<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chitty JL</submitter><funding>National Health and Medical Research Council</funding><pagination>11829-11839</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5512076</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>292(28)</volume><pubmed_abstract>There is significant clinical need for new antifungal agents to manage infections with pathogenic species such as &lt;i>Cryptococcus neoformans&lt;/i> Because the purine biosynthesis pathway is essential for many metabolic processes, such as synthesis of DNA and RNA and energy generation, it may represent a potential target for developing new antifungals. Within this pathway, the bifunctional enzyme adenylosuccinate (ADS) lyase plays a role in the formation of the key intermediates inosine monophosphate and AMP involved in the synthesis of ATP and GTP, prompting us to investigate ADS lyase in &lt;i>C. neoformans.&lt;/i> Here, we report that &lt;i>ADE13&lt;/i> encodes ADS lyase in &lt;i>C. neoformans.&lt;/i> We found that an &lt;i>ade13&lt;/i>Δ mutant is an adenine auxotroph and is unable to successfully cause infection</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>&lt;i>Cryptococcus neoformans&lt;/i> ADS lyase is an enzyme essential for virulence whose crystal structure reveals features exploitable in antifungal drug design.</pubmed_title><pmcid>PMC5512076</pmcid><funding_grant_id>APP1049716</funding_grant_id><funding_grant_id>1003325, 1110971</funding_grant_id><pubmed_authors>Chitty JL</pubmed_authors><pubmed_authors>Kappler U</pubmed_authors><pubmed_authors>Butler MS</pubmed_authors><pubmed_authors>Fraser JA</pubmed_authors><pubmed_authors>Blake KL</pubmed_authors><pubmed_authors>Thompson M</pubmed_authors><pubmed_authors>Koh YQAE</pubmed_authors><pubmed_authors>Robertson AAB</pubmed_authors><pubmed_authors>Williams SJ</pubmed_authors><pubmed_authors>Blundell RD</pubmed_authors><pubmed_authors>Cooper MA</pubmed_authors><pubmed_authors>Kobe B</pubmed_authors></additional><is_claimable>false</is_claimable><name>&lt;i>Cryptococcus neoformans&lt;/i> ADS lyase is an enzyme essential for virulence whose crystal structure reveals features exploitable in antifungal drug design.</name><description>There is significant clinical need for new antifungal agents to manage infections with pathogenic species such as &lt;i>Cryptococcus neoformans&lt;/i> Because the purine biosynthesis pathway is essential for many metabolic processes, such as synthesis of DNA and RNA and energy generation, it may represent a potential target for developing new antifungals. Within this pathway, the bifunctional enzyme adenylosuccinate (ADS) lyase plays a role in the formation of the key intermediates inosine monophosphate and AMP involved in the synthesis of ATP and GTP, prompting us to investigate ADS lyase in &lt;i>C. neoformans.&lt;/i> Here, we report that &lt;i>ADE13&lt;/i> encodes ADS lyase in &lt;i>C. neoformans.&lt;/i> We found that an &lt;i>ade13&lt;/i>Δ mutant is an adenine auxotroph and is unable to successfully cause infection</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jul</publication><modification>2026-05-05T10:47:55.254Z</modification><creation>2019-03-26T23:46:09Z</creation></dates><accession>S-EPMC5512076</accession><cross_references><pubmed>28559277</pubmed><doi>10.1074/jbc.M117.787994</doi><doi>10.1074/jbc.m117.787994</doi></cross_references></HashMap>