This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-threonine:NAD+ oxidoreductase. Other names in common use include L-threonine dehydrogenase, threonine 3-dehydrogenase, and threonine dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism.
Structural studiesedit
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2D8A, 2DFV, and 2DQ4.
Referencesedit
Green ML, Elliott WH (1964). "The enzymic formation of aminoacetone from threonine and its further metabolism". Biochem. J. 92 (3): 537–49. doi:10.1042/bj0920537. PMC1206098. PMID 4284408.
Epperly BR, Dekker EE (April 1991). "L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies". The Journal of Biological Chemistry. 266 (10): 6086–92. doi:10.1016/S0021-9258(18)38087-6. PMID 2007567.
Edgar AJ (October 2002). "The human L-threonine 3-dehydrogenase gene is an expressed pseudogene". BMC Genetics. 3: 18. doi:10.1186/1471-2156-3-18. PMC131051. PMID 12361482.
threonine, dehydrogenase, enzymology, enzyme, that, catalyzes, chemical, reaction, homotetramer, thermus, thermophilusidentifiersec, 103cas, 9067, 6databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabolic, pathwaypriamp. In enzymology a L threonine 3 dehydrogenase EC 1 1 1 103 is an enzyme that catalyzes the chemical reactionL threonine 3 dehydrogenaseL threonine 3 dehydrogenase homotetramer Thermus thermophilusIdentifiersEC no 1 1 1 103CAS no 9067 99 6DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins L Threonine dehydrogenaseIdentifiersSymbolTDHNCBI gene157739HGNC15547RefSeqNM 152566UniProtQ8IZJ6Other dataEC number1 1 1 103LocusChr 8 p23 1Search forStructuresSwiss modelDomainsInterPro L threonine NAD displaystyle rightleftharpoons L 2 amino 3 oxobutanoate NADH H Thus the two substrates of this enzyme are L threonine and NAD whereas its 3 products are L 2 amino 3 oxobutanoate NADH and H This enzyme belongs to the family of oxidoreductases specifically those acting on the CH OH group of donor with NAD or NADP as acceptor The systematic name of this enzyme class is L threonine NAD oxidoreductase Other names in common use include L threonine dehydrogenase threonine 3 dehydrogenase and threonine dehydrogenase This enzyme participates in glycine serine and threonine metabolism Structural studies editAs of late 2007 3 structures have been solved for this class of enzymes with PDB accession codes 2D8A 2DFV and 2DQ4 References editGreen ML Elliott WH 1964 The enzymic formation of aminoacetone from threonine and its further metabolism Biochem J 92 3 537 49 doi 10 1042 bj0920537 PMC 1206098 PMID 4284408 Hartshorne D Greenberg DM 1964 Studies on liver threonine dehydrogenase Arch Biochem Biophys 105 173 8 doi 10 1016 0003 9861 64 90250 4 PMID 14165492 Epperly BR Dekker EE April 1991 L threonine dehydrogenase from Escherichia coli Identification of an active site cysteine residue and metal ion studies The Journal of Biological Chemistry 266 10 6086 92 doi 10 1016 S0021 9258 18 38087 6 PMID 2007567 Edgar AJ October 2002 The human L threonine 3 dehydrogenase gene is an expressed pseudogene BMC Genetics 3 18 doi 10 1186 1471 2156 3 18 PMC 131051 PMID 12361482 Portal nbsp Biology This EC 1 1 1 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title L threonine 3 dehydrogenase amp oldid 1188035027, wikipedia, wiki, book, books, library,
