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Q51602292-3DF258DD-E442-476C-A5EC-9DC207B53EA4
Q51602292-3DF258DD-E442-476C-A5EC-9DC207B53EA4
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http://www.wikidata.org/entity/statement/Q51602292-3DF258DD-E442-476C-A5EC-9DC207B53EA4
Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases.
P2860
Q51602292-3DF258DD-E442-476C-A5EC-9DC207B53EA4
BestRank
Statement
http://www.wikidata.org/entity/statement/Q51602292-3DF258DD-E442-476C-A5EC-9DC207B53EA4
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wasDerivedFrom
f389679501548c368c6c0f8c88837964498de4f4
P2860
Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states.