Nucleases of the S1–P1 family can be found in fungi, plants, protozoan parasites and, interestingly, in some bacteria. A cluster of three zinc ions coordinates the substrate/product scissile phosphate and the reaction mechanism utilizes water activated by Zn2+ ions as a nucleophile [2]. Their native role usually lies in nucleotides/nucleosides scavenging [3], specific apoptotic functions [4, 5] and in symbiont (pathogen)–host interactions [6]. This enzyme class is generally substrate sequence–nonspecific and representatives from different types of organisms realize substrate binding via a variation of the same basic approach. Even if several studies already addressed ligand binding in this nuclease family exhaustive experimental evidence regarding ligand binding principles in this family is still missing.
Function
They are zinc dependent nucleases/3’nucleotidases active on both RNA and DNA with acidic or close to neutral pH optima. They act as phosphoesterases cleaving the P–O3’ bond and producing 5‘mononucleotides as end products.
Disease
is a disease
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Relevance
Structural highlights
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