{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T03:56:18Z","timestamp":1788926178615,"version":"build-2803163510"},"reference-count":46,"publisher":"National Academy of Sciences","issue":"34","license":[{"start":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T00:00:00Z","timestamp":1439164800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.pnas.org\/site\/misc\/userlicense.xhtml"}],"funder":[{"name":"JST","award":["ERATO Asano Active Enzyme Molecule Project"],"award-info":[{"award-number":["ERATO Asano Active Enzyme Molecule Project"]}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2015,8,25]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>Hydroxynitrile lyase (HNL) has been isolated from plants and bacteria and is a valuable tool in the chiral-specific synthesis of cyanohydrins, which are important building blocks of fine chemicals and pharmaceuticals. To discover more efficient and stable HNLs, we focused on the invasive cyanogenic millipede as a bioresource. The HNL identified from the millipede showed not only the highest specific activity toward benzaldehyde among known HNLs, including the almond HNL in industrial use, along with wide temperature and pH stabilities, but also high enantioselectivity in the synthesis of various cyanohydrins. These properties make it suitable as an industrial biocatalyst. Arthropods are likely to be valuable sources of potential biocatalysts for the next generation of industrial biotechnology.<\/jats:p>","DOI":"10.1073\/pnas.1508311112","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T22:30:34Z","timestamp":1439245834000},"page":"10605-10610","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":70,"title":["Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede,\n                    <i>Chamberlinius hualienensis<\/i>"],"prefix":"10.1073","volume":"112","author":[{"given":"Mohammad","family":"Dadashipour","sequence":"first","affiliation":[{"name":"Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan;"},{"name":"Asano Active Enzyme Molecule Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuko","family":"Ishida","sequence":"additional","affiliation":[{"name":"Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan;"},{"name":"Asano Active Enzyme Molecule Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazunori","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan;"},{"name":"Asano Active Enzyme Molecule Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuhisa","family":"Asano","sequence":"additional","affiliation":[{"name":"Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan;"},{"name":"Asano Active Enzyme Molecule Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2015,8,10]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","unstructured":"Y Asano Hydrolysis of nitriles to amides. Science of Synthesis: Biocatalysis in Organic Synthesis eds Faber K Fessner WD Turner N (Georg Thieme Stuttgart) Vol 1 pp 255\u2013276. (2015).","DOI":"10.1055\/sos-SD-214-00188"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"1821","DOI":"10.2307\/3870232","article-title":"Preformed antimicrobial compounds and plant defense against fungal attack","volume":"8","author":"Osbourn AE","year":"1996","unstructured":"AE Osbourn, Preformed antimicrobial compounds and plant defense against fungal attack. Plant Cell 8, 1821\u20131831 (1996).","journal-title":"Plant Cell"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1002\/anie.198704581","article-title":"Enzyme-catalyzed cyanohydrin synthesis in organic solvents","volume":"26","author":"Effenberger F","year":"1987","unstructured":"F Effenberger, T Ziegler, S F\u00f6rster, Enzyme-catalyzed cyanohydrin synthesis in organic solvents. Angew Chem Int Ed Engl 26, 458\u2013460 (1987).","journal-title":"Angew Chem Int Ed Engl"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"13739","DOI":"10.1016\/S0040-4020(01)85686-6","article-title":"Synthetic applications of optically active cyanohydrins. Enantioselective syntheses of the hydroxyamides tembamide and aegeline, the cardiac drug denopamine, and some analogues of the bronchodilator salbutamol","volume":"50","author":"Brown RFC","year":"1994","unstructured":"RFC Brown, AC Donohue, WR Jackson, TD McCarthy, Synthetic applications of optically active cyanohydrins. Enantioselective syntheses of the hydroxyamides tembamide and aegeline, the cardiac drug denopamine, and some analogues of the bronchodilator salbutamol. Tetrahedron 50, 13739\u201313752 (1994).","journal-title":"Tetrahedron"},{"key":"e_1_3_4_5_2","first-page":"677","volume-title":"Biocatalysis in the Pharmaceutical and Biotechnology Industries","author":"Effenberger F","year":"2007","unstructured":"F Effenberger, S F\u00f6rster, C Kobler, State of the art and applications in stereoselective synthesis of chiral cyanohydrins. Biocatalysis in the Pharmaceutical and Biotechnology Industries, ed RN Patel (CRC, New York), pp. 677\u2013698 (2007)."},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"15","DOI":"10.2174\/157017909787314858","article-title":"Enantioselective enzyme-catalysed synthesis of cyanohydrins","volume":"6","author":"Holt J","year":"2009","unstructured":"J Holt, U Hanefeld, Enantioselective enzyme-catalysed synthesis of cyanohydrins. Curr Org Synth 6, 15\u201337 (2009).","journal-title":"Curr Org Synth"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0957-4166(94)00384-N","article-title":"Enzyme catalyzed addition of hydrocyanic acid to substituted pivalaldehydes-A novel synthesis of (R)-pantolactone","volume":"6","author":"Effenberger F","year":"1995","unstructured":"F Effenberger, J Eichhorn, J Roos, Enzyme catalyzed addition of hydrocyanic acid to substituted pivalaldehydes-A novel synthesis of (R)-pantolactone. Tetrahedron Asymmetry 6, 271\u2013282 (1995).","journal-title":"Tetrahedron Asymmetry"},{"key":"e_1_3_4_8_2","first-page":"238","article-title":"Durch enzyme bewirkte asymmetrische synthesen","volume":"14","author":"Rosenthaler L","year":"1908","unstructured":"L Rosenthaler, Durch enzyme bewirkte asymmetrische synthesen. Biochem Z 14, 238\u2013253 (1908).","journal-title":"Biochem Z"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","unstructured":"J Brussee A van der Gen Biocatalysis in the enantioselective formation of chiral cyanohydrins valuable building blocks in organic synthesis. Stereoselective Biocatalysis ed Patel RN (CRC Boca Raton FL) pp 289\u2013319. (2000).","DOI":"10.1201\/9781420027242.ch11"},{"key":"e_1_3_4_10_2","first-page":"287","article-title":"Hydroxynitrile lyases: Biological sources and application as biocatalysts","volume":"42","author":"Fechter MH","year":"2004","unstructured":"MH Fechter, H Griengl, Hydroxynitrile lyases: Biological sources and application as biocatalysts. Food Technol Biotechnol 42, 287\u2013294 (2004).","journal-title":"Food Technol Biotechnol"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.csbj.2014.07.002","article-title":"Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum","volume":"10","author":"Wiedner R","year":"2014","unstructured":"R Wiedner, M Gruber-Khadjawi, H Schwab, K Steiner, Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum. Comput Struct Biotechnol J 10, 58\u201362 (2014).","journal-title":"Comput Struct Biotechnol J"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1271\/bbb.69.2349","article-title":"Screening for new hydroxynitrilases from plants","volume":"69","author":"Asano Y","year":"2005","unstructured":"Y Asano, , Screening for new hydroxynitrilases from plants. Biosci Biotechnol Biochem 69, 2349\u20132357 (2005).","journal-title":"Biosci Biotechnol Biochem"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"4815","DOI":"10.1002\/anie.200352141","article-title":"Comprehensive step-by-step engineering of an (R)-hydroxynitrile lyase for large-scale asymmetric synthesis","volume":"42","author":"Glieder A","year":"2003","unstructured":"A Glieder, , Comprehensive step-by-step engineering of an (R)-hydroxynitrile lyase for large-scale asymmetric synthesis. Angew Chem Int Ed Engl 42, 4815\u20134818 (2003).","journal-title":"Angew Chem Int Ed Engl"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1021\/cs200325q","article-title":"Hydroxynitrile lyases: Insights into biochemistry, discovery, and engineering","volume":"1","author":"Dadashipour M","year":"2011","unstructured":"M Dadashipour, Y Asano, Hydroxynitrile lyases: Insights into biochemistry, discovery, and engineering. ACS Catal 1, 1121\u20131149 (2011).","journal-title":"ACS Catal"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"6308","DOI":"10.1039\/c3cs35491a","article-title":"Immobilisation of hydroxynitrile lyases","volume":"42","author":"Hanefeld U","year":"2013","unstructured":"U Hanefeld, Immobilisation of hydroxynitrile lyases. Chem Soc Rev 42, 6308\u20136321 (2013).","journal-title":"Chem Soc Rev"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3897\/zookeys.98.1183","article-title":"Revision of the Taiwanese millipede genus Chamberlinius Wang, 1956, with descriptions of two new species and a reclassification of the tribe Chamberlinini (Diplopoda, Polydesmida, Paradoxosomatidae, Paradoxosomatinae)","volume":"98","author":"Chen C-C","year":"2011","unstructured":"C-C Chen, SI Golovatch, H-W Chang, S-H Chen, Revision of the Taiwanese millipede genus Chamberlinius Wang, 1956, with descriptions of two new species and a reclassification of the tribe Chamberlinini (Diplopoda, Polydesmida, Paradoxosomatidae, Paradoxosomatinae). ZooKeys 98, 1\u201327 (2011).","journal-title":"ZooKeys"},{"key":"e_1_3_4_17_2","first-page":"47","article-title":"Obstruction of trains by the outbreaks of a millipede Chamberlinius hualienensis WANG (Diplopoda: Polydesmida)","volume":"69","author":"Niijima K","year":"2002","unstructured":"K Niijima, T Arimura, Obstruction of trains by the outbreaks of a millipede Chamberlinius hualienensis WANG (Diplopoda: Polydesmida). Edaphologia 69, 47\u201349 (2002).","journal-title":"Edaphologia"},{"key":"e_1_3_4_18_2","first-page":"208","article-title":"Identification of mandelonitrile as a major secretory compound from Chamberlinius hualienensis Wang (Polydesmida: Paradoxosomatidae)","volume":"8","author":"Noguchi S","year":"1997","unstructured":"S Noguchi, N Mori, Y Higa, Y Kuwahara, Identification of mandelonitrile as a major secretory compound from Chamberlinius hualienensis Wang (Polydesmida: Paradoxosomatidae). Jpn J Environ Entomol Zool 8, 208\u2013214 (1997).","journal-title":"Jpn J Environ Entomol Zool"},{"key":"e_1_3_4_19_2","volume-title":"Chemical Defenses of Arthropods","author":"Blum MS","year":"1981","unstructured":"MS Blum Chemical Defenses of Arthropods (Academic, New York, 1981)."},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1126\/science.153.3742.1341","article-title":"Defensive secretions of arthropods","volume":"153","author":"Eisner T","year":"1966","unstructured":"T Eisner, J Meinwald, Defensive secretions of arthropods. Science 153, 1341\u20131350 (1966).","journal-title":"Science"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1271\/bbb.80023","article-title":"Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat)","volume":"72","author":"Ueatrongchit T","year":"2008","unstructured":"T Ueatrongchit, A Kayo, H Komeda, Y Asano, A H-Kittikun, Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat). Biosci Biotechnol Biochem 72, 1513\u20131522 (2008).","journal-title":"Biosci Biotechnol Biochem"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1016\/j.enzmictec.2010.02.008","article-title":"Hydroxynitrile lyase from Passiflora edulis: Purification, characteristics and application in asymmetric synthesis of (R)-mandelonitrile","volume":"46","author":"Ueatrongchit T","year":"2010","unstructured":"T Ueatrongchit, K Tamura, T Ohmiya, A H-Kittikun, Y Asano, Hydroxynitrile lyase from Passiflora edulis: Purification, characteristics and application in asymmetric synthesis of (R)-mandelonitrile. Enzyme Microb Technol 46, 456\u2013465 (2010).","journal-title":"Enzyme Microb Technol"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1271\/bbb.100187","article-title":"Characterization of a new (R)-hydroxynitrile lyase from the Japanese apricot Prunus mume and cDNA cloning and secretory expression of one of the isozymes in Pichia pastoris","volume":"75","author":"Fukuta Y","year":"2011","unstructured":"Y Fukuta, , Characterization of a new (R)-hydroxynitrile lyase from the Japanese apricot Prunus mume and cDNA cloning and secretory expression of one of the isozymes in Pichia pastoris. Biosci Biotechnol Biochem 75, 214\u2013220 (2011).","journal-title":"Biosci Biotechnol Biochem"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1104\/pp.109.4.1231","article-title":"Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum","volume":"109","author":"Wajant H","year":"1995","unstructured":"H Wajant, S F\u00f6rster, D Selmar, F Effenberger, K Pfizenmaier, Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum. Plant Physiol 109, 1231\u20131238 (1995).","journal-title":"Plant Physiol"},{"key":"e_1_3_4_25_2","first-page":"90","article-title":"Purification and protein characterization of hydroxynitrile lyases from Sorghum and Almond","volume":"15","author":"Jansen I","year":"1992","unstructured":"I Jansen, R Woker, MR Kula, Purification and protein characterization of hydroxynitrile lyases from Sorghum and Almond. Biotechnol Appl Biochem 15, 90\u201399 (1992).","journal-title":"Biotechnol Appl Biochem"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"10908","DOI":"10.1016\/j.tet.2005.08.105","article-title":"A new (R)-hydroxynitrile lyase from Prunus mume: Asymmetric synthesis of cyanohydrins","volume":"61","author":"Nanda S","year":"2005","unstructured":"S Nanda, Y Kato, Y Asano, A new (R)-hydroxynitrile lyase from Prunus mume: Asymmetric synthesis of cyanohydrins. Tetrahedron 61, 10908\u201310916 (2005).","journal-title":"Tetrahedron"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.jbiotec.2011.02.004","article-title":"S-selective hydroxynitrile lyase from a plant Baliospermum montanum: molecular characterization of recombinant enzyme","volume":"153","author":"Dadashipour M","year":"2011","unstructured":"M Dadashipour, , S-selective hydroxynitrile lyase from a plant Baliospermum montanum: molecular characterization of recombinant enzyme. J Biotechnol 153, 100\u2013110 (2011).","journal-title":"J Biotechnol"},{"key":"e_1_3_4_28_2","first-page":"30","volume-title":"Green Chemistry: Theory and Practice","author":"Anastas PT","year":"1998","unstructured":"PT Anastas, JC Warner Green Chemistry: Theory and Practice (Oxford Univ Press, New York), pp. 30 (1998)."},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"1370","DOI":"10.1002\/chem.19970030825","article-title":"Stereoselective synthesis of (S)-3,4-methylenedioxyamphetamines from (R)-cyanohydrins","volume":"3","author":"Effenberger F","year":"1997","unstructured":"F Effenberger, J J\u04d3ger, Stereoselective synthesis of (S)-3,4-methylenedioxyamphetamines from (R)-cyanohydrins. Chemistry 3, 1370\u20131374 (1997).","journal-title":"Chemistry"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"3028","DOI":"10.1128\/aem.57.10.3028-3032.1991","article-title":"Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750","volume":"57","author":"Yamamoto K","year":"1991","unstructured":"K Yamamoto, K Oishi, I Fujimatsu, K Komatsu, Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl Environ Microbiol 57, 3028\u20133032 (1991).","journal-title":"Appl Environ Microbiol"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"7548","DOI":"10.1021\/jo901548t","article-title":"Enantioselective chemoenzymatic synthesis of trans-aziridines","volume":"74","author":"Ritzen B","year":"2009","unstructured":"B Ritzen, MCM van Oers, FL van Delft, FPJT Rutjes, Enantioselective chemoenzymatic synthesis of trans-aziridines. J Org Chem 74, 7548\u20137551 (2009).","journal-title":"J Org Chem"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/S0969-2126(01)00639-6","article-title":"The hydroxynitrile lyase from almond: A lyase that looks like an oxidoreductase","volume":"9","author":"Dreveny I","year":"2001","unstructured":"I Dreveny, K Gruber, A Glieder, A Thompson, C Kratky, The hydroxynitrile lyase from almond: A lyase that looks like an oxidoreductase. Structure 9, 803\u2013815 (2001).","journal-title":"Structure"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1006\/abbi.1994.1267","article-title":"Purification, characterization, and cloning of alpha-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)","volume":"311","author":"Hughes J","year":"1994","unstructured":"J Hughes, FJ Carvalho, MA Hughes, Purification, characterization, and cloning of alpha-hydroxynitrile lyase from cassava (Manihot esculenta Crantz). Arch Biochem Biophys 311, 496\u2013502 (1994).","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1016\/j.cell.2010.11.042","article-title":"Essential role of coiled coils for aggregation and activity of Q\/N-rich prions and PolyQ proteins","volume":"143","author":"Fiumara F","year":"2010","unstructured":"F Fiumara, L Fioriti, ER Kandel, WA Hendrickson, Essential role of coiled coils for aggregation and activity of Q\/N-rich prions and PolyQ proteins. Cell 143, 1121\u20131135 (2010).","journal-title":"Cell"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","unstructured":"C Perez-Iratxeta MA Andrade-Navarro K2D2: Estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8:25. (2008).","DOI":"10.1186\/1472-6807-8-25"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"W668-73","DOI":"10.1093\/nar\/gkh371","article-title":"DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data","volume":"32","author":"Whitmore L","year":"2004","unstructured":"L Whitmore, BA Wallace, DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32, W668-73 (2004).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1111\/j.1095-8312.2000.tb01279.x","article-title":"How many species of arthropods? Erwin\u2019s estimate revised","volume":"71","author":"Odegaard F","year":"2000","unstructured":"F Odegaard, How many species of arthropods? Erwin\u2019s estimate revised. Biol J Linn Soc Lond 71, 583\u2013597 (2000).","journal-title":"Biol J Linn Soc Lond"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/s00253-007-1025-6","article-title":"Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry","volume":"76","author":"Purkarthofer T","year":"2007","unstructured":"T Purkarthofer, W Skranc, C Schuster, H Griengl, Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry. Appl Microbiol Biotechnol 76, 309\u2013320 (2007).","journal-title":"Appl Microbiol Biotechnol"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/S0167-4838(99)00108-9","article-title":"Study of the (S)-hydroxynitrile lyase from Hevea brasiliensis: Mechanistic implications","volume":"1432","author":"Hanefeld U","year":"1999","unstructured":"U Hanefeld, AJJ Straathof, JJ Heijnen, Study of the (S)-hydroxynitrile lyase from Hevea brasiliensis: Mechanistic implications. Biochim Biophys Acta 1432, 185\u2013193 (1999).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"W5-9","DOI":"10.1093\/nar\/gkn201","article-title":"NCBI BLAST: A better web interface","volume":"36","author":"Johnson M","year":"2008","unstructured":"M Johnson, , NCBI BLAST: A better web interface. Nucleic Acids Res 36, W5-9 (2008).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1038\/emboj.2013.79","article-title":"Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology","volume":"32","author":"Steentoft C","year":"2013","unstructured":"C Steentoft, , Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. EMBO J 32, 1478\u20131488 (2013).","journal-title":"EMBO J"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"W197-201","DOI":"10.1093\/nar\/gkn238","article-title":"The Jpred 3 secondary structure prediction server","volume":"36","author":"Cole C","year":"2008","unstructured":"C Cole, JD Barber, GJ Barton, The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36, W197-201 (2008).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"44","DOI":"10.2144\/05381BM04","article-title":"Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris","volume":"38","author":"Lin-Cereghino J","year":"2005","unstructured":"J Lin-Cereghino, , Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris. Biotechniques 38, 44\u201348, 46, 48 (2005).","journal-title":"Biotechniques"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"1775","DOI":"10.1016\/S0965-1748(02)00136-4","article-title":"Cloning of putative odorant-degrading enzyme and integumental esterase cDNAs from the wild silkmoth, Antheraea polyphemus","volume":"32","author":"Ishida Y","year":"2002","unstructured":"Y Ishida, WS Leal, Cloning of putative odorant-degrading enzyme and integumental esterase cDNAs from the wild silkmoth, Antheraea polyphemus. Insect Biochem Mol Biol 32, 1775\u20131780 (2002).","journal-title":"Insect Biochem Mol Biol"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"3847","DOI":"10.1073\/pnas.1323928111","article-title":"Niemann-Pick type C2 protein mediating chemical communication in the worker ant","volume":"111","author":"Ishida Y","year":"2014","unstructured":"Y Ishida, , Niemann-Pick type C2 protein mediating chemical communication in the worker ant. Proc Natl Acad Sci USA 111, 3847\u20133852 (2014).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_46_2","first-page":"101","volume-title":"Stereochemistry of Organic Compounds","author":"Eliel EL","year":"1994","unstructured":"EL Eliel, SH Wilen, LN Mander Stereochemistry of Organic Compounds (Wiley, New York), pp. 101\u2013152 (1994)."}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1508311112","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1508311112","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,8,12]],"date-time":"2023-08-12T21:53:40Z","timestamp":1691877220000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1508311112"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,8,10]]},"references-count":46,"journal-issue":{"issue":"34","published-print":{"date-parts":[[2015,8,25]]}},"alternative-id":["10.1073\/pnas.1508311112"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1508311112","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,8,10]]},"assertion":[{"value":"2015-08-10","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}