{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T06:40:58Z","timestamp":1788504058039,"version":"build-2803163510"},"reference-count":34,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":3287,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2000,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Conserved deamidation of PKA catalytic subunit isozymes C\u03b1 and C\u03b2\u2014more than 25% at Asn2 in vivo in both cases\u2014has been shown to yield Asp2\u2010 and isoAsp2\u2010containing isozymes (Jedrzejewski PT, Girod A, Tholey A, K\u00f6nig N, Thullner S, Kinzel V, Bossemeyer D, 1998, <jats:italic>Protein Sci 7<\/jats:italic>: 457\u2013469). Isoaspartate formation in proteins in vivo is indicative of succinimide intermediates involved in both the initial deamidation reaction as well as the \u201crepair\u201d of isoAsp to Asp by the action of protein L\u2010isoaspartyl (D\u2010aspartyl) O\u2010methyl transferase (PIMT). L\u2010Succinimide is prone to racemization to D\u2010succinimide, which may hydrolyze to D\u2010isoAsp\u2010 and D\u2010Asp\u2010containing diastereomers with, respectively, no and poor substrate character for PIMT. To analyze native PKA catalytic subunit from cardiac muscle for these isomers the N\u2010terminal tryptic peptides (T1) of the enzyme were analyzed following procedures refined specifically with a set of corresponding synthetic peptides. The methods combined high resolution high\u2010performance liquid chromatography and a new mass spectrometric procedure for the discrimination between Asp\u2010 and isoAsp\u2010residues in peptides (Lehmann et al., 2000). The results demonstrate the occurrence of D\u2010isoAsp\u2010 and D\u2010Asp\u2010containing T1 fragments in addition to the L\u2010isomers. The small amount of the L\u2010isoAsp isomer, representing only part of the D\u2010isoAsp isomer, and the relatively large amounts of the L\u2010Asp and D\u2010Asp isomers argues for an effective action of PIMT present in cardiac tissue.<\/jats:p>","DOI":"10.1110\/ps.9.11.2269","type":"journal-article","created":{"date-parts":[[2009,2,17]],"date-time":"2009-02-17T22:24:29Z","timestamp":1234909469000},"page":"2269-2277","source":"Crossref","is-referenced-by-count":19,"title":["The amino terminus of PKA catalytic subunit\u2014A site for introduction of posttranslation heterogeneities by deamidation: D\u2010Asp2 and D\u2010isoAsp2 containing isozymes"],"prefix":"10.1002","volume":"9","author":[{"given":"Volker","family":"Kinzel","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norbert","family":"K\u00f6nig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk","family":"Bossemeyer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00fcdiger","family":"Pipkorn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolf D.","family":"Lehmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"4853","DOI":"10.1016\/S0021-9258(19)34052-9","article-title":"Evidence for the in vivo deamidation and isomerization of an asparaginyl residue in cytosolic serine hydroxy\u2010methyltransferase","volume":"265","author":"Artigues A","year":"1990","journal-title":"J Biol Chem"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"10714","DOI":"10.1016\/S0021-9258(18)90570-3","article-title":"Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. 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