{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:53:41Z","timestamp":1786978421424,"version":"build-2736575974"},"reference-count":25,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2015,10,16]],"date-time":"2015-10-16T00:00:00Z","timestamp":1444953600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2015,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Halohydrin hydrogen\u2010halide\u2010lyase (H\u2010Lyase) is a bacterial enzyme that is involved in the degradation of halohydrins. This enzyme catalyzes the intramolecular nucleophilic displacement of a halogen by a vicinal hydroxyl group in halohydrins to produce the corresponding epoxides. The epoxide products are subsequently hydrolyzed by an epoxide hydrolase, yielding the corresponding 1, 2\u2010diol. Until now, six different H\u2010Lyases have been studied. These H\u2010Lyases are grouped into three subtypes (A, B, and C) based on amino acid sequence similarities and exhibit different enantioselectivity.\n                    <jats:italic>Corynebacterium<\/jats:italic>\n                    sp. strain N\u20101074 has two different isozymes of H\u2010Lyase, HheA (A\u2010type) and HheB (B\u2010type). We have determined their crystal structures to elucidate the differences in enantioselectivity among them. All three groups share a similar structure, including catalytic sites. The lack of enantioselectivity of HheA seems to be due to the relatively wide size of the substrate tunnel compared to that of other H\u2010Lyases. Among the B\u2010type H\u2010Lyases, HheB shows relatively high enantioselectivity compared to that of HheB\n                    <jats:sub>GP1<\/jats:sub>\n                    . This difference seems to be due to amino acid replacements at the active site tunnel. The binding mode of 1, 3\u2010dicyano\u20102\u2010propanol at the catalytic site in the crystal structure of the HheB\u2010DiCN complex suggests that the product should be (\n                    <jats:italic>R<\/jats:italic>\n                    )\u2010epichlorohydrin, which agrees with the enantioselectivity of HheB. Comparison with the structure of HheC provides a clue for the difference in their enantioselectivity. Proteins 2015; 83:2230\u20132239. \u00a9 2015 Wiley Periodicals, Inc.\n                  <\/jats:p>","DOI":"10.1002\/prot.24938","type":"journal-article","created":{"date-parts":[[2015,9,30]],"date-time":"2015-09-30T19:54:44Z","timestamp":1443642884000},"page":"2230-2239","source":"Crossref","is-referenced-by-count":16,"title":["Crystal structures of halohydrin hydrogen\u2010halide\u2010lyases from\n                    <i>Corynebacterium<\/i>\n                    sp. N\u20101074"],"prefix":"10.1002","volume":"83","author":[{"given":"Fumiaki","family":"Watanabe","sequence":"first","affiliation":[{"name":"Yokohama Research Laboratories Mitsubishi Rayon Co. Ltd. Yokohama Kanagawa 230\u20100053 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fujio","family":"Yu","sequence":"additional","affiliation":[{"name":"Yokohama Research Laboratories Mitsubishi Rayon Co. Ltd. Yokohama Kanagawa 230\u20100053 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akashi","family":"Ohtaki","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Life Science, Graduate School of Technology Tokyo University of Agriculture and Technology Koganei Tokyo 184\u20108588 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuaki","family":"Yamanaka","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Life Science, Graduate School of Technology Tokyo University of Agriculture and Technology Koganei Tokyo 184\u20108588 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keiichi","family":"Noguchi","sequence":"additional","affiliation":[{"name":"Instrumentation Analysis Center Tokyo University of Agriculture and Technology Koganei Tokyo 184\u20108588 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masafumi","family":"Yohda","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Life Science, Graduate School of Technology Tokyo University of Agriculture and Technology Koganei Tokyo 184\u20108588 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masafumi","family":"Odaka","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Life Science, Graduate School of Technology Tokyo University of Agriculture and Technology Koganei Tokyo 184\u20108588 Japan"},{"name":"Department of Life Science, Faculty and Graduate School of Engineering and Resource Science Akita University Akita City, Akita 010\u20108502 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2015,10,16]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0957-4166(02)00222-7"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1002\/cbic.200700734"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.183.17.5058-5066.2001"},{"key":"e_1_2_8_5_1","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1128\/jb.173.1.124-129.1991","article-title":"Purification and characterization of haloalcohol dehalogenase from Arthrobacter Sp Strain Ad2","volume":"173","author":"den Wijngaard AJ","year":"1991","journal-title":"J Bacteriol"},{"key":"e_1_2_8_6_1","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1128\/aem.60.4.1297-1301.1994","article-title":"Characterization of a novel enantioselective halohydrin hydrogen\u2010halide\u2010lyase","volume":"60","author":"Nakamura T","year":"1994","journal-title":"Appl Environ Microbiol"},{"key":"e_1_2_8_7_1","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1128\/aem.59.1.227-230.1993","article-title":"Production of (R)\u22123\u2010chloro\u20101,2\u2010propanediol from prochiral 1,3\u2010dichloro\u20102\u2010propanol by corynebacterium sp. strain N\u20101074","volume":"59","author":"Nakamura T","year":"1993","journal-title":"Appl Environ Microbiol"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1271\/bbb.58.1451"},{"key":"e_1_2_8_9_1","doi-asserted-by":"crossref","first-page":"2050","DOI":"10.1128\/JB.181.7.2050-2058.1999","article-title":"Degradation of 1,2\u2010dibromoethane by Mycobacterium sp. strain GP1","volume":"181","author":"Poelarends GJ","year":"1999","journal-title":"J Bacteriol"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0040-4020(01)89297-8"},{"key":"e_1_2_8_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/adsc.200505333"},{"key":"e_1_2_8_12_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/cdg479"},{"key":"e_1_2_8_13_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi034941a"},{"key":"e_1_2_8_14_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi047613z"},{"key":"e_1_2_8_15_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01866-05"},{"key":"e_1_2_8_16_1","doi-asserted-by":"publisher","DOI":"10.1271\/bbb1961.55.1931"},{"key":"e_1_2_8_17_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.174.23.7613-7619.1992"},{"key":"e_1_2_8_18_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1011254402785"},{"key":"e_1_2_8_19_1","volume-title":"Methods Enzymol. Macromolecular Crystallography, Part A","author":"Otwinowski Z","year":"1997"},{"key":"e_1_2_8_20_1","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","author":"Collaborative Computational Project N.","year":"1994","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_8_21_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444998003254"},{"key":"e_1_2_8_22_1","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.1999.4094"},{"key":"e_1_2_8_23_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444999000839"},{"key":"e_1_2_8_24_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889892009944"},{"key":"e_1_2_8_25_1","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/btu364"},{"key":"e_1_2_8_26_1","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.06586-11"}],"container-title":["Proteins: Structure, Function, and Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.24938","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.24938","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/prot.24938","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,3]],"date-time":"2023-10-03T16:36:35Z","timestamp":1696350995000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/prot.24938"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,10,16]]},"references-count":25,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2015,12]]}},"alternative-id":["10.1002\/prot.24938"],"URL":"https:\/\/doi.org\/10.1002\/prot.24938","archive":["Portico"],"relation":{},"ISSN":["0887-3585","1097-0134"],"issn-type":[{"value":"0887-3585","type":"print"},{"value":"1097-0134","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,10,16]]}}}