{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T17:13:42Z","timestamp":1790702022802,"version":"4.1.0"},"reference-count":57,"publisher":"Elsevier BV","issue":"36","license":[{"start":{"date-parts":[[2014,9,1]],"date-time":"2014-09-01T00:00:00Z","timestamp":1409529600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":2197,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2014,9]]},"DOI":"10.1074\/jbc.m114.597682","type":"journal-article","created":{"date-parts":[[2014,7,19]],"date-time":"2014-07-19T00:27:39Z","timestamp":1405729659000},"page":"25149-25165","source":"Crossref","is-referenced-by-count":34,"title":["High Throughput Screen Identifies Small Molecule Inhibitors Specific for Mycobacterium tuberculosis Phosphoserine Phosphatase"],"prefix":"10.1016","volume":"289","author":[{"given":"Garima","family":"Arora","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prabhakar","family":"Tiwari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rahul Shubhra","family":"Mandal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arpit","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deepak","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sudipto","family":"Saha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ramandeep","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M114.597682_bib1","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1126\/science.1185449","article-title":"The population dynamics and control of tuberculosis","volume":"328","author":"Dye","year":"2010","journal-title":"Science"},{"key":"10.1074\/jbc.M114.597682_bib2","doi-asserted-by":"crossref","first-page":"208","DOI":"10.3389\/fmicb.2013.00208","article-title":"Resistance in tuberculosis: what do we know and where can we go?","volume":"4","author":"Green","year":"2013","journal-title":"Front. Microbiol"},{"key":"10.1074\/jbc.M114.597682_bib3","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/nature09657","article-title":"The challenge of new drug discovery for tuberculosis","volume":"469","author":"Koul","year":"2011","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.597682_bib4","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/31159","article-title":"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence","volume":"393","author":"Cole","year":"1998","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.597682_bib5","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.chembiol.2011.12.016","article-title":"Cholesterol catabolism by Mycobacterium tuberculosis requires transcriptional and metabolic adaptations","volume":"19","author":"Griffin","year":"2012","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.M114.597682_bib6","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1046\/j.1365-2958.2003.03425.x","article-title":"Genes required for mycobacterial growth defined by high density mutagenesis","volume":"48","author":"Sassetti","year":"2003","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M114.597682_bib7","doi-asserted-by":"crossref","first-page":"12989","DOI":"10.1073\/pnas.2134250100","article-title":"Genetic requirements for mycobacterial survival during infection","volume":"100","author":"Sassetti","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.597682_bib8","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1128\/JB.01269-06","article-title":"Biosynthesis of phosphoserine in the Methanococcales","volume":"189","author":"Helgad\u00f3ttir","year":"2007","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M114.597682_bib9","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/0065-2571(84)90021-9","article-title":"Enzymes of serine metabolism in normal, developing and neoplastic rat tissues","volume":"22","author":"Snell","year":"1984","journal-title":"Adv. Enzyme Regul"},{"key":"10.1074\/jbc.M114.597682_bib10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/jb.163.1.1-7.1985","article-title":"Serine hydroxymethyltransferase from Escherichia coli: purification and properties","volume":"163","author":"Schirch","year":"1985","journal-title":"J Bacteriol"},{"key":"10.1074\/jbc.M114.597682_bib11","doi-asserted-by":"crossref","first-page":"11007","DOI":"10.1074\/jbc.274.16.11007","article-title":"Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana","volume":"274","author":"Ho","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib12","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1107\/S0907444912004829","article-title":"Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis","volume":"68","author":"Coulibaly","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.597682_bib13","doi-asserted-by":"crossref","first-page":"14892","DOI":"10.1074\/jbc.M414489200","article-title":"Crystal structure of Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits","volume":"280","author":"Dey","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib14","doi-asserted-by":"crossref","first-page":"14884","DOI":"10.1074\/jbc.M414488200","article-title":"d-3-Phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymes","volume":"280","author":"Dey","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib15","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1111\/j.1365-2958.2011.07806.x","article-title":"Dysregulation of serine biosynthesis contributes to the growth defect of a Mycobacterium tuberculosis crp mutant","volume":"82","author":"Bai","year":"2011","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M114.597682_bib16","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1111\/j.1742-4658.2012.08633.x","article-title":"Human HAD phosphatases: structure, mechanism, and roles in health and disease","volume":"280","author":"Seifried","year":"2013","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M114.597682_bib17","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1006\/jmbi.1994.1711","article-title":"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity: application of an iterative approach to database search","volume":"244","author":"Koonin","year":"1994","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M114.597682_bib18","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0969-2126(00)00558-X","article-title":"Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution","volume":"9","author":"Wang","year":"2001","journal-title":"Structure"},{"key":"10.1074\/jbc.M114.597682_bib19","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/j.jmb.2006.06.049","article-title":"Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes","volume":"361","author":"Burroughs","year":"2006","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M114.597682_bib20","doi-asserted-by":"crossref","first-page":"8525","DOI":"10.1073\/pnas.131213698","article-title":"BeF3\u2212 acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF3\u2212 complex with phosphoserine phosphatase","volume":"98","author":"Cho","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.597682_bib21","doi-asserted-by":"crossref","first-page":"46651","DOI":"10.1074\/jbc.M204866200","article-title":"Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase","volume":"277","author":"Kim","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib22","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1107\/S0907444903005407","article-title":"High-resolution structure of human phosphoserine phosphatase in open conformation","volume":"59","author":"Peeraer","year":"2003","journal-title":"Acta Crystallogr. D. Biol. Crystallogr"},{"key":"10.1074\/jbc.M114.597682_bib23","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/250194a0","article-title":"Chemical and biological evolution of nucleotide-binding protein","volume":"250","author":"Rossmann","year":"1974","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.597682_bib24","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1111\/j.1462-5822.2011.01743.x","article-title":"Porphyromonas gingivalis SerB-mediated dephosphorylation of host cell cofilin modulates invasion efficiency","volume":"14","author":"Moffatt","year":"2012","journal-title":"Cell. Microbiol"},{"key":"10.1074\/jbc.M114.597682_bib25","doi-asserted-by":"crossref","first-page":"e1003326","DOI":"10.1371\/journal.ppat.1003326","article-title":"The serine phosphatase SerB of Porphyromonas gingivalis suppresses IL-8 production by dephosphorylation of NF-\u03baB RelA\/p65","volume":"9","author":"Takeuchi","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M114.597682_bib26","doi-asserted-by":"crossref","first-page":"11027","DOI":"10.1073\/pnas.0509813103","article-title":"A Porphyromonas gingivalis haloacid dehalogenase family phosphatase interacts with human phosphoproteins and is important for invasion","volume":"103","author":"Tribble","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M114.597682_bib27","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol"},{"key":"10.1074\/jbc.M114.597682_bib28","first-page":"406","article-title":"The neighbor-joining method: a new method for reconstructing phylogenetic trees","volume":"4","author":"Saitou","year":"1987","journal-title":"Mol. Biol. Evol"},{"key":"10.1074\/jbc.M114.597682_bib29","doi-asserted-by":"crossref","first-page":"2731","DOI":"10.1093\/molbev\/msr121","article-title":"MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods","volume":"28","author":"Tamura","year":"2011","journal-title":"Mol. Biol. Evol"},{"key":"10.1074\/jbc.M114.597682_bib30","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1002\/pro.5560020916","article-title":"Verification of protein structures: patterns of nonbonded atomic interactions","volume":"2","author":"Colovos","year":"1993","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M114.597682_bib31","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1093\/nar\/29.1.221","article-title":"PDBsum: summaries and analyses of PDB structures","volume":"29","author":"Laskowski","year":"2001","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M114.597682_bib32","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/356083a0","article-title":"Assessment of protein models with three-dimensional profiles","volume":"356","author":"L\u00fcthy","year":"1992","journal-title":"Nature"},{"key":"10.1074\/jbc.M114.597682_bib33","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/S0014-2999(97)01304-6","article-title":"Novel phosphoserine phosphatase inhibitors","volume":"337","author":"Hawkinson","year":"1997","journal-title":"Eur. J. Pharmacol"},{"key":"10.1074\/jbc.M114.597682_bib34","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/0014-2999(96)00253-1","article-title":"The metabotropic glutamate receptor antagonist l-2-amino-3-phosphonopropionic acid inhibits phosphoserine phosphatase","volume":"307","author":"Hawkinson","year":"1996","journal-title":"Eur. J. Pharmacol"},{"key":"10.1074\/jbc.M114.597682_bib35","doi-asserted-by":"crossref","first-page":"6177","DOI":"10.1021\/jm051256o","article-title":"Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes","volume":"49","author":"Friesner","year":"2006","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.M114.597682_bib36","doi-asserted-by":"crossref","first-page":"11934","DOI":"10.1074\/jbc.M111.330621","article-title":"Discovery and analysis of cofactor-dependent phosphoglycerate mutase homologs as novel phosphoserine phosphatases in Hydrogenobacter thermophilus","volume":"287","author":"Chiba","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib37","doi-asserted-by":"crossref","first-page":"13166","DOI":"10.1074\/jbc.M311393200","article-title":"The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity","volume":"279","author":"Singh","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib38","doi-asserted-by":"crossref","first-page":"1982","DOI":"10.1128\/AAC.01235-07","article-title":"Biological activities of novel gyrase inhibitors of the aminocoumarin class","volume":"52","author":"Anderle","year":"2008","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.M114.597682_bib39","doi-asserted-by":"crossref","first-page":"37181","DOI":"10.1074\/jbc.M003701200","article-title":"The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone","volume":"275","author":"Marcu","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M114.597682_bib40","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1099\/mic.0.054064-0","article-title":"Alanine racemase mutants of Mycobacterium tuberculosis require d-alanine for growth and are defective for survival in macrophages and mice","volume":"158","author":"Awasthy","year":"2012","journal-title":"Microbiology"},{"key":"10.1074\/jbc.M114.597682_bib41","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1128\/IAI.68.5.2888-2898.2000","article-title":"Attenuation of and protection induced by a leucine auxotroph of Mycobacterium tuberculosis","volume":"68","author":"Hondalus","year":"2000","journal-title":"Infect Immun"},{"key":"10.1074\/jbc.M114.597682_bib42","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1128\/IAI.69.2.1442-1150.2001","article-title":"Characterization of auxotrophic mutants of Mycobacterium tuberculosis and their potential as vaccine candidates","volume":"69","author":"Smith","year":"2001","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M114.597682_bib43","doi-asserted-by":"crossref","first-page":"e20374","DOI":"10.1371\/journal.pone.0020374","article-title":"New classes of alanine racemase inhibitors identified by high-throughput screening show antimicrobial activity against Mycobacterium tuberculosis","volume":"6","author":"Anthony","year":"2011","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M114.597682_bib44","doi-asserted-by":"crossref","first-page":"5295","DOI":"10.1021\/jm400395p","article-title":"Identification, biochemical and structural evaluation of species-specific inhibitors against type I methionine aminopeptidases","volume":"56","author":"Kishor","year":"2013","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.M114.597682_bib45","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.bcp.2013.05.004","article-title":"Inhibition of mycobacterial alanine racemase activity and growth by thiadiazolidinones","volume":"86","author":"Lee","year":"2013","journal-title":"Biochem. Pharmacol"},{"key":"10.1074\/jbc.M114.597682_bib46","doi-asserted-by":"crossref","first-page":"6457","DOI":"10.1021\/jm400710k","article-title":"Structure-guided design of novel thiazolidine inhibitors of O-acetyl serine sulfhydrylase from Mycobacterium tuberculosis","volume":"56","author":"Poyraz","year":"2013","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.M114.597682_bib47","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1111\/j.1742-4658.2008.06763.x","article-title":"A novel inhibitor of indole-3-glycerol phosphate synthase with activity against multidrug-resistant Mycobacterium tuberculosis","volume":"276","author":"Shen","year":"2009","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M114.597682_bib48","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1021\/ci3004545","article-title":"Discovery of novel acetohydroxyacid synthase inhibitors as active agents against Mycobacterium tuberculosis by virtual screening and bioassay","volume":"53","author":"Wang","year":"2013","journal-title":"J. Chem. Inf. Model"},{"key":"10.1074\/jbc.M114.597682_bib49","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.plipres.2008.01.003","article-title":"Roles of l-serine and sphingolipid synthesis in brain development and neuronal survival","volume":"47","author":"Hirabayashi","year":"2008","journal-title":"Prog. Lipid Res"},{"key":"10.1074\/jbc.M114.597682_bib50","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1128\/JB.182.1.143-145.2000","article-title":"Cysteine biosynthesis pathway in the archaeon Methanosarcina barkeri encoded by acquired bacterial genes?","volume":"182","author":"Kitabatake","year":"2000","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M114.597682_bib51","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1128\/jb.121.1.239-249.1975","article-title":"Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes","volume":"121","author":"Largen","year":"1975","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M114.597682_bib52","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1128\/jb.89.4.1145-1150.1965","article-title":"Glycine synthesis and metabolism in Escherichia coli","volume":"89","author":"Pizer","year":"1965","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M114.597682_bib53","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1023\/A:1007586314648","article-title":"d-Amino acids as putative neurotransmitters: focus on d-serine","volume":"25","author":"Snyder","year":"2000","journal-title":"Neurochem. Res"},{"key":"10.1074\/jbc.M114.597682_bib54","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1128\/jb.109.1.34-43.1972","article-title":"Genetic and physiological control of serine and glycine biosynthesis in Saccharomyces","volume":"109","author":"Ulane","year":"1972","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M114.597682_bib55","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1016\/j.bmcl.2012.01.011","article-title":"Identification of 3-acyl-2-phenylamino-1,4-dihydroquinolin-4-one derivatives as inhibitors of the phosphatase SerB653 in Porphyromonas gingivalis, implicated in periodontitis","volume":"22","author":"Jung","year":"2012","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1074\/jbc.M114.597682_bib56","doi-asserted-by":"crossref","first-page":"5025","DOI":"10.1021\/jm100456a","article-title":"Computer-aided identification of Trypanosoma brucei uridine diphosphate galactose 4\u2032-epimerase inhibitors: toward the development of novel therapies for African sleeping sickness","volume":"53","author":"Durrant","year":"2010","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.M114.597682_bib57","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/nature10350","article-title":"Functional genomics reveal that the serine synthesis pathway is essential in breast cancer","volume":"476","author":"Possemato","year":"2011","journal-title":"Nature"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820316665?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820316665?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M114.597682","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T04:34:33Z","timestamp":1641270873000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820316665"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,9]]},"references-count":57,"journal-issue":{"issue":"36","published-print":{"date-parts":[[2014,9]]}},"alternative-id":["S0021925820316665"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m114.597682","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2014,9]]}}}