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J. Biol. Chem., Vol. 255, Issue 2, 331-334, Jan, 1980
JA Gerlt, JA Coderre and MS Wolin
Adenylate cyclase from Brevibacterium liquefaciens (ATCC 14929) catalyzes
the formation of the RP-diastereomer of adenosine 3':5'- cyclic
monophosphorothioate from the SP-diastereomer of adenosine-5'-(1-
thiotriphosphate). The reaction catalyzed by this adenylate cyclase
proceeds with inversion of configuration at phosphorus, indicating that the
cyclization reaction is direct and does not involve formation of an
adenylated enzyme intermediate.
Mechanism of the adenylate cyclase reaction. Stereochemistry of the reaction catalyzed by the enzyme from Brevibacterium liquefaciens
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