Catalytic Zinc Site and Mechanism of the Metalloenzyme PR-AMP Cyclohydrolase
Author:
Affiliation:
1. Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana 47907, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi300391m
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4. N1-(5‘-Phosphoribosyl)adenosine−5‘-Monophosphate Cyclohydrolase: Purification and Characterization of a Unique Metalloenzyme
5. Transition-state stabilization by adenosine deaminase: 1,6-addition of water to purine ribonucleoside, the enzyme's affinity for 6-hydroxy-1,6-dihydropurine ribonucleoside, and the effective concentration of substrate water at the active site
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