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Cited by 305

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Two-Metal-Ion Catalysis in Adenylyl Cyclase

Tesmer, John J. G., Sunahara, Roger K., Johnson, Roger A., Gosselin, Gilles, Gilman, Alfred G., Sprang, Stephen R.·1999·Science

Abstract

Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor.

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Metadata

Authors
Tesmer, J. J. G., Sunahara, R. K., Johnson, R. A., Gosselin, G., Gilman, A. G., & Sprang, S. R.
Venue
Science
Published
1999-07-30
Volume
285
Issue
5428
Pages
756-760
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2151421295
Cited by
305
References
32
FWCI
6.09
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Two-Metal-Ion Catalysis in Adenylyl Cyclase. https://app.cochat.ai/papers/10.1126/science.285.5428.756
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Tesmer, J. J. G., Sunahara, R. K., Johnson, R. A., Gosselin, G., Gilman, A. G., & Sprang, S. R. (1999). Two-Metal-Ion Catalysis in Adenylyl Cyclase. Science. https://doi.org/10.1126/science.285.5428.756

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