Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue
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Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseProbing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzymeConnecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial EnzymeReflections on the catalytic power of a TIM-barrel.A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Enzyme architecture: on the importance of being in a protein cage.
P2860
Revisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue
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2011 nî lūn-bûn
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2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2011 թվականի օգոստոսին հրատարակված գիտական հոդված
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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name
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@ast
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@en
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@nl
type
label
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@ast
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@en
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@nl
prefLabel
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@ast
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@en
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@nl
P2093
P2860
P356
P1433
P1476
Revisiting the mechanism of th ...... erved glutamic acid 97 residue
@en
P2093
Hemalatha Balaram
M R N Murthy
Moumita Samanta
Padmanabhan Balaram
P2860
P304
P356
10.1002/CBIC.201100116
P577
2011-08-16T00:00:00Z