{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1521699230022918656.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"NDL_BIB_ID","@value":"024429893"}},{"identifier":{"@type":"URI","@value":"http://id.ndl.go.jp/bib/024429893"}},{"identifier":{"@type":"URI","@value":"https://ndlsearch.ndl.go.jp/books/R000000004-I024429893"}},{"identifier":{"@type":"DOI","@value":"10.1016/j.jbiosc.2012.10.024"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S1389172312004501?httpAccept=text/plain"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S1389172312004501?httpAccept=text/xml"}},{"identifier":{"@type":"PMID","@value":"23218487"}},{"identifier":{"@type":"NAID","@value":"110009603684"}},{"identifier":{"@type":"URI","@value":"https://search.jamas.or.jp/link/ui/2014000598"}}],"dc:title":[{"@value":"Application of protein N-terminal amidase in enzymatic synthesis of dipeptides containing acidic amino acids specifically at the N-terminus"}],"dcterms:alternative":[{"@value":"Application of protein N-terminal amidase in enzymatic synthesis of dipeptides containing acidic amino acids specifically at the N-terminus"}],"dc:language":"en","description":[{"notation":[{"@value":"Dipeptides exhibit unique physiological functions and physical properties, e.g., l-aspartyl-l-phenylalanine-methyl ester (Asp-Phe-OMe, aspartame) as an artificial sweetener, and functional studies of peptides have been carried out in various fields. Therefore, to establish a manufacturing process for the useful dipeptides, we investigated its enzymatic synthesis by utilizing an l-amino acid ligase (Lal), which catalyzes dipeptide synthesis in an ATP-dependent manner. Many Lals were obtained, but the Lals recognizing acidic amino acids as N-terminal substrates have not been identified. To increase the variety of dipeptides that are enzymatically synthesized, we proposed a two-step synthesis: Asn-Xaa and Gln-Xaa (Asn, l-asparagine; Gln, l-glutamine; and Xaa, arbitrary amino acids) synthesized by Lals were continuously deamidated by a novel amidase, yielding Asp-Xaa and Glu-Xaa (Asp, l-aspartic acid; and Glu, l-glutamic acid). We searched for amidases that specifically deamidate the N-terminus of Asn or Gln in dipeptides since none have been previously reported. We focused on the protein N-terminal amidase from Saccharomyces cerevisiae (NTA1), and assayed its activity toward dipeptides. Our findings showed that NTA1 deamidated l-asparaginyl-l-valine (Asn-Val) and l-glutaminyl-glycine (Gln-Gly), but did not deamidate l-valyl-l-asparagine and l-alanyl-l-glutamine, suggesting that this deamidation activity is N-terminus specific. The specific activity toward Asn-Val and Gln-Gly were 190 ± 30 nmol min(-1) mg(-1)·protein and 136 ± 6 nmol min(-1) mg(-1)·protein. Additionally, we examined some characteristics of NTA1. Acidic dipeptide synthesis was examined by a combination of Lals and NTA1, resulting in the synthesis of 12 kinds of Asp-Xaa, including Asp-Phe, a precursor of aspartame, and 11 kinds of Glu-Xaa."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1581135652922467840","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000239645224"}],"foaf:name":[{"@value":"Toshinobu Arai"}]},{"@id":"https://cir.nii.ac.jp/crid/1581135652922467843","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000239645226"}],"foaf:name":[{"@value":"Eriko Takano"}]},{"@id":"https://cir.nii.ac.jp/crid/1581135652922467841","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000239645225"}],"foaf:name":[{"@value":"Atsushi Noguchi"}]}],"publication":{"publicationIdentifier":[{"@type":"NDL_BIB_ID","@value":"000000160357"},{"@type":"ISSN","@value":"13891723"},{"@type":"PISSN","@value":"13891723"},{"@type":"NCID","@value":"AA11307678"}],"prism:publicationName":[{"@value":"Journal of bioscience and bioengineering"}],"dc:publisher":[{"@value":"Suita : Society for Biotechnology"}],"prism:publicationDate":"2013-04","prism:volume":"115","prism:number":"4","prism:startingPage":"382","prism:endingPage":"387"},"reviewed":"false","url":[{"@id":"http://id.ndl.go.jp/bib/024429893"},{"@id":"https://ndlsearch.ndl.go.jp/books/R000000004-I024429893"},{"@id":"https://api.elsevier.com/content/article/PII:S1389172312004501?httpAccept=text/plain"},{"@id":"https://api.elsevier.com/content/article/PII:S1389172312004501?httpAccept=text/xml"},{"@id":"https://search.jamas.or.jp/link/ui/2014000598"}],"foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Protein%20N-terminal%20amidase","dc:title":"Protein N-terminal amidase"},{"@id":"https://cir.nii.ac.jp/all?q=L-Amino%20acid%20ligase","dc:title":"L-Amino acid ligase"},{"@id":"https://cir.nii.ac.jp/all?q=Peptide%20synthesis","dc:title":"Peptide synthesis"},{"@id":"https://cir.nii.ac.jp/all?q=Functional%20peptide","dc:title":"Functional peptide"},{"@id":"https://cir.nii.ac.jp/all?q=Aspartame","dc:title":"Aspartame"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360283693432693248","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"<scp>l</scp>\n            -Amino Acid Ligase from Pseudomonas syringae Producing Tabtoxin Can Be Used for Enzymatic Synthesis of Various Functional Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292618790785408","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Fermentative Production of<scp>l</scp>-Alanyl-<scp>l</scp>-Glutamine by a Metabolically Engineered<i>Escherichia coli</i>Strain Expressing<scp>l</scp>-Amino Acid α-Ligase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292619544374528","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"<i>ywfE</i>in<i>Bacillus subtilis</i>Codes for a Novel Enzyme,<scp>l</scp>-Amino Acid Ligase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292621372897280","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A Mouse Amidase Specific for N-terminal Asparagine"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565164572657280","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references","cites"],"jpcoar:relatedTitle":[{"@value":"Novel <scp>CCK</scp>‐dependent vasorelaxing dipeptide, <scp>A</scp>rg‐<scp>P</scp>he, decreases blood pressure and food intake in rodents"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565169113744384","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A novel l-amino acid ligase from bacillus licheniformis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848661758610560","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"ATP regulation in bioproduction"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855568799085952","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Some Enzymatic Properties and Substrate Specificities of Peptidoglutaminase-I and II"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418520179598720","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"l-Asparaginase from Erwinia carotovora"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699993917256576","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Protein NH2-terminal asparagine deamidase. Isolation and characterization of a new enzyme."}]},{"@id":"https://cir.nii.ac.jp/crid/1361699994248896640","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Peptide synthesis: chemical or enzymatic"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699995428644096","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Protein‐glutaminase from <i>Chryseobacterium proteolyticum</i>, an enzyme that deamidates glutaminyl residues in proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699996190189184","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Yeast N-terminal Amidase"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262946008691712","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825893443254272","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The N-End Rule Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825894842867072","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Dipeptide synthesis by l-amino acid ligase from Ralstonia solanacearum"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107371319784064","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Poly-α-Glutamic Acid Synthesis Using a Novel Catalytic Activity of RimK from\n            <i>Escherichia coli</i>\n            K-12"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670318986500608","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synthesis and application of dipeptides; 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