Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate Decarboxylase
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Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Enzyme Architecture: Erection of Active Orotidine 5'-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes.Orotidine 5'-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis.Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)† †Electronic supplementary information (ESI) available: Further experimental and computational data. See DOI: 10.1039/c5sc03666f.
P2860
Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate Decarboxylase
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2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@ast
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@en
type
label
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@ast
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@en
prefLabel
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@ast
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@en
P2093
P2860
P1433
P1476
Rate and Equilibrium Constants ...... 5'-Monophosphate Decarboxylase
@en
P2093
Bogdana Goryanova
John A Gerlt
Lawrence M Goldman
Shonoi Ming
Tina L Amyes
P2860
P304
P356
10.1021/ACS.BIOCHEM.5B00591
P407
P577
2015-07-14T00:00:00Z