{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T17:03:03Z","timestamp":1791219783153,"version":"4.1.0"},"reference-count":47,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2006,6,1]],"date-time":"2006-06-01T00:00:00Z","timestamp":1149120000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,6,1]],"date-time":"2006-06-01T00:00:00Z","timestamp":1149120000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2006,6]]},"DOI":"10.1016\/j.jmb.2006.03.058","type":"journal-article","created":{"date-parts":[[2006,4,19]],"date-time":"2006-04-19T13:42:33Z","timestamp":1145454153000},"page":"690-707","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":103,"title":["Crystal Structure of Pullulanase: Evidence for Parallel Binding of Oligosaccharides in the Active Site"],"prefix":"10.1016","volume":"359","author":[{"given":"Bunzo","family":"Mikami","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Iwamoto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominggus","family":"Malle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hye-Jin","family":"Yoon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elif","family":"Demirkan-Sarikaya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshihiro","family":"Mezaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshio","family":"Katsuya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2006.03.058_bib1","first-page":"191","article-title":"Glycogen and starch debranching enzymes","volume":"5","author":"Lee","year":"1971","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2006.03.058_bib2","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1080\/10408410490435115","article-title":"Pullulan degrading enzymes of bacterial origin","volume":"30","author":"Doman-Pytka","year":"2004","journal-title":"Crit. Rev. Microbiol."},{"key":"10.1016\/j.jmb.2006.03.058_bib3","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/S0008-6215(00)84494-8","article-title":"Action of Pseudomonas isoamylase on various branched oligo- and poly-saccharides","volume":"61","author":"Kainuma","year":"1978","journal-title":"Carbohydr. Res."},{"key":"10.1016\/j.jmb.2006.03.058_bib4","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1042\/bj3110350","article-title":"Families, superfamilies and subfamilies of glycosyl hydrolases","volume":"311","author":"Henrissat","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2006.03.058_bib5","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/S1367-5931(02)00311-3","article-title":"Starch-hydrolyzing enzymes from thermophilic archaea and bacteria","volume":"6","author":"Bertoldo","year":"2002","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.jmb.2006.03.058_bib6","first-page":"83","article-title":"Observations on the specificity and nomenclature of starch debranching enzymes","volume":"44","author":"Manners","year":"1997","journal-title":"J. Appl. Glycosci."},{"key":"10.1016\/j.jmb.2006.03.058_bib7","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1093\/pcp\/pcf091","article-title":"Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue","volume":"43","author":"Nakamura","year":"2002","journal-title":"Plant Cell Physiol."},{"key":"10.1016\/j.jmb.2006.03.058_bib8","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/0006-291X(66)90474-8","article-title":"Pullulanase from Aerobacter aerogenes; production in a cell-bound state. Purification and properties of the enzyme","volume":"3","author":"Wallenfels","year":"1966","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jmb.2006.03.058_bib9","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1042\/bj1080033","article-title":"Metabolism of the reserve polysaccharide of Streptococcus mitis. Some properties of a pullulanase","volume":"108","author":"Walker","year":"1968","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2006.03.058_bib10","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/0005-2744(75)90192-8","article-title":"Purification and some properties of alkaline pullulanase from a strain of Bacillus no. 202-1, an alkalophilic microorganism","volume":"397","author":"Nakamura","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2006.03.058_bib11","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1128\/aem.49.2.294-298.1985","article-title":"Cloning of the pullulanase gene and overproduction of pullulanase in Escherichia coli and Klebsiella aerogenes","volume":"49","author":"Takizawa","year":"1985","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jmb.2006.03.058_bib12","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1128\/jb.169.5.2301-2306.1987","article-title":"Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70","volume":"169","author":"Katsuragi","year":"1987","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2006.03.058_bib13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0167-4838(00)00302-2","article-title":"Relationship of sequence and structure to specificity in the \u03b1-amylase family of enzymes","volume":"1546","author":"MacGregor","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2006.03.058_bib14","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1046\/j.1432-1033.2003.03404.x","article-title":"Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain","volume":"270","author":"Janecek","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2006.03.058_bib15","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0922-338X(97)89246-X","article-title":"Amino acid residues specific for the catalytic action towards \u03b1-1,6-glucosidic linkages in Klebsiella pullulanase","volume":"84","author":"Yamashita","year":"1997","journal-title":"J. Ferment. Bioeng."},{"key":"10.1016\/j.jmb.2006.03.058_bib16","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1128\/AEM.65.5.2084-2091.1999","article-title":"Pullulanase type from Fervidobacterium pennavorans Ven5: cloning, sequencing, and expression of the gene and biochemical characterization of the recombinant enzyme","volume":"65","author":"Bertoldo","year":"1999","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jmb.2006.03.058_bib17","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1042\/bj2520343","article-title":"Purification and characterization of a highly thermostable novel pullulanase from Clostridium thermohydrosulfuricum","volume":"252","author":"Saha","year":"1988","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2006.03.058_bib18","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1093\/oxfordjournals.jbchem.a124010","article-title":"Interaction between pullulanase from Klebsiella pneumoniae and cyclodextrins","volume":"113","author":"Iwamoto","year":"1993","journal-title":"J. Biochem."},{"key":"10.1016\/j.jmb.2006.03.058_bib19","doi-asserted-by":"crossref","first-page":"1264","DOI":"10.1093\/oxfordjournals.jbchem.a124673","article-title":"Comparison of the binding of beta-cyclodextrin and alpha- and gamma-cyclodextrins with pullulanase from Klebsiella pneumoniae as studied by equilibrium and kinetic fluorometry","volume":"116","author":"Iwamoto","year":"1994","journal-title":"J. Biochem."},{"key":"10.1016\/j.jmb.2006.03.058_bib20","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1093\/oxfordjournals.jbchem.a124669","article-title":"Random mutagenesis of pullulanase from Klebsiella aerogenes for studies of the structure and function of the enzyme","volume":"116","author":"Yamashita","year":"1994","journal-title":"J. Biochem."},{"key":"10.1016\/j.jmb.2006.03.058_bib21","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1007\/BF01024938","article-title":"Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta\/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes","volume":"12","author":"Jesperson","year":"1993","journal-title":"J. Protein Chem."},{"key":"10.1016\/j.jmb.2006.03.058_bib22","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1006\/jmbi.1998.1992","article-title":"Three-dimensional structure of Pseudomonas isoamylase at 2.2\u00c5 resolution","volume":"281","author":"Katsuya","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2006.03.058_bib23","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system (CNS): a new software system for macromolecular structure determination","volume":"54","author":"Br\u00fcnger","year":"1998","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.03.058_bib24","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1107\/S0365110X52002161","article-title":"Traitement statistique des erreurs dans la determination des structures cristallines","volume":"5","author":"Luzzati","year":"1952","journal-title":"Acta Crystallog."},{"key":"10.1016\/j.jmb.2006.03.058_bib25","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0065-3233(08)60402-7","article-title":"Conformations of polypeptides and proteins","volume":"23","author":"Ramachandran","year":"1968","journal-title":"Advan. Protein Chem."},{"key":"10.1016\/j.jmb.2006.03.058_bib26","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1093\/protein\/gzg088","article-title":"Vicinal disulfide turns","volume":"16","author":"Carugo","year":"2003","journal-title":"Protein Eng."},{"key":"10.1016\/j.jmb.2006.03.058_bib27","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/S0969-2126(03)00151-5","article-title":"The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs","volume":"11","author":"Robert","year":"2003","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2006.03.058_bib28","doi-asserted-by":"crossref","first-page":"15633","DOI":"10.1021\/bi048215z","article-title":"Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens","volume":"43","author":"van Bueren","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2006.03.058_bib29","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.mib.2005.04.013","article-title":"Microbial starch-binding domain","volume":"8","author":"Rodriguez-Sanoja","year":"2005","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jmb.2006.03.058_bib30","doi-asserted-by":"crossref","first-page":"7050","DOI":"10.1021\/bi9829377","article-title":"Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose","volume":"38","author":"Mikami","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2006.03.058_bib31","first-page":"619","article-title":"Structure of separated starch-binding domain of Bacillus cereus \u03b2-amylase","volume":"9","author":"Yoon","year":"1999","journal-title":"J. Microbiol. Biotechnol."},{"key":"10.1016\/j.jmb.2006.03.058_bib32","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1042\/bj3210557","article-title":"Nomenclature for sugar-binding subsites in glycosyl hydrolases","volume":"15","author":"Davies","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2006.03.058_bib33","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/S1389-1723(99)80114-5","article-title":"The concept of the alpha-amylase family: structural similarity and common catalytic mechanism","volume":"87","author":"Kuriki","year":"1999","journal-title":"J. Biosci. Bioeng."},{"key":"10.1016\/j.jmb.2006.03.058_bib34","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0167-4838(00)00041-8","article-title":"Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family","volume":"1478","author":"Park","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2006.03.058_bib35","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1271\/bbb.65.401","article-title":"The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 alpha-amylases: effects of domain N on activity, specificity, stability and dimerization","volume":"65","author":"Yokota","year":"2001","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.jmb.2006.03.058_bib36","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1042\/BA20010052","article-title":"Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose","volume":"35","author":"Cheong","year":"2002","journal-title":"Biotechnol. Appl. Biochem."},{"key":"10.1016\/j.jmb.2006.03.058_bib37","doi-asserted-by":"crossref","first-page":"4778","DOI":"10.1021\/bi9921182","article-title":"Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques","volume":"39","author":"Brayer","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2006.03.058_bib38","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2006.03.058_bib39","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1107\/S090744499900935X","article-title":"The finer things in X-ray diffraction data collection","volume":"55","author":"Pflugrath","year":"1999","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.03.058_bib40","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1016\/S0076-6879(97)77033-2","article-title":"PHASES-95: a program package for processing and analyzing diffraction data from macromolecules","volume":"277","author":"Furey","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2006.03.058_bib41","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. Crystallog."},{"key":"10.1016\/j.jmb.2006.03.058_bib42","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/381272a0","article-title":"Errors in protein structures","volume":"381","author":"Hooft","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2006.03.058_bib43","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure","volume":"24","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallog."},{"key":"10.1016\/j.jmb.2006.03.058_bib44","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1107\/S0907444994006396","article-title":"Raster3D version 2.0. A program for photorealistic molecular graphics","author":"Merrit","year":"1994","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2006.03.058_bib45","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/S1093-3263(97)00021-1","article-title":"An extensively modified version of MolScript that includes greatly enhanced coloring capabilities","volume":"15","author":"Esnouf","year":"1997","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.jmb.2006.03.058_bib46","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1002\/prot.340110407","article-title":"Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons","volume":"11","author":"Nicholls","year":"1991","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1016\/j.jmb.2006.03.058_bib47","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1107\/S0021889802022112","article-title":"Single-crystal structure validation with the program PLATON","volume":"36","author":"Spek","year":"2003","journal-title":"J. Appl. Crystallog"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283606004219?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283606004219?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T20:55:15Z","timestamp":1758315315000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283606004219"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,6]]},"references-count":47,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2006,6]]}},"alternative-id":["S0022283606004219"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2006.03.058","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2006,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Crystal Structure of Pullulanase: Evidence for Parallel Binding of Oligosaccharides in the Active Site","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2006.03.058","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2006 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}