{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T11:31:50Z","timestamp":1774265510564,"version":"3.50.1"},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,7,1]],"date-time":"2019-07-01T00:00:00Z","timestamp":1561939200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,7,1]],"date-time":"2019-07-01T00:00:00Z","timestamp":1561939200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100004731","name":"Natural Science Foundation of Zhejiang Province","doi-asserted-by":"publisher","award":["LY15B060011"],"award-info":[{"award-number":["LY15B060011"]}],"id":[{"id":"10.13039\/501100004731","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004731","name":"Natural Science Foundation of Zhejiang Province","doi-asserted-by":"publisher","award":["LQ12B06007"],"award-info":[{"award-number":["LQ12B06007"]}],"id":[{"id":"10.13039\/501100004731","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002858","name":"China Postdoctoral Science Foundation","doi-asserted-by":"publisher","award":["2016M601966"],"award-info":[{"award-number":["2016M601966"]}],"id":[{"id":"10.13039\/501100002858","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21406201"],"award-info":[{"award-number":["21406201"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21206024"],"award-info":[{"award-number":["21206024"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Hangzhou Science and Technology","award":["20130533B17"],"award-info":[{"award-number":["20130533B17"]}]},{"name":"Hangzhou Science and Technology","award":["20151232I34"],"award-info":[{"award-number":["20151232I34"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Enzyme and Microbial Technology"],"published-print":{"date-parts":[[2019,7]]},"DOI":"10.1016\/j.enzmictec.2019.04.001","type":"journal-article","created":{"date-parts":[[2019,4,2]],"date-time":"2019-04-02T11:20:13Z","timestamp":1554204013000},"page":"77-85","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"special_numbering":"C","title":["Recombinant expression and molecular insights into the catalytic mechanism of an NADPH-dependent conjugated polyketone reductase for the asymmetric synthesis of (R)-pantolactone"],"prefix":"10.1016","volume":"126","author":[{"given":"Pengfei","family":"Cheng","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jiapao","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yifeng","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinpeng","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1953-4323","authenticated-orcid":false,"given":"Xiaolin","family":"Pei","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Weike","family":"Su","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.enzmictec.2019.04.001_bib0005","first-page":"559","article-title":"Vitamins, 8. Pantothenic acid","volume":"A27","author":"Kaiser","year":"1996"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0010","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.2174\/1385272043369944","article-title":"Synthesis and applications of (R)- and (S)-pantolactone as chiral auxiliaries","volume":"8","author":"Camps","year":"2004","journal-title":"Curr. Org. Chem."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0015","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1021\/ie050774u","article-title":"Calcium Pantothenate. Part 1. (R,S)-Pantolactone technology improvement at the tonnage scale","volume":"45","author":"Rowicki","year":"2006","journal-title":"Ind. Eng. Chem. Res."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0020","series-title":"Analysis of the Development Status and Prospects of China Calcium Pantothenate API Industry in 2018","author":"Gao","year":"2018"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0025","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.apcata.2004.08.028","article-title":"Catalytic processes in vitamins synthesis and production","volume":"280","author":"Bonrath","year":"2005","journal-title":"Appl. Catal. A Gen."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0030","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/0141-0229(95)00250-2","article-title":"Optical resolution of racemic pantoic acid through microbial stereoselective lactonization in an organic solvent\/water two-phase system","volume":"19","author":"Kataoka","year":"1996","journal-title":"Enzym. Microb. Tech."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0035","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1007\/BF00169925","article-title":"Lactonohydrolase-catalyzed optical resolution of pantoyl lactone: selection of a potent enzyme producer and optimization of culture and reaction conditions for practical resolution","volume":"44","author":"Kataoka","year":"1995","journal-title":"Appl. Microbiol. Biot."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0040","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1007\/BF00166911","article-title":"Optical resolution of racemic pantolactone with a novel fungal enzyme, lactonohydrolase","volume":"43","author":"Kataoka","year":"1995","journal-title":"Appl. Microbiol. Biot."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0045","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1111\/j.1432-1033.1992.tb16698.x","article-title":"Purification and characterization of a novel FMN-dependent enzyme. Membrane-bound L-(+)-pantoyl lactone dehydrogenase from Nocardia asteroides","volume":"204","author":"Kataoka","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0050","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.jbiotec.2005.03.015","article-title":"Practical resolution system for DL-pantoyl lactone using the lactonase from Fusarium oxysporum","volume":"118","author":"Sakamoto","year":"2005","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0055","first-page":"289","article-title":"Novel chemoenzymatic syntesis of D(-)-pantoyl lactone","volume":"51","author":"Shimizu","year":"1987","journal-title":"Agric. Biol. Chem."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0060","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1016\/S0957-4166(00)00130-0","article-title":"Enzymatic kinetic resolution of pantolactone: relevance to chiral auxiliary chemistry","volume":"11","author":"Haughton","year":"2000","journal-title":"Tetrahedron Asymmetr."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0065","series-title":"L-pantolactone-hydrolase And a Method for Producing d-pantolactone","author":"Maria","year":"2001"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0070","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","year":"1995","journal-title":"Tetrahedron Asymmetr."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0075","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0304-4165(89)80031-5","article-title":"Ketopantoyl-lactone reductase from Candida parapsilosis: purification and characterization as a conjugated polyketone reductase","volume":"990","author":"Hata","year":"1989","journal-title":"Biochimica Et Biophysica Acta"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0080","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1271\/bbb.65.2785","article-title":"Isolation and primary structural analysis of two conjugated polyketone reductases from Candida parapsilosis","volume":"65","author":"Hidalgo","year":"2001","journal-title":"Biosci. Biotech. Biochem."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0085","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/s00253-003-1484-3","article-title":"Gene cloning and overexpression of two conjugated polyketone reductases, novel aldo-keto reductase family enzymes of Candida parapsilosis","volume":"64","author":"Kataoka","year":"2004","journal-title":"Appl. Microbiol. Biot."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0090","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1007\/s10529-017-2415-1","article-title":"Asymmetric reduction of ketopantolactone using a strictly (R)-stereoselective carbonyl reductase through efficient NADPH regeneration and the substrate constant-feeding strategy","volume":"39","author":"Zhao","year":"2017","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0095","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1038\/nprot.2012.045","article-title":"Site-specific chemical protein conjugation using genetically encoded aldehyde tags","volume":"7","author":"Rabuka","year":"2012","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0100","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1007\/s10529-013-1215-5","article-title":"Addition of Co2+ to culture medium decides the functional expression of a recombinant nitrile hydratase in Escherichia coli","volume":"35","author":"Pei","year":"2013","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0105","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0110","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.1016\/j.biortech.2010.07.114","article-title":"Purification and characterization of glutaminase-free l-asparaginase from Pectobacterium carotovorum MTCC 1428","volume":"102","author":"Kumar","year":"2011","journal-title":"Bioresource. Technol."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0115","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1002\/bit.24371","article-title":"Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge","volume":"109","author":"Le","year":"2012","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0120","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0125","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1007\/s13738-014-0465-z","article-title":"Analytical evaluation of steviol glycosides by capillary electrophoresis supported with molecular docking studies","volume":"12","author":"Ayyappa","year":"2015","journal-title":"J. Iran. Chem. Soc."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0130","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.cbi.2014.09.024","article-title":"The aldo-keto reductases (AKRs): overview","volume":"234","author":"Penning","year":"2015","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0135","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s00253-013-5073-9","article-title":"Structure of conjugated polyketone reductase from Candida parapsilosis IFP0708 reveals conformational changes for substrate recognition upon NADPH binding","volume":"98","author":"Qin","year":"2014","journal-title":"Appl. Microbiol. Biot."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0140","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.abb.2006.07.005","article-title":"A new member of the aldo-keto reductase family from the plant pathogen Xylella fastidiosa","volume":"453","author":"Rosselli","year":"2006","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0145","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1016\/S0957-4166(03)00526-3","article-title":"Recent developments in asymmetric reduction of ketones with biocatalysts","volume":"14","author":"Nakamura","year":"2003","journal-title":"Tetrahedron Asymmetry"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0150","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1351\/pac196409010119","article-title":"Specification of the stereospecificity of some oxido-reductases by diamond lattice sections","volume":"9","author":"Prelog","year":"1964","journal-title":"Pure Appl. Chem."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0155","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1080\/15216540600818143","article-title":"Catalytic mechanism and substrate selectivity of aldo-keto reductases: insights from structure-function studies of Candida tenuis xylose reductase","volume":"58","author":"Kratzer","year":"2006","journal-title":"IUBMB Life"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0160","doi-asserted-by":"crossref","first-page":"4944","DOI":"10.1021\/bi035833r","article-title":"Studies of the enzymic mechanism of Candida tenuis xylose reductase (AKR2B5): X-ray structure and catalytic reaction profile for the H113A mutant","volume":"43","author":"Kratzer","year":"2004","journal-title":"Biochmistry"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0165","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.abb.2013.08.018","article-title":"Identification, characterization, and crystal structure of an aldo-keto reductase (AKR2E4) from the silkworm Bombyx mori","volume":"538","author":"Yamamoto","year":"2013","journal-title":"Arch. Biochme Biophys."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0170","doi-asserted-by":"crossref","first-page":"2021","DOI":"10.1021\/bi00174a007","article-title":"Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme","volume":"33","author":"Bohren","year":"1994","journal-title":"Biochemistry"},{"issue":"34","key":"10.1016\/j.enzmictec.2019.04.001_bib0175","doi-asserted-by":"crossref","first-page":"11264","DOI":"10.1021\/bi00035a036","article-title":"Mechanism of human aldehyde reductase: characterizatio of the active site pocket","volume":"1995","author":"Barski","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0180","doi-asserted-by":"crossref","first-page":"4095","DOI":"10.1016\/j.febslet.2008.11.003","article-title":"Tyr-51 is the proton donor-acceptor for NAD(H)-dependent interconversion of xylose and xylito by Candida renuis xylos reductase (AKR2B5)","volume":"582","author":"Pival","year":"2008","journal-title":"FEBS Lett."},{"key":"10.1016\/j.enzmictec.2019.04.001_bib0185","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.bbrc.2016.04.079","article-title":"Structural characterizaiton of an aldo-keto reductase (AKR2E5) from the silkworm Bombyx mori","volume":"474","author":"Yamamoto","year":"2016","journal-title":"Biochem. Biophys. Res. Comun."}],"container-title":["Enzyme and Microbial Technology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022919300468?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022919300468?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T01:37:54Z","timestamp":1758850674000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141022919300468"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7]]},"references-count":37,"alternative-id":["S0141022919300468"],"URL":"https:\/\/doi.org\/10.1016\/j.enzmictec.2019.04.001","relation":{},"ISSN":["0141-0229"],"issn-type":[{"value":"0141-0229","type":"print"}],"subject":[],"published":{"date-parts":[[2019,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Recombinant expression and molecular insights into the catalytic mechanism of an NADPH-dependent conjugated polyketone reductase for the asymmetric synthesis of (R)-pantolactone","name":"articletitle","label":"Article Title"},{"value":"Enzyme and Microbial Technology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.enzmictec.2019.04.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}