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The structure of the Arabidopsis thaliana guanosine deaminaseThe structure of the Arabidopsis thaliana guanosine deaminase
Structural highlights
FunctionGSDA_ARATH Catalyzes the hydrolytic deamination of guanosine, producing xanthosine and ammonia. Deaminates exclusively guanosine and 2'-deoxyguanosine but no other aminated purines, pyrimidines, or pterines. Deamination of guanosine by GSDA is the only source of xanthosine production in Arabidopsis.[1] Publication Abstract from PubMedGuanosine deaminase (GSDA) in plants specifically deaminates (de)guanosine to produce xanthosine with high specificity, which is further converted to xanthine, a key intermediate in purine metabolism and nitrogen recycling. We solved GSDA's structures from Arabidopsis thaliana in the free and ligand-bound forms at high resolutions. Unlike GDA, the enzyme employs a single-proton shuttle mechanism for catalysis and both the substrate and enzyme undergo structural rearrangements. The last fragment of the enzyme loops back and seals the active site, and the substrate rotates during the reaction, both essential to deamination. We further identified more substrates that could be employed by the enzyme and compare it with other deaminases to reveal the recognition differences of specific substrates. Our studies provide insight into this important enzyme involved in purine metabolism and will potentially aid in the development of deaminase-based gene-editing tools. The C-terminal loop of Arabidopsis thaliana guanosine deaminase is essential to catalysis.,Jia Q, Zeng H, Li H, Xiao N, Tang J, Gao S, Zhang J, Xie W Chem Commun (Camb). 2021 Sep 23;57(76):9748-9751. doi: 10.1039/d1cc03042f. PMID:34477187[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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