{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T21:33:23Z","timestamp":1790026403447,"version":"4.0.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1997,4,15]]},"abstract":"<jats:p>Rat liver d-3-phosphoglycerate dehydrogenase was purified to homogeneity and digested with trypsin, and the sequences of two peptides were determined. This sequence information was used to screen a rat hepatoma cDNA library. Among 11 positive clones, two covered the whole coding sequence. The deduced amino acid sequence (533 residues; Mr 56493) shared closer similarity with Bacillus subtilis 3-phosphoglycerate dehydrogenase than with the enzymes from Escherichia coli, Haemophilus influenzae and Saccharomyces cerevisiae. In all cases the similarity was most apparent in the substrate- and NAD+-binding domains, and low or insignificant in the C-terminal domain. A corresponding 2.1 kb mRNA was present in rat tissues including kidney, brain and testis, whatever the dietary status, and also in livers of animals fed a protein-free, carbohydrate-rich diet, but not in livers of control rats, suggesting transcriptional regulation. The full-length rat 3-phosphoglycerate dehydrogenase was expressed in E. coli and purified. The recombinant enzyme and the protein purified from liver displayed hyperbolic kinetics with respect to 3-phosphoglycerate, NAD+ and NADH, but substrate inhibition by 3-phosphohydroxypyruvate was observed; this inhibition was antagonized by salts. Similar properties were observed with a truncated form of 3-phosphoglycerate dehydrogenase lacking the C-terminal domain, indicating that the latter is not implicated in substrate inhibition or in salt effects. By contrast with the bacterial enzyme, rat 3-phosphoglycerate dehydrogenase did not catalyse the reduction of 2-oxoglutarate, indicating that this enzyme is not involved in human d- or l-hydroxyglutaric aciduria.<\/jats:p>","DOI":"10.1042\/bj3230365","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:54:07Z","timestamp":1439243647000},"page":"365-370","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":82,"title":["Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase"],"prefix":"10.1042","volume":"323","author":[{"given":"Younes","family":"ACHOURI","sequence":"first","affiliation":[{"name":"Laboratory of Physiological Chemistry, International Institute of Cellular and Molecular Pathology and Universit\u00e9 Catholique de Louvain, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark H.","family":"RIDER","sequence":"additional","affiliation":[{"name":"Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology and Universit\u00e9 Catholique de Louvain, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emile","family":"VAN SCHAFTINGEN","sequence":"additional","affiliation":[{"name":"Laboratory of Physiological Chemistry, International Institute of Cellular and Molecular Pathology and Universit\u00e9 Catholique de Louvain, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariette","family":"ROBBI","sequence":"additional","affiliation":[{"name":"Laboratory of Physiological Chemistry, International Institute of Cellular and Molecular Pathology and Universit\u00e9 Catholique de Louvain, B-1200 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/323\/2\/365\/624186\/bj3230365.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/323\/2\/365\/624186\/bj3230365.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T00:02:50Z","timestamp":1637712170000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/323\/2\/365\/32668\/Cloning-sequencing-and-expression-of-rat-liver-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,4,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1997,4,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3230365","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,4,15]]}}}