{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T19:02:57Z","timestamp":1773687777290,"version":"3.50.1"},"reference-count":45,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,10,1]],"date-time":"2021-10-01T00:00:00Z","timestamp":1633046400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003995","name":"Anhui Provincial Natural Science Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003995","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Protein Expression and Purification"],"published-print":{"date-parts":[[2021,10]]},"DOI":"10.1016\/j.pep.2021.105909","type":"journal-article","created":{"date-parts":[[2021,5,20]],"date-time":"2021-05-20T07:57:02Z","timestamp":1621497422000},"page":"105909","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Biochemical characterization and redesign of the coenzyme specificity of a novel monofunctional NAD+-dependent homoserine dehydrogenase from the human pathogen Neisseria gonorrhoeae"],"prefix":"10.1016","volume":"186","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1440-1847","authenticated-orcid":false,"given":"Wanggang","family":"Tang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xue","family":"Dong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jiang","family":"Meng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yanan","family":"Feng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Manman","family":"Xie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Haonan","family":"Xu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1216-3184","authenticated-orcid":false,"given":"Ping","family":"Song","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.pep.2021.105909_bib1","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1093\/jb\/mvy094","article-title":"The crystal structure of homoserine dehydrogenase complexed with l-homoserine and NADPH in a closed form","volume":"165","author":"Akai","year":"2019","journal-title":"J. Biochem."},{"key":"10.1016\/j.pep.2021.105909_bib2","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1107\/S1399004715004617","article-title":"Structural basis for the catalytic mechanism of homoserine dehydrogenase","volume":"71","author":"Navratna","year":"2015","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.pep.2021.105909_bib3","doi-asserted-by":"crossref","first-page":"11674","DOI":"10.1038\/srep11674","article-title":"Crystal structures of a hyperthermophilic archaeal homoserine dehydrogenase suggest a novel cofactor bnding mode fo roxidoreductases","volume":"5","author":"Hayashi","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.pep.2021.105909_bib4","doi-asserted-by":"crossref","first-page":"5361","DOI":"10.1074\/jbc.M207379200","article-title":"Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine","volume":"278","author":"Paris","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2021.105909_bib5","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1006\/prep.2001.1539","article-title":"Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana","volume":"24","author":"Paris","year":"2002","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.pep.2021.105909_bib6","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1093\/oxfordjournals.jbchem.a123427","article-title":"Inhibition of homoserine dehydrogenase I by L-serine in Escherichia coli","volume":"109","author":"Hama","year":"1991","journal-title":"J. Biochem."},{"key":"10.1016\/j.pep.2021.105909_bib7","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1080\/09168451.2018.1511365","article-title":"A novel bifunctional aspartate kinase-homoserine dehydrogenase from the hyperthermophilic bacterium, Thermotoga maritima","volume":"82","author":"Ohshida","year":"2018","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.pep.2021.105909_bib8","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0378-1119(91)90296-N","article-title":"A C-terminal deletion in Corynebacterium glutamicum homoserine dehydrogenase abolishes allosteric inhibition by L-threonine","volume":"107","author":"Archer","year":"1991","journal-title":"Gene"},{"key":"10.1016\/j.pep.2021.105909_bib9","doi-asserted-by":"crossref","first-page":"3228","DOI":"10.1128\/jb.173.10.3228-3230.1991","article-title":"Analysis of a Corynebacterium glutamicum hom gene coding for a feedback-resistant homoserine dehydrogenase","volume":"173","author":"Reinscheid","year":"1991","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.pep.2021.105909_bib10","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1074\/jbc.M109.068882","article-title":"Threonine-insensitive homoserine dehydrogenase from soybean: genomic organization, kinetic mechanism, and in vivo activity","volume":"285","author":"Schroeder","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2021.105909_bib11","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/0014-5793(93)81359-8","article-title":"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases","volume":"323","author":"Thomas","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.pep.2021.105909_bib12","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/S0167-4838(00)00203-X","article-title":"Characterization of yeast homoserine dehydrogenase, an antifungal target: the invariant histidine 309 is important for enzyme integrity","volume":"1544","author":"Jacques","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.pep.2021.105909_bib13","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/73359","article-title":"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases","volume":"7","author":"DeLaBarre","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.pep.2021.105909_bib14","first-page":"14","article-title":"Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction","volume":"3","author":"Tomonaga","year":"2015","journal-title":"Biochem. Biophys. Rep."},{"key":"10.1016\/j.pep.2021.105909_bib15","doi-asserted-by":"crossref","first-page":"5749","DOI":"10.1038\/s41598-018-24063-1","article-title":"Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex","volume":"8","author":"Ogata","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.pep.2021.105909_bib16","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.4014\/jmb.2004.04060","article-title":"Molecular and enzymatic features of homoserine dehydrogenase from Bacillus subtilis","volume":"30","author":"Kim","year":"2020","journal-title":"J. Microbiol. Biotechnol."},{"key":"10.1016\/j.pep.2021.105909_bib17","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/bkcs.11929","article-title":"Biochemical characterization of homoserine dehydrogenase from Pseudomonas aeruginosa","volume":"41","author":"Kim","year":"2019","journal-title":"Bull. Kor. Chem. Soc."},{"key":"10.1016\/j.pep.2021.105909_bib18","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1097\/MOH.0000000000000394","article-title":"Pathogenesis of Neisseria gonorrhoeae in the female reproductive tract: neutrophilic host response, sustained infection, and clinical sequelae","volume":"25","author":"Stevens","year":"2018","journal-title":"Curr. Opin. Hematol."},{"key":"10.1016\/j.pep.2021.105909_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pmed.1002344","article-title":"Antimicrobial resistance in Neisseria gonorrhoeae: global surveillance and a call for international collaborative action","volume":"14","author":"Wi","year":"2017","journal-title":"PLoS Med."},{"key":"10.1016\/j.pep.2021.105909_bib20","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1056\/NEJMp1812269","article-title":"Neisseria gonorrhoeae - Rising infection rates, dwindling treatment options","volume":"379","author":"Blank","year":"2018","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.pep.2021.105909_bib21","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1128\/CMR.00010-14","article-title":"Antimicrobial resistance in Neisseria gonorrhoeae in the 21st century: past, evolution, and future","volume":"27","author":"Unemo","year":"2014","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.pep.2021.105909_bib22","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.3389\/fmicb.2015.01190","article-title":"Proteomics of Neisseria gonorrhoeae: the treasure hunt for countermeasures against an old disease","volume":"6","author":"Baarda","year":"2015","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.pep.2021.105909_bib23","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.chembiol.2003.09.016","article-title":"Simultaneous in vitro assay of the first four enzymes in the fungal aspartate pathway identifies a new class of aspartate kinase inhibitor","volume":"10","author":"Bareich","year":"2003","journal-title":"Chem. Biol."},{"key":"10.1016\/j.pep.2021.105909_bib24","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1021\/ar000057q","article-title":"The central enzymes of the aspartate family of amino acid biosynthesis","volume":"34","author":"Viola","year":"2001","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.pep.2021.105909_bib25","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1007\/s00894-019-4221-2","article-title":"New inhibitors of homoserine dehydrogenase from Paracoccidioides brasiliensis presenting antifungal activity","volume":"25","author":"Bueno","year":"2019","journal-title":"J. Mol. Model."},{"key":"10.1016\/j.pep.2021.105909_bib26","doi-asserted-by":"crossref","DOI":"10.1002\/psc.3060","article-title":"Antifungal dipeptides incorporating an inhibitor of homoserine dehydrogenase","volume":"24","author":"Skwarecki","year":"2018","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.pep.2021.105909_bib27","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1006\/jmbi.2000.4042","article-title":"A novel method for multiple sequence alignments","volume":"302","author":"Notredame","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.pep.2021.105909_bib28","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.pep.2021.105909_bib29","doi-asserted-by":"crossref","first-page":"1710","DOI":"10.1093\/bioinformatics\/btl150","article-title":"Molecular complexes at a glance: automated generation of two-dimensional complex diagrams","volume":"22","author":"Stierand","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.pep.2021.105909_bib30","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1007\/s12033-021-00308-9","article-title":"Purification and characterization of (2R,3R)-2,3-butanediol dehydrogenase of the human pathogen Neisseria gonorrhoeae FA1090 produced in Escherichia coli","volume":"63","author":"Tang","year":"2021","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.pep.2021.105909_bib31","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/0378-1119(89)90358-2","article-title":"Site-directed mutagenesis by overlap extension using the polymerase chain reaction","volume":"77","author":"Ho","year":"1989","journal-title":"Gene"},{"key":"10.1016\/j.pep.2021.105909_bib32","doi-asserted-by":"crossref","first-page":"5915","DOI":"10.3390\/ijms21165915","article-title":"Biochemical characterization and crystal structure of a novel NAD+-dependent isocitrate dehydrogenase from Phaeodactylum tricornutum","volume":"21","author":"Huang","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.pep.2021.105909_bib33","doi-asserted-by":"crossref","first-page":"2011","DOI":"10.1128\/AEM.04007-13","article-title":"Molecular characterization of an NADPH-dependent acetoin reductase\/2,3-butanediol dehydrogenase from Clostridium beijerinckii NCIMB 8052","volume":"80","author":"Raedts","year":"2014","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.pep.2021.105909_bib34","doi-asserted-by":"crossref","first-page":"W296","DOI":"10.1093\/nar\/gky427","article-title":"SWISS-MODEL: homology modelling of protein structures and complexes","volume":"46","author":"Waterhouse","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.pep.2021.105909_bib35","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.pep.2021.105909_bib36","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.pep.2021.105909_bib37","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1016\/S0959-440X(01)00272-X","article-title":"The ACT domain family","volume":"11","author":"Chipman","year":"2001","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.pep.2021.105909_bib38","first-page":"532","article-title":"L-Homoserine fermentation Part VI. Effect of threonine and methionine on L-homoserine in dehydrogenase in Micrococcus glutamicus 534-Co147","volume":"25","author":"Nara","year":"1961","journal-title":"Agric. Biol. Chem."},{"key":"10.1016\/j.pep.2021.105909_bib39","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1021\/sb400133g","article-title":"Rational design of allosteric regulation of homoserine dehydrogenase by a nonnatural inhibitor L-lysine","volume":"4","author":"Chen","year":"2015","journal-title":"ACS Synth. Biol."},{"key":"10.1016\/j.pep.2021.105909_bib40","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nsb0195-69","article-title":"The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase","volume":"2","author":"Schuller","year":"1995","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.pep.2021.105909_bib41","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/S0167-4838(00)00202-8","article-title":"Homoserine dehydrogenase from Saccharomyces cerevisiae: kinetic mechanism and stereochemistry of hydride transfer","volume":"1544","author":"Jacques","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.pep.2021.105909_bib42","doi-asserted-by":"crossref","first-page":"2462","DOI":"10.1096\/fj.14-257014","article-title":"A unique homodimeric NAD+-linked isocitrate dehydrogenase from the smallest autotrophic eukaryote Ostreococcus tauri","volume":"29","author":"Tang","year":"2015","journal-title":"Faseb. J."},{"key":"10.1016\/j.pep.2021.105909_bib43","doi-asserted-by":"crossref","first-page":"11666","DOI":"10.1073\/pnas.92.25.11666","article-title":"A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity","volume":"92","author":"Chen","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.pep.2021.105909_bib44","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1093\/protein\/12.10.851","article-title":"Redesign of the coenzyme specificity in L-lactate dehydrogenase from Bacillus stearothermophilus using site-directed mutagenesis and media engineering","volume":"12","author":"Holmberg","year":"1999","journal-title":"Protein Eng."},{"key":"10.1016\/j.pep.2021.105909_bib45","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1038\/343038a0","article-title":"Redesign of the coenzyme specificity of a dehydrogenase by protein engineering","volume":"343","author":"Scrutton","year":"1990","journal-title":"Nature"}],"container-title":["Protein Expression and Purification"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592821000929?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592821000929?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T01:54:34Z","timestamp":1760925274000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046592821000929"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,10]]},"references-count":45,"alternative-id":["S1046592821000929"],"URL":"https:\/\/doi.org\/10.1016\/j.pep.2021.105909","relation":{},"ISSN":["1046-5928"],"issn-type":[{"value":"1046-5928","type":"print"}],"subject":[],"published":{"date-parts":[[2021,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Biochemical characterization and redesign of the coenzyme specificity of a novel monofunctional NAD+-dependent homoserine dehydrogenase from the human pathogen Neisseria gonorrhoeae","name":"articletitle","label":"Article Title"},{"value":"Protein Expression and Purification","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.pep.2021.105909","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"105909"}}