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Balancing the stability-activity trade-off by fine-tuning dehalogenase access tunnels

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Balancing the Stability-Activity Trade-off by Fine-Tuning
Engineering of access tunnel in haloalkane dehalogenase to minimise stability-function trade-off R. Chaloupkova 1, V. Liskova 1, D. Bednar 1, T. Prudnikova 2,3, P. Rezacova 4,5, T. Koudelakova 1, E. Sebestova 1, I. Kuta Smatanova 2, J. Brezovsky 1, J. Damborsky 1,6 1 Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic …
Caver Web 1.0: identification of tunnels and channels in
A variant of the haloalkane dehalogenase DhaA with greatly enhanced stability and tolerance of organic solvents but reduced activity was created by mutating four residues in the access tunnel. To create a stabilized enzyme with superior catalytic activity, two of the four originally modified residues were randomized.
Reprint - Masaryk University balancing the stability-activity trade-off by fine-tuning dehalogenase access tunnels
Basic information; Original name: Balancing the Stability-Activity Trade-off by Fine-Tuning Dehalogenase Access Tunnels. Authors: LIŠKOVÁ, Veronika (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution), T. PRUDNIKOVA (112 Belarus), P. REZACOVA (203 Czech Republic), Táňa KOUDELÁKOVÁ …
Balancing the Stability-Activity Trade-off by Fine-Tuning
Abstract A variant of the haloalkane dehalogenase DhaA with greatly enhanced stability and tolerance of organic solvents but reduced activity was created by mutating four residues in the access
Exploiting the activity–stability trade-off of glucose
A variant of the haloalkane dehalogenase DhaA with greatly enhanced stability and tolerance of organic solvents but reduced activity was created by mutating four residues in the access tunnel. To create a stabilized enzyme with superior catalytic activity, two of the four originally modified residues were randomized. The resulting mutant F176G exhibited 10- and 32-times enhanced …
Balancing the Stability–Activity Trade‐Off by Fine‐Tuning
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Balancing the Stability-Activity Trade-off by Fine-Tuning balancing the stability-activity trade-off by fine-tuning dehalogenase access tunnels
Basic information; Original name: Balancing the Stability-Activity Trade-off by Fine-Tuning Dehalogenase Access Tunnels. Authors: LIŠKOVÁ, Veronika (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution), T. PRUDNIKOVA (112 Belarus), P. REZACOVA (203 Czech Republic), Táňa KOUDELÁKOVÁ …
Engineering of access tunnel in haloalkane dehalogenase to
A variant of the haloalkane dehalogenase DhaA with greatly enhanced stability and tolerance of organic solvents but reduced activity was created by mutating four residues in the access tunnel. To create a stabilized enzyme with superior catalytic activity, two of the four originally modified residues were randomized.
Caver Web 1.0: identification of tunnels and channels in
Základní údaje; Originální název: Balancing the Stability-Activity Trade-off by Fine-Tuning Dehalogenase Access Tunnels. Autoři: LIŠKOVÁ, Veronika (203 Česká republika, domácí), David BEDNÁŘ (203 Česká republika, domácí), T. PRUDNIKOVA (112 Bělorusko), P. REZACOVA (203 Česká republika), Táňa KOUDELÁKOVÁ (203 Česká republika, domácí), …
Expansion of Access Tunnels and Active‐Site Cavities
Delicate balance between activity and stability of enzymes can be manipulated by fine-tuning the diameter and dynamics of their access tunnels. Discover the …
Balancing the Stability-Activity Trade-off by Fine …
10 reasons why you will fall in love with MU . Ask our ambassador . Research
Balancing the Stability-Activity Trade-off by … balancing the stability-activity trade-off by fine-tuning dehalogenase access tunnels
Cosolvent molecules entered the enzymes access tunnels and active sites, enlarged their volumes with no change in overall protein structure, but surprisingly did not act as competitive inhibitors. At low concentrations, the cosolvents either enhanced catalysis by lowering K 0.5 and increasing k cat, or caused enzyme inactivation by promoting substrate inhibition and …
Balancing the Stability-Activity Trade-Off by Fine-Tuning balancing the stability-activity trade-off by fine-tuning dehalogenase access tunnels
Research interests: protein crystallogenesis and crystallography Facility responsibility: X-ray ivanaks at seznam.cz (kuta at prf.jcu.cz) (+420)-608-106-109 C 01 025 Part time also at the Institute of Microbiology ASCR, Nove Hrady
Balancing the Stability-Activity Trade-off by Fine-Tuning
The importance of access tunnels in proteins has been demonstrated by many studies in the last decade (Kingsley et al., Balancing the Stability-Activity Trade-Off by Fine-Tuning Dehalogenase Access Tunnels. ChemCatChem , 7, 648 – 659. Google Scholar. Crossref. Search ADS Manak. M. et al. (2017) Interactive Analysis of Connoly Surfaces for Various …
CAVER Analyst 2.0: analysis and visualization of channels
Delicate balance between activity and stability of enzymes can be manipulated by fine‐tuning the diameter and dynamics of their access tunnels. Citing Literature Supporting Information
Balancing the Stability–Activity Trade‐Off by Fine‐Tuning
Balancing the Stability–Activity Trade-Off by Fine-Tuning Dehalogenase Access Tunnels Tuning enzyme access tunnels: The catalytic activity and stability of en- zymes can be inversely related. It is shown that haloalkane dehalogenases with high stability and activity can be created by fine-tuning the diameter and dynamics of the access tunnels that connect buried active …
Balancing the Stability–Activity Trade‐Off by Fine‐Tuning
Balancing the Stability–Activity Trade-Off by Fine-Tuning Dehalogenase Access Tunnels Tuning enzyme access tunnels: The catalytic activity and stability of en-zymes can be inversely related. It is shown that haloalkane dehalogenases with high stability and activity can be created by fine-tuning the diameter and dynamics of the access tunnels that

 

 

 

               

 

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