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Q37701676-F313968C-A89E-40FF-8D99-F78325AECBB0
Q37701676-F313968C-A89E-40FF-8D99-F78325AECBB0
BestRank
Statement
http://www.wikidata.org/entity/statement/Q37701676-F313968C-A89E-40FF-8D99-F78325AECBB0
Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces
P2860
Q37701676-F313968C-A89E-40FF-8D99-F78325AECBB0
BestRank
Statement
http://www.wikidata.org/entity/statement/Q37701676-F313968C-A89E-40FF-8D99-F78325AECBB0
rank
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Statement
wasDerivedFrom
e5839d9e933d81bca0559123d3ccadeeb3db0907
P2860
Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.