1,4-dihydroxy-2-naphthoyl-CoA hydrolase

Class of enzymes 1,4-dihydroxy-2-naphthoyl-CoA hydrolase 3.1.2.28 The enzyme 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (EC 3.1.2.28; systematic name 1,4-dihydroxy-2-naphthoyl-CoA hydrolase)3.1.2.28 catalyses the following reaction: 70% 1,4-dihydroxy-2-naphthoyl-CoA H2O class=skin-invert-image coenzyme A + Q27102818 (1) 2 The enzyme characterised from plants including Rubia tinctorum hydrolyses 1,4-dihydroxy-2-naphthoyl-CoA to coenzyme A and 1,4-dihydroxy-2-naphthoic acid (1), which form the thioester in the starting material. 1,4-naphthoquinone, an intermediate in juglone (5-hydroxy-1,4-naphthoquinone) biosynthesis Muller, W Leistner, E Phytochemistry 1976 15 3 407–410 10.1016/s0031-9422(00)86833-8 1976PChem..15..407M Quantitative assessment of metabolic flux by 13C NMR analysis. Biosynthesis of anthraquinones in Rubia tinctorum Eichinger D, Bacher A, Zenk MH, Eisenreich W J. Am. Chem. Soc. 1999 121 33 7469–7475 10.1021/ja990622o 1999JAChS.121.7469E A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1 Widhalm, J.R. van Oostende, C. Furt, F. Basset, G.J. Proc. Natl. Acad. Sci. USA 2009 106 14 5599–5603 19321747 10.1073/pnas.0900738106 2660889 2009PNAS..106.5599W http://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1033&context=plantscifacpub free This enzyme participates in the biosynthesis of juglone, phylloquinone, and several plant pigments. Its structure contains a HotDog domain.Caswell Benjamin T. De Carvalho Caio C. Nguyen Hung Roy Monikrishna Nguyen Tin Cantu David C. Thioesterase enzyme families: Functions, structures, and mechanisms Protein Science 2022 31 3 652–676 10.1002/pro.4263 34921469 8862431 References External links 1,4-dihydroxy-2-naphthoyl-CoA+hydrolase Biology no Category:EC 3.1.2