable substrates for future PKS engineering.

Anbieter: Dodax
Stand: 28.01.2020
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Using Mass Spectrometry for Biochemical Studies...
98,77 € *
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This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from trans-AT Polyketide Synthases (PKSs). Using a combination of electrospray ionisation-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, the specificity of a range of KS domains from the bacillaene and psymberin PKSs have been succsessfully studied with regard to the initial acylation step of KS-catalysis.In addition, the ability to alter the substrate tolerance of KS domains by simple point mutations in the active site has been demonstrated. A series of acyl-ACPs have been synthesised using a novel methodology and employed to probe the substrate specificity of both KS domains and the previously uncharcterised acyl hydrolase domain, PedC.KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. The findings in this thesis provide important insights into mechanisms of KS specificity and show that mutagenesis can be used to expand the repertoire of acceptable substrates for future PKS engineering.

Anbieter: Dodax AT
Stand: 28.01.2020
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Aquifex aeolicus sulfide: quinone oxidoreductase
100,80 € *
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The membrane associated flavoenzyme sulfide:quinone oxidoreductase (SQR) has been essential in the early stages of life on Earth, when the organisms had to survive high sulfide concentrations in the environment. Interestingly, it has been successively conserved in many species belonging to all three biological domains, and also in humans, revealing that its activity in the cells is still crucial nowadays. In particular, SQR is involved in sulfide detoxification, in sulfide-dependent respiration and photosynthesis, in heavy metal tolerance and in the regulation of sulfide homeostasis in higher eukaryotes, where sulfide has recently been discovered to act as a neurotransmitter. However, despite its high microbiological and medical relevance, SQR had remained poorly characterized until now, so the understanding of its function was limited. This book describes the SQR from the hyperthermophilic bacterium Aquifex aeolicus in a detailed structural, biochemical and functional perspective, thereby offering for the first time a deep insight into its intriguing but complicated enzymatic reaction.

Anbieter: Dodax AT
Stand: 28.01.2020
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Aquifex aeolicus sulfide: quinone oxidoreductase
98,00 € *
ggf. zzgl. Versand

The membrane associated flavoenzyme sulfide:quinone oxidoreductase (SQR) has been essential in the early stages of life on Earth, when the organisms had to survive high sulfide concentrations in the environment. Interestingly, it has been successively conserved in many species belonging to all three biological domains, and also in humans, revealing that its activity in the cells is still crucial nowadays. In particular, SQR is involved in sulfide detoxification, in sulfide-dependent respiration and photosynthesis, in heavy metal tolerance and in the regulation of sulfide homeostasis in higher eukaryotes, where sulfide has recently been discovered to act as a neurotransmitter. However, despite its high microbiological and medical relevance, SQR had remained poorly characterized until now, so the understanding of its function was limited. This book describes the SQR from the hyperthermophilic bacterium Aquifex aeolicus in a detailed structural, biochemical and functional perspective, thereby offering for the first time a deep insight into its intriguing but complicated enzymatic reaction.

Anbieter: Dodax
Stand: 28.01.2020
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Using Mass Spectrometry for Biochemical Studies...
106,99 € *
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Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases ab 106.99 € als pdf eBook: . Aus dem Bereich: eBooks, Fachthemen & Wissenschaft, Wissenschaften allgemein,

Anbieter: hugendubel
Stand: 28.01.2020
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Using Mass Spectrometry for Biochemical Studies...
117,49 € *
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Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases ab 117.49 € als gebundene Ausgabe: 1st ed. 2016. Aus dem Bereich: Bücher, Wissenschaft, Biologie,

Anbieter: hugendubel
Stand: 28.01.2020
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