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Recently, the team of Professor Xu Yan and Yu Xiaowei from the Brewing Microbiology and Applied Enzymology Laboratory of Jiangnan University's Bioengineering College has made important progress in the research of lipase propeptide.
The research results "Propeptide in Rhizopus chinensislipase: new insights into its mechanism of activity and substrate selectivity by computational The cover of "design" was published in the Journal of Agricultural and Food Chemistry (IF=4.
192)
.
The research results "Propeptide in Rhizopus chinensislipase: new insights into its mechanism of activity and substrate selectivity by computational The cover of "design" was published in the Journal of Agricultural and Food Chemistry (IF=4.
192)
.
Lipase (EC 3.
1.
1.
3) has good hydrolysis and synthesis activity on ester bonds, and is widely used in food, pharmaceutical, detergent and bio-energy related industries
.
Among them, fungal lipase has obvious advantages due to its high stability and wide substrate specificity
.
There is a propeptide domain in the structure of most fungal lipases, which is very important for the secretion, catalytic efficiency and substrate selectivity of the lipase
.
In this study, Rhizopus chinensis lipase (Rhizopus chinensis lipase, RCL) was used as the research model, using a combination of Metadynamics simulation, classical molecular dynamics simulation, and site-directed mutagenesis to discuss in depth the influence of the lipase propeptide domain.
Function and mechanism of substrate selectivity
.
The calculation results show that the propeptide domain significantly inhibits the movement of the RCL lid.
Through dynamic cross-correlation analysis and independent gradient model analysis, a key region of inhibition (Val5-Thr10) is found on the leader peptide, and in this fragment Carry out rational design and determination of enzymatic reaction kinetics
.
The catalytic efficiency of the optimal lipase mutant is 7 times higher than that of the wild type, and it also shows the ability of the propeptide domain to change the chain length selectivity of the lipase substrate
.
After substrate expansion, it is found that this regulatory ability is also reflected in other substrates of triglycerides
.
In this study, computer simulation and site-directed mutagenesis are combined to reveal the important role of propeptide key regions in improving the catalytic efficiency of lipase and the controllable change of substrate specificity.
It is also an important role for industrial enzymes that also have similar domains in the leader peptide.
The design and transformation provide a theoretical basis
.
(Bioon.
com)
1.
1.
3) has good hydrolysis and synthesis activity on ester bonds, and is widely used in food, pharmaceutical, detergent and bio-energy related industries
.
Among them, fungal lipase has obvious advantages due to its high stability and wide substrate specificity
.
There is a propeptide domain in the structure of most fungal lipases, which is very important for the secretion, catalytic efficiency and substrate selectivity of the lipase
.
In this study, Rhizopus chinensis lipase (Rhizopus chinensis lipase, RCL) was used as the research model, using a combination of Metadynamics simulation, classical molecular dynamics simulation, and site-directed mutagenesis to discuss in depth the influence of the lipase propeptide domain.
Function and mechanism of substrate selectivity
.
The calculation results show that the propeptide domain significantly inhibits the movement of the RCL lid.
Through dynamic cross-correlation analysis and independent gradient model analysis, a key region of inhibition (Val5-Thr10) is found on the leader peptide, and in this fragment Carry out rational design and determination of enzymatic reaction kinetics
.
The catalytic efficiency of the optimal lipase mutant is 7 times higher than that of the wild type, and it also shows the ability of the propeptide domain to change the chain length selectivity of the lipase substrate
.
After substrate expansion, it is found that this regulatory ability is also reflected in other substrates of triglycerides
.
In this study, computer simulation and site-directed mutagenesis are combined to reveal the important role of propeptide key regions in improving the catalytic efficiency of lipase and the controllable change of substrate specificity.
It is also an important role for industrial enzymes that also have similar domains in the leader peptide.
The design and transformation provide a theoretical basis
.
(Bioon.
com)
Recently, the team of Professor Xu Yan and Yu Xiaowei from the Brewing Microbiology and Applied Enzymology Laboratory of Jiangnan University's Bioengineering College has made important progress in the research of lipase propeptide.
The research results "Propeptide in Rhizopus chinensislipase: new insights into its mechanism of activity and substrate selectivity by computational The cover of "design" was published in the Journal of Agricultural and Food Chemistry (IF=4.
192)
.
The research results "Propeptide in Rhizopus chinensislipase: new insights into its mechanism of activity and substrate selectivity by computational The cover of "design" was published in the Journal of Agricultural and Food Chemistry (IF=4.
192)
.
Lipase (EC 3.
1.
1.
3) has good hydrolysis and synthesis activity on ester bonds, and is widely used in food, pharmaceutical, detergent and bio-energy related industries
.
Among them, fungal lipase has obvious advantages due to its high stability and wide substrate specificity
.
There is a propeptide domain in the structure of most fungal lipases, which is very important for the secretion, catalytic efficiency and substrate selectivity of the lipase
.
In this study, Rhizopus chinensis lipase (Rhizopus chinensis lipase, RCL) was used as the research model, using a combination of Metadynamics simulation, classical molecular dynamics simulation, and site-directed mutagenesis to discuss in depth the influence of the lipase propeptide domain.
Function and mechanism of substrate selectivity
.
The calculation results show that the propeptide domain significantly inhibits the movement of the RCL lid.
Through dynamic cross-correlation analysis and independent gradient model analysis, a key region of inhibition (Val5-Thr10) is found on the leader peptide, and in this fragment Carry out rational design and determination of enzymatic reaction kinetics
.
The catalytic efficiency of the optimal lipase mutant is 7 times higher than that of the wild type, and it also shows the ability of the propeptide domain to change the chain length selectivity of the lipase substrate
.
After substrate expansion, it is found that this regulatory ability is also reflected in other substrates of triglycerides
.
In this study, computer simulation and site-directed mutagenesis are combined to reveal the important role of propeptide key regions in improving the catalytic efficiency of lipase and the controllable change of substrate specificity.
It is also an important role for industrial enzymes that also have similar domains in the leader peptide.
The design and transformation provide a theoretical basis
.
(Bioon.
com)
1.
1.
3) has good hydrolysis and synthesis activity on ester bonds, and is widely used in food, pharmaceutical, detergent and bio-energy related industries
.
Among them, fungal lipase has obvious advantages due to its high stability and wide substrate specificity
.
There is a propeptide domain in the structure of most fungal lipases, which is very important for the secretion, catalytic efficiency and substrate selectivity of the lipase
.
In this study, Rhizopus chinensis lipase (Rhizopus chinensis lipase, RCL) was used as the research model, using a combination of Metadynamics simulation, classical molecular dynamics simulation, and site-directed mutagenesis to discuss in depth the influence of the lipase propeptide domain.
Function and mechanism of substrate selectivity
.
The calculation results show that the propeptide domain significantly inhibits the movement of the RCL lid.
Through dynamic cross-correlation analysis and independent gradient model analysis, a key region of inhibition (Val5-Thr10) is found on the leader peptide, and in this fragment Carry out rational design and determination of enzymatic reaction kinetics
.
The catalytic efficiency of the optimal lipase mutant is 7 times higher than that of the wild type, and it also shows the ability of the propeptide domain to change the chain length selectivity of the lipase substrate
.
After substrate expansion, it is found that this regulatory ability is also reflected in other substrates of triglycerides
.
In this study, computer simulation and site-directed mutagenesis are combined to reveal the important role of propeptide key regions in improving the catalytic efficiency of lipase and the controllable change of substrate specificity.
It is also an important role for industrial enzymes that also have similar domains in the leader peptide.
The design and transformation provide a theoretical basis
.
(Bioon.
com)
