title: A new biosynthetic route of porphyrin precursors in common between animals and plants.
abstract: An additional enzyme, 4-oxo-5-hydroxyvalerate (OHV) dehydrogenase was identified and characterized. This enzyme catalyzes the conversion of OHV to 4,5-dioxovalerate, a direct precursor of 5-aminolevulinate. The enzyme was partially purified from rat liver supernatant as two isoenzyme (ca. 40,000 and 70,000 dalton). 5-Aminolevulinate was formed from OHV via 4,5-dioxovalerate by this dehydrogenase and alanine-4,5-dioxovalerate aminotransferase (EC 2.6.1.43). This dehydrogenase required NADP or NAD as a hydrogen acceptor. The enzyme was heat sensitive and catalyzed the reaction reversibly. The dehydrogenase was present in the high speed supernatants of liver and kidney of rat, rabbit and human, and that of spinach leaf.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000622:Aminolevulinic Acid / Q000096:biosynthesis; D000818:Animals; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D010944:Plants / Q000201:enzymology*; D011166:Porphyrins / Q000096:biosynthesis; D011773:Pyruvates / Q000096:biosynthesis; D019289:Pyruvic Acid; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D000637:Transaminases / Q000378:metabolism; D014631:Valerates / Q000096:biosynthesis*
chemical_list: D011166:Porphyrins; D011773:Pyruvates; D014631:Valerates; C007509:4,5-dioxovaleric acid; D019289:Pyruvic Acid; D000622:Aminolevulinic Acid; D000429:Alcohol Oxidoreductases; C037795:4-oxo-5-hydroxyvalerate dehydrogenase; D000637:Transaminases; C019687:aminolevulinate aminotransferase