PMID:21474759: Difference between revisions
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| | !align=left |Citation | ||
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'''No author listed''' (2011) A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. ''Science'' '''332''':234-8 | |||
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| | !align=left |Abstract | ||
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Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21474759 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3151171 PMC3151171] | |||
Online version:[http://dx.doi.org/10.1126/science.1198542 10.1126/science.1198542] | Online version:[http://dx.doi.org/10.1126/science.1198542 10.1126/science.1198542] | ||
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!align=left |Keywords | |||
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Amino Acid Sequence; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Folic Acid/chemistry; Kinetics; Models, Molecular; Molecular Sequence Data; Mutant Proteins/chemistry; Mutant Proteins/metabolism; NADP/chemistry; Protein Conformation; Tetrahydrofolate Dehydrogenase/chemistry; Tetrahydrofolate Dehydrogenase/genetics; Tetrahydrofolate Dehydrogenase/metabolism | |||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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Revision as of 19:12, 1 September 2013
| Citation |
No author listed (2011) A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science 332:234-8 |
|---|---|
| Abstract |
Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts. |
| Links |
PubMed PMC3151171 Online version:10.1126/science.1198542 |
| Keywords |
Amino Acid Sequence; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Escherichia coli/enzymology; Folic Acid/chemistry; Kinetics; Models, Molecular; Molecular Sequence Data; Mutant Proteins/chemistry; Mutant Proteins/metabolism; NADP/chemistry; Protein Conformation; Tetrahydrofolate Dehydrogenase/chemistry; Tetrahydrofolate Dehydrogenase/genetics; Tetrahydrofolate Dehydrogenase/metabolism |
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