'Super-perfect' enzymes: Structural stabilities and activities of recombinant triose phosphate isomerases from Pyrococcus furiosus and Thermococcus onnurineus produced in Escherichia coli.
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Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.Endoglucanase activity at a second site in Pyrococcus furiosus triosephosphate isomerase-Promiscuity or compensation for a metabolic handicap?Flux Control in Glycolysis Varies Across the Tree of Life.Kinetics study on recombinant alkaline phosphatase and correlation with the generated fluorescent signal.Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production.
P2860
'Super-perfect' enzymes: Structural stabilities and activities of recombinant triose phosphate isomerases from Pyrococcus furiosus and Thermococcus onnurineus produced in Escherichia coli.
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2015年の論文
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2015年論文
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name
'Super-perfect' enzymes: Struc ...... produced in Escherichia coli.
@en
type
label
'Super-perfect' enzymes: Struc ...... produced in Escherichia coli.
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prefLabel
'Super-perfect' enzymes: Struc ...... produced in Escherichia coli.
@en
P1476
'Super-perfect' enzymes: Struc ...... s produced in Escherichia coli
@en
P2093
Prerna Sharma
P304
P356
10.1016/J.BBRC.2015.03.102
P50
P577
2015-03-27T00:00:00Z