{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T07:45:31Z","timestamp":1768722331496,"version":"3.49.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1992,12,1]]},"abstract":"<jats:p>Escherichia coli dihydrodipicolinate synthase (DHDPS) (EC 4.2.1.52), the first enzyme unique to lysine biosynthesis, catalyses the condensation of pyruvate and aspartate beta-semialdehyde (ASA) by a ping-pong mechanism. Pyruvate binds first to the enzyme, forming a Schiff base with the epsilon-amino group of Lys-161, followed by binding of ASA. Km values of 0.57 and 0.55 mM were determined for pyruvate and DL-ASA respectively. 3-Bromopyruvate inhibits DHDPS with a Ki of 1.6 mM. DHDPS is 50% inhibited by 1.0 mM-L-lysine, 1.2 mM-sodium dipicolinate or 4.6 mM-S-2-aminoethyl-L-cysteine. Crystals of DHDPS diffracting to beyond a resolution of 0.24 nm (2.4 A) were obtained under several experimental conditions. Diffraction patterns were compatible with trigonal space groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 12.26 nm and c = 11.19 nm. The density of the crystals indicates the presence of a dimer of DHDPS subunits per asymmetric unit.<\/jats:p>","DOI":"10.1042\/bj2880691","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:29:52Z","timestamp":1439242192000},"page":"691-695","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":76,"title":["<i>Escherichia coli<\/i> dihydrodipicolinate synthase. Identification of the active site and crystallization"],"prefix":"10.1042","volume":"288","author":[{"given":"B","family":"Laber","sequence":"first","affiliation":[{"name":"Max-Planck-Institute f\u00fcr Biochemie, D-8033 Martinsried, Federal Republic of Germany"}]},{"given":"F X","family":"Gomis-R\u00fcth","sequence":"additional","affiliation":[{"name":"Max-Planck-Institute f\u00fcr Biochemie, D-8033 Martinsried, Federal Republic of Germany"}]},{"given":"M J","family":"Rom\u00e3o","sequence":"additional","affiliation":[{"name":"Max-Planck-Institute f\u00fcr Biochemie, D-8033 Martinsried, Federal Republic of Germany"}]},{"given":"R","family":"Huber","sequence":"additional","affiliation":[{"name":"Max-Planck-Institute f\u00fcr Biochemie, D-8033 Martinsried, Federal Republic of Germany"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/288\/2\/691\/608745\/bj2880691.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/288\/2\/691\/608745\/bj2880691.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T22:16:03Z","timestamp":1637705763000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/288\/2\/691\/29049\/Escherichia-coli-dihydrodipicolinate-synthase"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,12,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1992,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2880691","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,12,1]]}}}