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Q27674002-2E33FBD4-B6CF-483D-B472-F82F99725FEE
Q27674002-2E33FBD4-B6CF-483D-B472-F82F99725FEE
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http://www.wikidata.org/entity/statement/Q27674002-2E33FBD4-B6CF-483D-B472-F82F99725FEE
Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: A Structure-Based Explanation for How the 5′-Phosphate Group Activates the Enzyme
P2860
Q27674002-2E33FBD4-B6CF-483D-B472-F82F99725FEE
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27674002-2E33FBD4-B6CF-483D-B472-F82F99725FEE
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wasDerivedFrom
3b0ac17fb7245ddd8443cea7bbf25bb11211d806
P2860
Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.