{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,2]],"date-time":"2026-03-02T23:19:46Z","timestamp":1772493586568,"version":"3.50.1"},"reference-count":52,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2021,3,30]],"date-time":"2021-03-30T00:00:00Z","timestamp":1617062400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/publicdomain\/zero\/1.0\/"}],"funder":[{"DOI":"10.13039\/100012728","name":"Frederick National Laboratory for Cancer Research","doi-asserted-by":"publisher","award":["HHSN261200800001E"],"award-info":[{"award-number":["HHSN261200800001E"]}],"id":[{"id":"10.13039\/100012728","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P20GM103449"],"award-info":[{"award-number":["P20GM103449"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"crossref","award":["P20GM103449"],"award-info":[{"award-number":["P20GM103449"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"crossref"}]},{"name":"NIH Intramural Research Program","award":["ZIA BC 010341"],"award-info":[{"award-number":["ZIA BC 010341"]}]},{"name":"NIH Intramural Research Program","award":["ZIA BC 010341"],"award-info":[{"award-number":["ZIA BC 010341"]}]},{"name":"NIH Intramural Research Program","award":["ZIC BC 011016"],"award-info":[{"award-number":["ZIC BC 011016"]}]},{"name":"NIH Intramural Research Program","award":["ZIC BC 011016"],"award-info":[{"award-number":["ZIC BC 011016"]}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p><jats:italic>N<\/jats:italic>-hydroxylating flavin-dependent monooxygenases (FMOs) are involved in the biosynthesis of hydroxamate siderophores, playing a key role in microbial virulence. Herein, we report the first structural and kinetic characterization of a novel alkyl diamine <jats:italic>N<\/jats:italic>-hydroxylase DesB from <jats:italic>Streptomyces sviceus<\/jats:italic> (<jats:italic>Ss<\/jats:italic>DesB). This enzyme catalyzes the first committed step in the biosynthesis of desferrioxamine B, a clinical drug used to treat iron overload disorders. X-ray crystal structures of the <jats:italic>Ss<\/jats:italic>DesB holoenzyme with FAD and the ternary complex with bound NADP<jats:sup>+<\/jats:sup> were solved at 2.86 \u00c5 and 2.37 \u00c5 resolution, respectively, providing a structural view of the active site environment. <jats:italic>Ss<\/jats:italic>DesB crystallized as a tetramer and the structure of the individual protomers closely resembles the structures of homologous <jats:italic>N<\/jats:italic>-hydroxylating FMOs from <jats:italic>Erwinia amylovora<\/jats:italic> (DfoA), <jats:italic>Pseudomonas aeruginosa<\/jats:italic> (PvdA), and <jats:italic>Aspergillus fumigatus<\/jats:italic> (SidA). Using NADPH oxidation, oxygen consumption, and product formation assays, kinetic parameters were determined for various substrates with <jats:italic>Ss<\/jats:italic>DesB. <jats:italic>Ss<\/jats:italic>DesB exhibited typical saturation kinetics with substrate inhibition at high concentrations of NAD(P)H as well as cadaverine. The apparent <jats:italic>k<\/jats:italic><jats:sub><jats:italic>cat<\/jats:italic><\/jats:sub> values for NADPH in steady-state NADPH oxidation and oxygen consumption assays were 0.28 \u00b1 0.01 s<jats:sup>-1<\/jats:sup> and 0.24 \u00b1 0.01 s<jats:sup>-1<\/jats:sup>, respectively. However, in product formation assays used to measure the rate of <jats:italic>N<\/jats:italic>-hydroxylation, the apparent <jats:italic>k<\/jats:italic><jats:sub><jats:italic>cat<\/jats:italic><\/jats:sub> for NADPH (0.034 \u00b1 0.008 s<jats:sup>-1<\/jats:sup>) was almost 10-fold lower under saturating FAD and cadaverine concentrations, reflecting an uncoupled reaction, and the apparent NADPH K<jats:sub>M<\/jats:sub> was 33 \u00b1 24 \u03bcM. Under saturating FAD and NADPH concentrations, the apparent <jats:italic>k<\/jats:italic><jats:sub><jats:italic>cat<\/jats:italic><\/jats:sub> and K<jats:sub>M<\/jats:sub> for cadaverine in Csaky assays were 0.048 \u00b1 0.004 s<jats:sup>-1<\/jats:sup> and 19 \u00b1 9 \u03bcM, respectively. <jats:italic>Ss<\/jats:italic>DesB also <jats:italic>N<\/jats:italic>-hydroxylated putrescine, spermidine, and L-lysine substrates but not alkyl (di)amines that were branched or had fewer than four methylene units in an alkyl chain. These data demonstrate that <jats:italic>Ss<\/jats:italic>DesB has wider substrate scope compared to other well-studied ornithine and lysine <jats:italic>N<\/jats:italic>-hydroxylases, making it an amenable biocatalyst for the production of desferrioxamine B, derivatives, and other <jats:italic>N<\/jats:italic>-substituted products.<\/jats:p>","DOI":"10.1371\/journal.pone.0248385","type":"journal-article","created":{"date-parts":[[2021,3,30]],"date-time":"2021-03-30T17:37:03Z","timestamp":1617125823000},"page":"e0248385","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":13,"title":["Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus"],"prefix":"10.1371","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1089-1276","authenticated-orcid":true,"given":"Lesley-Ann","family":"Giddings","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3463-8881","authenticated-orcid":true,"given":"George T.","family":"Lountos","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kang Woo","family":"Kim","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew","family":"Brockley","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Danielle","family":"Needle","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Scott","family":"Cherry","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joseph E.","family":"Tropea","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David S.","family":"Waugh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2021,3,30]]},"reference":[{"key":"pone.0248385.ref001","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.molcatb.2016.08.003","article-title":"Identification and 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