• Source: L-threonine 3-dehydrogenase

    • In enzymology, a 3/info/l" target="_blank">L-3/info/threonine" target="_blank">threonine 3-dehydrogenase (EC 1.1.1.103) is an enzyme that catalyzes the chemical reaction

    3/info/l" target="_blank">L-3/info/threonine" target="_blank">threonine + NAD+



    ⇌


    {\displaystyle \rightleftharpoons }

    3/info/l" target="_blank">L-2-amino-3-oxobutanoate + NADH + H+
    Thus, the two substrates of this enzyme are 3/info/l" target="_blank">L-3/info/threonine" target="_blank">threonine and NAD+, whereas its 3 products are 3/info/l" target="_blank">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 3/info/l" target="_blank">L-3/info/threonine" target="_blank">threonine:NAD+ oxidoreductase. Other names in common use include 3/info/l" target="_blank">L-3/info/threonine" target="_blank">threonine dehydrogenase, 3/info/threonine" target="_blank">threonine 3-dehydrogenase, and 3/info/threonine" target="_blank">threonine dehydrogenase. This enzyme participates in glycine, serine and 3/info/threonine" target="_blank">threonine metabolism.


    Structural studies


    As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2D8A, 2DFV, and 2DQ4.


    References



    Green ML, Elliott WH (1964). "The enzymic formation of aminoacetone from 3/info/threonine" target="_blank">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 3/info/threonine" target="_blank">threonine dehydrogenase". Arch. Biochem. Biophys. 105: 173–8. doi:10.1016/0003-9861(64)90250-4. PMID 14165492.
    Epperly BR, Dekker EE (April 1991). "3/info/l" target="_blank">L-3/info/threonine" target="_blank">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 3/info/l" target="_blank">L-3/info/threonine" target="_blank">threonine 3-dehydrogenase gene is an expressed pseudogene". BMC Genetics. 3: 18. doi:10.1186/1471-2156-3-18. PMC 131051. PMID 12361482.

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