{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T20:35:20Z","timestamp":1790800520786,"version":"4.1.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,4,15]]},"abstract":"<jats:p>Cystathionine \u03b3-synthase catalyses the first reaction specific for methionine biosynthesis in plants, the \u03b3-replacement of the phosphoryl substituent of O-phosphohomoserine by cysteine. A cDNA encoding cystathionine \u03b3-synthase from Arabidopsis thalianahas been cloned and used to overexpress the enzyme in Escherichia coli.The native recombinant enzyme is a homotetramer composed of 53\u00a0kDa subunits, each being tightly associated with one molecule of pyridoxal 5\u00b4-phosphate that binds at lysine-379 of the protein precursor. The replacement reaction follows a Ping Pong mechanism with a Vmax of 33.6 units\/mg and Km values of 2.5\u00a0mM and 460\u00a0\u00b5M for O-phosphohomoserine and cysteine respectively. The protective effect of O-phosphohomoserine against enzyme inactivation by propargylglycine indicated that the Kd for the substrate is approx. 1\/2500 of its Km value. Thus most of these biochemical properties are similar to those previously reported for plant and bacterial cystathionine \u03b3-synthases. However, the plant enzyme differs markedly from its enterobacterial counterparts because it catalyses a very faint \u03b3-elimination of O-phosphohomoserine in the absence of cysteine, this process being about 1\/2700 as fast as the \u03b3-replacement reaction and approx. 1\/1500 as fast as the \u03b3-elimination catalysed by the E. colienzyme. This huge difference could be attributed to the inability of the A. thalianacystathionine \u03b3-synthase to accumulate a long-wavelength-absorbing species that is characteristic for the efficient \u03b3-elimination reaction catalysed by the enterobacterial enzyme.<\/jats:p>","DOI":"10.1042\/bj3310639","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T22:01:27Z","timestamp":1439244087000},"page":"639-648","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":80,"title":["Cystathionine \u03b3-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli"],"prefix":"10.1042","volume":"331","author":[{"given":"St\u00e9phane","family":"RAVANEL","sequence":"first","affiliation":[{"name":"Laboratoire Mixte CNRS\/Rh\u00f4ne-Poulenc (UMR41), Rh\u00f4ne-Poulenc Agrochimie, 14\u201320 rue Pierre Baizet, 69263 Lyon cedex 09, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bertrand","family":"GAKI\u00c8RE","sequence":"additional","affiliation":[{"name":"Laboratoire Mixte CNRS\/Rh\u00f4ne-Poulenc (UMR41), Rh\u00f4ne-Poulenc Agrochimie, 14\u201320 rue Pierre Baizet, 69263 Lyon cedex 09, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"JOB","sequence":"additional","affiliation":[{"name":"Laboratoire Mixte CNRS\/Rh\u00f4ne-Poulenc (UMR41), Rh\u00f4ne-Poulenc Agrochimie, 14\u201320 rue Pierre Baizet, 69263 Lyon cedex 09, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roland","family":"DOUCE","sequence":"additional","affiliation":[{"name":"Laboratoire Mixte CNRS\/Rh\u00f4ne-Poulenc (UMR41), Rh\u00f4ne-Poulenc Agrochimie, 14\u201320 rue Pierre Baizet, 69263 Lyon cedex 09, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/331\/2\/639\/631534\/bj3310639.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/331\/2\/639\/631534\/bj3310639.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T00:31:25Z","timestamp":1637713885000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/331\/2\/639\/33917\/Cystathionine-synthase-from-Arabidopsis-thaliana"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,4,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1998,4,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3310639","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,4,15]]}}}