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Discovery of a Ni<sup>2+</sup>-dependent guanidine hydrolase in bacteria

Discovery of a Ni2+-dependent guanidine hydrolase in bacteria

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FUNCK, Dietmar, Malte SINN, Jennifer R. FLEMING, Marco STANOPPI, Janine DIETRICH, Rocío LÓPEZ-IGUAL, Olga MAYANS, Jörg S. HARTIG, 2022. Discovery of a Ni2+-dependent guanidine hydrolase in bacteria. In: Nature. Springer Nature. 603(7901), pp. 515-521. ISSN 0028-0836. eISSN 1476-4687. Available under: doi: 10.1038/s41586-022-04490-x

@article{Funck2022-03Disco-56910, title={Discovery of a Ni2+-dependent guanidine hydrolase in bacteria}, year={2022}, doi={10.1038/s41586-022-04490-x}, number={7901}, volume={603}, issn={0028-0836}, journal={Nature}, pages={515--521}, author={Funck, Dietmar and Sinn, Malte and Fleming, Jennifer R. and Stanoppi, Marco and Dietrich, Janine and López-Igual, Rocío and Mayans, Olga and Hartig, Jörg S.} }

Stanoppi, Marco Fleming, Jennifer R. Funck, Dietmar Funck, Dietmar Hartig, Jörg S. López-Igual, Rocío Stanoppi, Marco Fleming, Jennifer R. 2022-03 López-Igual, Rocío Discovery of a Ni<sup>2+</sup>-dependent guanidine hydrolase in bacteria Hartig, Jörg S. 2022-03-17T15:57:11Z 2022-03-17T15:57:11Z Sinn, Malte Nitrogen availability is a growth-limiting factor in many habitats1, and the global nitrogen cycle involves prokaryotes and eukaryotes competing for this precious resource. Only some bacteria and archaea can fix elementary nitrogen; all other organisms depend on the assimilation of mineral or organic nitrogen. The nitrogen-rich compound guanidine occurs widely in nature2-4, but its utilization is impeded by pronounced resonance stabilization5, and enzymes catalysing hydrolysis of free guanidine have not been identified. Here we describe the arginase family protein GdmH (Sll1077) from Synechocystis sp. PCC 6803 as a Ni<sup>2+</sup>-dependent guanidine hydrolase. GdmH is highly specific for free guanidine. Its activity depends on two accessory proteins that load Ni<sup>2+</sup> instead of the typical Mn<sup>2+</sup> ions into the active site. Crystal structures of GdmH show coordination of the dinuclear metal cluster in a geometry typical for arginase family enzymes and allow modelling of the bound substrate. A unique amino-terminal extension and a tryptophan residue narrow the substrate-binding pocket and identify homologous proteins in further cyanobacteria, several other bacterial taxa and heterokont algae as probable guanidine hydrolases. This broad distribution suggests notable ecological relevance of guanidine hydrolysis in aquatic habitats. Dietrich, Janine Mayans, Olga eng terms-of-use Mayans, Olga Sinn, Malte Dietrich, Janine

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