{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,8,23]],"date-time":"2025-08-23T00:10:08Z","timestamp":1755907808963,"version":"3.44.0"},"reference-count":37,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2025,6,18]],"date-time":"2025-06-18T00:00:00Z","timestamp":1750204800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"Photon Factory Advisory Committee","award":["2020G530 and 2021G575"],"award-info":[{"award-number":["2020G530 and 2021G575"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,9,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The \u03b1-amylase from Klebsiella pneumoniae (KpAmy13), which belongs to glycoside hydrolase family 13 subfamily 19, produces maltohexaose as an initial product when acting on starch and has been characterized as a maltohexaose-producing \u03b1-amylase. The crystal structure of KpAmy13 was determined at a resolution of 1.9\u00a0\u00c5, revealing the structures of all its domains: N, A, B and C. Domain N resembles the starch-binding domain known as carbohydrate-binding module family 69, found in \u03b1-glucan-related proteins. Although domain N does not conserve the starch-binding residues observed in other proteins, it has several hydrophobic residues on its surface, which might be involved in promoting catalysis. The catalytic cleft is located at the bottom of a circular depression. The domain N-truncated mutant of KpAmy13 in complex with maltohexaose showed that its non-reducing end glucose docks at subsite \u22126. The long and complex structure of domain B contributes to forming a cleft of the right size for six glucose moieties, demonstrating the exo-acting mechanism.<\/jats:p>","DOI":"10.1093\/jb\/mvaf034","type":"journal-article","created":{"date-parts":[[2025,6,17]],"date-time":"2025-06-17T07:38:41Z","timestamp":1750145921000},"page":"201-207","source":"Crossref","is-referenced-by-count":0,"title":["Crystal structure of <i>Klebsiella pneumoniae<\/i> maltohexaose-producing \u03b1-amylase"],"prefix":"10.1093","volume":"178","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3551-6854","authenticated-orcid":false,"given":"Zui","family":"Fujimoto","sequence":"first","affiliation":[{"name":"Research Center for Advanced Analysis, National Agriculture and Food Research Organization , 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8518 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9758-0052","authenticated-orcid":false,"given":"Naomi","family":"Kishine","sequence":"additional","affiliation":[{"name":"Research Center for Advanced Analysis, National Agriculture and Food Research Organization , 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8518 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-5417-1728","authenticated-orcid":false,"given":"Mitsuru","family":"Momma","sequence":"additional","affiliation":[{"name":"Research Center for Advanced Analysis, National Agriculture and Food Research Organization , 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8518 ,","place":["Japan"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2025,6,18]]},"reference":[{"key":"2025082219515115200_ref1","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0168-1656(01)00407-2","article-title":"Properties and applications of starch-converting enzymes of the \u03b1-amylase family","volume":"94","author":"Maarel","year":"2002","journal-title":"J. Biotechnol."},{"key":"2025082219515115200_ref2","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/0014-5793(72)80593-3","article-title":"Isolation and action pattern of maltohexaose producing amylase from Aerobacter aerogenes","volume":"26","author":"Kainuma","year":"1972","journal-title":"FEBS Lett."},{"key":"2025082219515115200_ref3","first-page":"137","article-title":"Isolation and cultivation of a novel microorganism producing a maltopentaose-forming enzyme","volume":"25","author":"Okemoto","year":"1986","journal-title":"Appl. Microbiol."},{"key":"2025082219515115200_ref4","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0006-291X(88)90554-2","article-title":"Nucleotide sequence of the maltohexaose-producing amylase gene from an alkalophilic Bacillus sp. #707 and structural similarity to liquefying type \u03b1-amylases","volume":"151","author":"Tsukamoto","year":"1989","journal-title":"Biochem. Biophys. Res. 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