Mechanism of the adenylate cyclase reaction. Stereochemistry of the reaction catalyzed by the enzyme from Brevibacterium liquefaciens

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 i...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-01, Vol.255 (2), p.331-334
Main Authors: Gerlt, J A, Coderre, J A, Wolin, M S
Format: Article
Language:English
Subjects:
Adenylyl Cyclases - metabolism
Brevibacterium - enzymology
Cyclic AMP - analogs & derivatives
Magnetic Resonance Spectroscopy
Stereoisomerism
Substrate Specificity
Thionucleotides
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)86171-9