{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T16:31:21Z","timestamp":1761237081910,"version":"build-2065373602"},"reference-count":45,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2004,9,1]],"date-time":"2004-09-01T00:00:00Z","timestamp":1093996800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2004,9,1]],"date-time":"2004-09-01T00:00:00Z","timestamp":1093996800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,11,22]],"date-time":"2023-11-22T00:00:00Z","timestamp":1700611200000},"content-version":"vor","delay-in-days":7021,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Research in Microbiology"],"published-print":{"date-parts":[[2004,9]]},"DOI":"10.1016\/j.resmic.2004.03.007","type":"journal-article","created":{"date-parts":[[2004,4,21]],"date-time":"2004-04-21T03:12:17Z","timestamp":1082517137000},"page":"525-534","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"title":["Cloning, characterization and heterologous expression of the aspartokinase and aspartate semialdehyde dehydrogenase genes of cephamycin C-producer Streptomyces clavuligerus"],"prefix":"10.1016","volume":"155","author":[{"given":"Sedef","family":"Tunca","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ebru I","family":"Y\u0131lmaz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacqueline","family":"Piret","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paloma","family":"Liras","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G\u00fclay","family":"\u00d6zcengiz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.resmic.2004.03.007_BIB001","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/417141a","article-title":"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)","volume":"417","author":"Bentley","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.resmic.2004.03.007_BIB002","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1111\/j.1432-1033.1980.tb04398.x","article-title":"Aspartate-\u03b2-semialdehyde dehydrogenase from Escherichia coli","volume":"104","author":"Biellmann","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.resmic.2004.03.007_BIB003","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1111\/j.1432-1033.1980.tb04399.x","article-title":"Aspartate-\u03b2-semialdehyde dehydrogenase from Escherichia coli. Affinity labelling with the substrate analogue l-2-amino-4-oxo-5-chloropentanoic acid: An example of half-site reactivity","volume":"104","author":"Biellmann","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.resmic.2004.03.007_BIB004","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0021-9258(18)71042-9","article-title":"Aspartic \u03b2-semialdehyde dehydrogenase and aspartic \u03b2-semialdehyde","volume":"213","author":"Black","year":"1955","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.resmic.2004.03.007_BIB005","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.resmic.2004.03.007_BIB006","first-page":"2931","article-title":"Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli","volume":"135","author":"Chen","year":"1989","journal-title":"J. Gen. Microbiol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB007","doi-asserted-by":"crossref","first-page":"9448","DOI":"10.1016\/S0021-9258(18)98372-9","article-title":"Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase","volume":"268","author":"Chen","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.resmic.2004.03.007_BIB008","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1111\/j.1365-2958.1994.tb00342.x","article-title":"Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria","volume":"11","author":"Cirillo","year":"1994","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB009","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1128\/jb.99.3.791-801.1969","article-title":"Regulation of the biosynthesis of amino acids of the aspartate family in coliform bacteria and pseudomonads","volume":"99","author":"Cohen","year":"1969","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB010","first-page":"3221","article-title":"Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum","volume":"134","author":"Cremer","year":"1988","journal-title":"J. Gen. Microbiol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB011","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1021\/bi00270a023","article-title":"A triglobular model for the polypeptide chain of aspartokinase I\u2013homoserine dehydrogenase I of Escherichia coli","volume":"22","author":"Fazel","year":"1983","journal-title":"Biochemistry"},{"key":"10.1016\/j.resmic.2004.03.007_BIB012","doi-asserted-by":"crossref","first-page":"4096","DOI":"10.1128\/jb.175.13.4096-4103.1993","article-title":"Gene structure and expression of the Corynebacterium flavum N13 ask\u2013asd operon","volume":"175","author":"Follettie","year":"1993","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB013","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/S0022-2836(83)80284-8","article-title":"Studies on transformation of E. coli with plasmids","volume":"166","author":"Hanahan","year":"1983","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB014","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1002\/j.1460-2075.1982.tb01178.x","article-title":"Nucleotide sequence of the asd gene of Escherichia coli: Absence of a typical attenuation signal","volume":"1","author":"Haziza","year":"1982","journal-title":"EMBO J."},{"key":"10.1016\/j.resmic.2004.03.007_BIB015","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1099\/00221287-147-6-1547","article-title":"Structure of the ask\u2013asd operon and formation of aspartokinase subunits in the cephamycin producer \u2018Amycolatopsis lactamdurans\u2019","volume":"147","author":"Hernando-Rico","year":"2001","journal-title":"Microbiology"},{"key":"10.1016\/j.resmic.2004.03.007_BIB016","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1099\/00207713-21-4-326","article-title":"Streptomyces clavuligerus sp. nov., a \u03b2-lactam antibiotic producer","volume":"21","author":"Higgins","year":"1971","journal-title":"Int. J. Syst. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB017","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1007\/BF00459522","article-title":"Restriction analysis of the Streptomyces glaucescens genome by agarose gel electrophoresis","volume":"130","author":"Hintermann","year":"1981","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB018","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/0005-2744(76)90089-9","article-title":"Lysine and lysine plus threonine inhibitable aspartokinases in Bacillus brevis","volume":"445","author":"Hitchcock","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.resmic.2004.03.007_BIB019","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1007\/BF00262424","article-title":"Aspartokinase genes lysC\u03b1 and lysC\u03b2 overlap and are adjacent to the aspartate \u03b2-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum","volume":"224","author":"Kalinowski","year":"1990","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.resmic.2004.03.007_BIB020","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0167-4838(91)90060-D","article-title":"Chemical and kinetic mechanism of aspartate-\u03b2-semialdehyde dehydrogenase from Escherichia coli","volume":"1077","author":"Karsten","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.resmic.2004.03.007_BIB021","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1128\/AAC.17.4.679","article-title":"l-lysine-\u03b5-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans","volume":"17","author":"Kern","year":"1980","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.resmic.2004.03.007_BIB022","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature (London)"},{"key":"10.1016\/j.resmic.2004.03.007_BIB023","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1099\/00221287-142-4-791","article-title":"Streptomyces akiyoshiensis differs from other Gram-positive bacteria in the organization of a core biosynthetic pathway gene for aspartate family amino acids","volume":"142","author":"Le","year":"1996","journal-title":"Microbiology"},{"key":"10.1016\/j.resmic.2004.03.007_BIB024","doi-asserted-by":"crossref","first-page":"6916","DOI":"10.1128\/jb.175.21.6916-6924.1993","article-title":"Precursor flux control through targeted chromosomal insertion of the lysine \u03b5-aminotransferase (lat) gene in cephamycin C biosynthesis","volume":"175","author":"Malmberg","year":"1993","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB025","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1007\/BF00164502","article-title":"Effects of enhanced lysine \u03b5-aminotransferase activity on cephamycin biosynthesis in Streptomyces clavuligerus","volume":"44","author":"Malmberg","year":"1995","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB026","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1111\/j.1574-6968.1996.tb08468.x","article-title":"Molecular control mechanisms of lysine and threonine biosynthesis in amino acid-producing corynebacteria: Redirecting carbon flow","volume":"143","author":"Malumbres","year":"1996","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.resmic.2004.03.007_BIB027","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1128\/AAC.21.1.74","article-title":"Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthetase and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus","volume":"21","author":"Mendelovitz","year":"1982","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.resmic.2004.03.007_BIB028","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1128\/jb.134.2.483-491.1978","article-title":"Aspartokinase of Streptococcus mutans: Purification, properties, and regulation","volume":"134","author":"McCarron","year":"1978","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB029","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1006\/prep.2002.1626","article-title":"Expression and purification of aspartate \u03b2-semialdehyde dehydrogenase from infectious microorganisms","volume":"25","author":"Moore","year":"2002","journal-title":"Protein Express. Purif."},{"key":"10.1016\/j.resmic.2004.03.007_BIB030","doi-asserted-by":"crossref","first-page":"6394","DOI":"10.1021\/bi00019a019","article-title":"Use of structural comparisons to select mutagenic targets in aspartate-\u03b2-semialdehyde dehydrogenase","volume":"34","author":"Ouyang","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.resmic.2004.03.007_BIB031","first-page":"207","article-title":"Induction of l-lysine \u03b5-aminotransferase by l-lysine in Streptomyces clavuligerus, producer of cephalosporins","volume":"144","author":"Rius","year":"1996","journal-title":"FEMS Microbiol. Lett."},{"year":"1989","series-title":"Molecular Cloning, A Laboratory Manual","author":"Sambrook","key":"10.1016\/j.resmic.2004.03.007_BIB032"},{"key":"10.1016\/j.resmic.2004.03.007_BIB033","series-title":"Regulation of Secondary Metabolites in Actinomycetes","first-page":"1","article-title":"Structural organization of antibiotic biosynthesis and resistance genes in actinomyces","author":"Seno","year":"1989"},{"key":"10.1016\/j.resmic.2004.03.007_BIB034","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1093\/oxfordjournals.jbchem.a129089","article-title":"Concerted inhibition and its reversal by end products of aspartate kinase in Brevibacterium flavum","volume":"65","author":"Shio","year":"1969","journal-title":"J. Biochem."},{"key":"10.1016\/j.resmic.2004.03.007_BIB035","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1099\/00207713-16-3-313","article-title":"Methods for characterization of Streptomyces species","volume":"16","author":"Shirling","year":"1966","journal-title":"Int. J. Syst. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB036","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1093\/nar\/20.5.961","article-title":"Compilation and analysis of DNA sequences associated with apparent streptomycete promoters","volume":"20","author":"Strohl","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.resmic.2004.03.007_BIB037","first-page":"69","article-title":"Transduction and genome structure in Streptomyces","volume":"29","author":"Stuttard","year":"1988","journal-title":"Dev. Ind. Microbiol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB038","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1128\/jb.117.1.133-143.1974","article-title":"Mapping of the structural genes of three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K12","volume":"117","author":"Theze","year":"1974","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB039","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/0014-5793(85)80297-0","article-title":"Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E. coli K12","volume":"181","author":"Veron","year":"1985","journal-title":"FEBS Lett."},{"key":"10.1016\/j.resmic.2004.03.007_BIB040","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1021\/ar000057q","article-title":"The central enzymes of the aspartate family of amino acid biosynthesis","volume":"34","author":"Viola","year":"2001","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.resmic.2004.03.007_BIB041","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0378-1119(92)90669-G","article-title":"Codon usage in the G+C-rich Streptomyces genome","volume":"113","author":"Wright","year":"1992","journal-title":"Gene"},{"key":"10.1016\/j.resmic.2004.03.007_BIB042","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1128\/jb.172.2.701-708.1990","article-title":"Comparison of the three aspartokinase isoenzymes in Bacillus subtilis Marburg and 168","volume":"172","author":"Zhang","year":"1990","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.resmic.2004.03.007_BIB043","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1042\/bj2830691","article-title":"Biochemical studies on the activity of delta-(l-alpha-aminoadipyl)-l-cysteinyl-d-valine synthetase from Streptomyces clavuligerus","volume":"283","author":"Zhang","year":"1992","journal-title":"Biochem. J."},{"key":"10.1016\/j.resmic.2004.03.007_BIB044","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/S0378-1119(99)00307-8","article-title":"Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV-producing Amycolatopsis mediterranei","volume":"237","author":"Zhang","year":"1999","journal-title":"Gene"},{"key":"10.1016\/j.resmic.2004.03.007_BIB045","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1007\/s002530000345","article-title":"Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase from the rifamycin SV-producing Amycolatopsis mediterranei U32","volume":"54","author":"Zhang","year":"2000","journal-title":"Appl. Microbiol. Biotechnol."}],"container-title":["Research in Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0923250804000932?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0923250804000932?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,13]],"date-time":"2025-10-13T04:59:30Z","timestamp":1760331570000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0923250804000932"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,9]]},"references-count":45,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2004,9]]}},"alternative-id":["S0923250804000932"],"URL":"https:\/\/doi.org\/10.1016\/j.resmic.2004.03.007","relation":{},"ISSN":["0923-2508"],"issn-type":[{"type":"print","value":"0923-2508"}],"subject":[],"published":{"date-parts":[[2004,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cloning, characterization and heterologous expression of the aspartokinase and aspartate semialdehyde dehydrogenase genes of cephamycin C-producer Streptomyces clavuligerus","name":"articletitle","label":"Article Title"},{"value":"Research in Microbiology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.resmic.2004.03.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"converted-article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2004 \u00c9ditions scientifiques et m\u00e9dicales Elsevier SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}