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Q42677110-60EE4AFB-4E24-4E6C-8878-34F7199629AD
Q42677110-60EE4AFB-4E24-4E6C-8878-34F7199629AD
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42677110-60EE4AFB-4E24-4E6C-8878-34F7199629AD
Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.
P2860
Q42677110-60EE4AFB-4E24-4E6C-8878-34F7199629AD
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42677110-60EE4AFB-4E24-4E6C-8878-34F7199629AD
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wasDerivedFrom
9b37a6b1ae870eadaa47fd426b3adda2499da941
P2860
Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation.