1,4-dihydroxy-2-naphthoate polyprenyltransferase

Class of enzymes 1,4-dihydroxy-2-naphthoate polyprenyltransferase 2.5.1.74 1-4-dihydroxy-2-napthoate (DHNA) polyprenyltransferase (EC 2.5.1.74) is an enzyme that catalyzes the chemical reaction: all-trans-nonaprenyl diphosphate + 1-4-dihydroxy-2-napthoate + H+ demethylmenaquinol-9 + diphosphate + carbon dioxide Hence, the 3 substrates of this enzyme are all-trans-nonaprenyl diphosphate, 1-4-dihydroxy-2-napthoate, and a hydrogen ion, and the three products are demethylmenaquinol-9, diphosphate, and carbon dioxide. However, other substrates this enzyme can use include farnesyl diphosphate or solanesyl diphosphate in replacement of all-trans-nonaprenyl diphosphate. http://www.brenda-enzymes.org/enzyme.php?ecno=2.5.1.74 Information on EC 2.5.1.74 - 1,4-dihydroxy-2-naphthoate polyprenyltransferase BRENDA database 2014 23 December 2014 1-4-dihydroxy-2-napthoate polyprenyltransferase is located at 88 min on the E. coli chromosome while the rest of the genes responsible for the synthesis of menaquinone (Vitamin K) are clustered at 51 min. This enzyme belongs to the transferase family, specifically transferring alkyl or aryl groups other than methyl groups. http://www.enzyme-database.org/ The Enzyme List Class 2 — Transferases ExplorEnz: Enzyme Database 2014 23 December 2014 Other names for the enzyme include 1-4-dihydroxy-2-napthoate octaprenyltransferase, 1-4-dihydroxy-2-napthoate monoprenyltransferase, and MenA. Function 1-4-dihydroxy-2-napthoate polyprenyltransferase is the 8th out of 9 steps in the biosynthesis of menaquinone (Vitamin K), specifically demethylmenaquinol-9 within E. coli. Vitamin K is a cofactor vital for living and functions as one electron transporter in photosynthesis as a redox molecule. Phylloquinone (Vitamin K1): function, enzymes and genes Advances in Botanical Research Fabrice Rébeillé Roland Douce 59 229–61 Academic Press Amsterdam van Oostende C, Widhalm JR, Furt F, Ducluzeau AL, Basset GJ 2011 The reactions this enzyme catalyzes works by taking the soluble bicyclic naphthalenoid compound DHNA and converting it into demethylmenaquinone-9 by attaching a 40 carbon side chain to DHNA. However, this enzyme is unique in the sense that it can put different lengths of carbon side chains onto DHNA to produce different demethylmenaquinols and menaquinols. Suvarna K, Stevenson D, Meganathan R, Hudspeth ME Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli Journal of Bacteriology 180 10 2782–7 May 1998 9573170 10.1128/jb.180.10.2782-2787.1998 107237 left|frameless|1662x1662px Other organisms that contain this pathway include Micrococcus luterus and Mycobacterium tuberculosis. Inhibitors and activators Both E. coli and Micrococcus luterus require Mg2+ to work and a pH of 7 in Micrococcus luterus is optimal. EDTA is also an activating compound for the enzyme in Micrococcus luterus at an optimal concentration of 5mM but once it reaches 20mM it becomes an inhibitor and Mg2+ is required to reactivate it. Enzyme InhibitorsOrganism(R)-1-(4-((3-((4-chlorophenyl)(methoxyimino)methyl)phenoxy)-methyl)piperidin-1-yl)octan-2-yl carbamateMycobacterium tuberculosis(R)-1-(4-((3-(4-chlorobenzoyl)phenoxy)methyl)piperidin-1-yl)-octan-2-yl carbamateMycobacterium tuberculosis(S)-(2-chloro-4-((1-(2-hydroxyoctyl)piperidin-4-yl)methoxy)-phenyl)(4-chlorophenyl)methanoneMycobacterium tuberculosis(S)-1-(4-((3-chloro-4-((4-chlorophenyl)(methoxyimino)methyl)-phenoxy)methyl)piperidin-1-yl)octan-2-yl carbamate Mycobacterium tuberculosis(S)-1-(4-((3-chloro-4-(4-chlorobenzoyl)phenoxy)methyl)-piperidin-1-yl)octan-2-yl carbamateMycobacterium tuberculosisCa2+Micrococcus luterusEDTAMicrococcus luterus Location The location of 1-4-dihydroxy-2-napthoate polyprenyltransferase is within the membrane. thumb|578x578px|Transmembrane domain plot of DHNA polyprenyltransferase showing what parts of the domain are inside and outside of the membrane of a cell.|centre References Category:EC 2.5.1