2.0 2012-05-31 13:50:14 -0600 2015-06-03 15:53:56 -0600 ECMDB01339 M2MDB000344 Glutaryl-CoA Glutaryl-coenzyme A (or Glutaryl-CoA) is an intermediate in the metabolism of lysine and tryptophan. Glutaryl-CoA Glutaryl-coenzyme A C26H42N7O19P3S 881.633 881.146902423 5-{[2-(3-{3-[({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-2-hydroxy-3-methylbutanamido}propanamido)ethyl]sulfanyl}-5-oxopentanoic acid 5-({2-[3-(3-{[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-2-hydroxy-3-methylbutanamido)propanamido]ethyl}sulfanyl)-5-oxopentanoic acid 103192-48-9 CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCSC(=O)CCCC(O)=O InChI=1S/C26H42N7O19P3S/c1-26(2,21(39)24(40)29-7-6-15(34)28-8-9-56-17(37)5-3-4-16(35)36)11-49-55(46,47)52-54(44,45)48-10-14-20(51-53(41,42)43)19(38)25(50-14)33-13-32-18-22(27)30-12-31-23(18)33/h12-14,19-21,25,38-39H,3-11H2,1-2H3,(H,28,34)(H,29,40)(H,35,36)(H,44,45)(H,46,47)(H2,27,30,31)(H2,41,42,43)/t14-,19-,20-,21?,25-/m1/s1 SYKWLIJQEHRDNH-KRPIADGTSA-N Solid Cytoplasm Periplasm logp -0.48 ALOGPS logs -2.39 ALOGPS solubility 3.62e+00 g/l ALOGPS logp -5.6 ChemAxon pka_strongest_acidic 0.82 ChemAxon pka_strongest_basic 3.84 ChemAxon iupac 5-{[2-(3-{3-[({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-2-hydroxy-3-methylbutanamido}propanamido)ethyl]sulfanyl}-5-oxopentanoic acid ChemAxon average_mass 881.633 ChemAxon mono_mass 881.146902423 ChemAxon smiles CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCSC(=O)CCCC(O)=O ChemAxon formula C26H42N7O19P3S ChemAxon inchi InChI=1S/C26H42N7O19P3S/c1-26(2,21(39)24(40)29-7-6-15(34)28-8-9-56-17(37)5-3-4-16(35)36)11-49-55(46,47)52-54(44,45)48-10-14-20(51-53(41,42)43)19(38)25(50-14)33-13-32-18-22(27)30-12-31-23(18)33/h12-14,19-21,25,38-39H,3-11H2,1-2H3,(H,28,34)(H,29,40)(H,35,36)(H,44,45)(H,46,47)(H2,27,30,31)(H2,41,42,43)/t14-,19-,20-,21?,25-/m1/s1 ChemAxon inchikey SYKWLIJQEHRDNH-KRPIADGTSA-N ChemAxon polar_surface_area 400.93 ChemAxon refractivity 187.7 ChemAxon polarizability 78.94 ChemAxon rotatable_bond_count 24 ChemAxon acceptor_count 19 ChemAxon donor_count 10 ChemAxon physiological_charge -5 ChemAxon formal_charge 0 ChemAxon Tryptophan metabolism The biosynthesis of L-tryptophan begins with L-glutamine interacting with a chorismate through a anthranilate synthase which results in a L-glutamic acid, a pyruvic acid, a hydrogen ion and a 2-aminobenzoic acid. The aminobenzoic acid interacts with a phosphoribosyl pyrophosphate through an anthranilate synthase component II resulting in a pyrophosphate and a N-(5-phosphoribosyl)-anthranilate. The latter compound is then metabolized by an indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in a 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate. This compound then interacts with a hydrogen ion through a indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase resulting in the release of carbon dioxide, a water molecule and a (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate. The latter compound then interacts with a D-glyceraldehyde 3-phosphate and an Indole. The indole interacts with an L-serine through a tryptophan synthase, β subunit dimer resulting in a water molecule and an L-tryptophan. The metabolism of L-tryptophan starts with L-tryptophan being dehydrogenated by a tryptophanase / L-cysteine desulfhydrase resulting in the release of a hydrogen ion, an Indole and a 2-aminoacrylic acid. The latter compound is isomerized into a 2-iminopropanoate. This compound then interacts with a water molecule and a hydrogen ion spontaneously resulting in the release of an Ammonium and a pyruvic acid. The pyruvic acid then interacts with a coenzyme A through a NAD driven pyruvate dehydrogenase complex resulting in the release of a NADH, a carbon dioxide and an Acetyl-CoA PW000815 ec00380 Metabolic Lysine degradation ec00310 Benzoate degradation via hydroxylation ec00362 Fatty acid metabolism This pathway depicts the degradation of palmitic acid (C16:0). Fatty acid degradation and synthesis are relatively simple processes that are essentially the reverse of each other. The process of fatty acid degradation, also known as Beta-Oxidation, converts an aliphatic compound into a set of activated acetyl units (acetyl CoA) that can be processed by the citric acid cycle. An activated fatty acid is first oxidized to introduce a double bond; the double bond is then hydrated to introduce an oxygen; the alcohol is then oxidized to a ketone; and, finally, the four carbon fragment is cleaved by coenzyme A to yield acetyl CoA and a fatty acid chain two carbons shorter. If the fatty acid has an even number of carbon atoms and is saturated, the process is simply repeated until the fatty acid is completely converted into acetyl CoA units. Fatty acid synthesis is essentially the reverse of this process. Because the result is a polymer, the process starts with monomers—in this case with activated acyl group and malonyl units. The malonyl unit is condensed with the acetyl unit to form a four-carbon fragment. To produce the required hydrocarbon chain, the carbonyl must be reduced. The fragment is reduced, dehydrated, and reduced again, exactly the opposite of degradation, to bring the carbonyl group to the level of a methylene group with the formation of butyryl CoA. Another activated malonyl group condenses with the butyryl unit and the process is repeated until a C16 fatty acid is synthesized. The first step converts the hydroxydecanoyl into a trans 2decenoyl acp through a protein complex conformed of a hydroxomyristoyl dehydratase and a hydroxydecanoyl dehydratase. The second step leads to the production of a cis 3 decenoyl acp through a 3-hydroxydecanoyl acp dehydratase. For the third step the cis 3 decenoyl acp enters a cycle involving a synthase, reductase, dehydratase and an enoyl reductase which in turn produce a cis x enoyl-acp, hydroxy cis x enoyl, trans x-2 cis x enoyl acp and cis x enoyl respectively.This is done until a palmitoleoyl is produce. In said case the pathway procedes in two different directions. It can either produce a palmitoleic acid through a acyl-coa thioesterase, or produce a Vaccenic acid through a different set of reactions. This process is achieved through a 3-oxoacyl acp synthase, a 3-oxoacyl acp reductase, a 3r hydroxymyristoyl dehydratase and an enoyl acp reductase that produces a transition through 3-oxo cis vaccenoyl acp, 3 hydroxy cis vaccenoyl acp, cis vaccen 2 enoyl acp and a cis vaccenoyl acp respectively. At this point it goes through one final reaction to produce a Vaccenic acid, through an acyl-CoA thioesterase PW000796 ec00071 Metabolic Microbial metabolism in diverse environments ec01120 Specdb::EiMs 2549 Specdb::NmrOneD 273538 Specdb::NmrOneD 273539 Specdb::NmrOneD 273540 Specdb::NmrOneD 273541 Specdb::NmrOneD 273542 Specdb::NmrOneD 273543 Specdb::NmrOneD 273544 Specdb::NmrOneD 273545 Specdb::NmrOneD 273546 Specdb::NmrOneD 273547 Specdb::NmrOneD 273548 Specdb::NmrOneD 273549 Specdb::NmrOneD 273550 Specdb::NmrOneD 273551 Specdb::NmrOneD 273552 Specdb::NmrOneD 273553 Specdb::NmrOneD 273554 Specdb::NmrOneD 273555 Specdb::NmrOneD 273556 Specdb::NmrOneD 273557 Specdb::MsMs 27347 Specdb::MsMs 27348 Specdb::MsMs 27349 Specdb::MsMs 33905 Specdb::MsMs 33906 Specdb::MsMs 33907 Specdb::MsMs 1471792 Specdb::MsMs 1471793 Specdb::MsMs 1471794 Specdb::MsMs 1471795 Specdb::MsMs 1471796 Specdb::MsMs 1471797 Specdb::MsMs 1471798 Specdb::MsMs 1471799 Specdb::MsMs 1471800 Specdb::MsMs 1471801 Specdb::MsMs 1471802 Specdb::MsMs 1471803 Specdb::MsMs 1471804 Specdb::MsMs 1471805 Specdb::MsMs 1471806 Specdb::MsMs 1471807 Specdb::MsMs 1471808 Specdb::MsMs 1471809 Specdb::MsMs 1471810 HMDB01339 439252 388388 C00527 15524 GLUTARYL-COA Glutaryl-CoA Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. 22080510 Corral I, Martinez Castrillo JC, Martinez-Pardo M, Gimeno A: [Glutaric aciduria type I: diagnosis in adulthood and phenotypic variability] Neurologia. 2001 Oct;16(8):377-80. 11738016 Mahfoud A, Dominguez CL, Rizzo C, Ribes A: [In utero macrocephaly as clinical manifestation of glutaric aciduria type I. Report of a novel mutation] Rev Neurol. 2004 Nov 16-30;39(10):939-42. 15573311 Hyman DB, Tanaka K: Specific glutaryl-CoA dehydrogenating activity is deficient in cultured fibroblasts from glutaric aciduria patients. J Clin Invest. 1984 Mar;73(3):778-84. 6423663 2-oxoglutarate dehydrogenase E1 component P0AFG3 ODO1_ECOLI sucA http://ecmdb.ca/proteins/P0AFG3.xml Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex P0AFG6 ODO2_ECOLI sucB http://ecmdb.ca/proteins/P0AFG6.xml Oxoadipic acid + Coenzyme A + NAD <> Glutaryl-CoA + Carbon dioxide + NADH + Hydrogen ion R01933 Glutaryl-CoA + Enzyme N6-(dihydrolipoyl)lysine <> Coenzyme A + [Dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine R02571 Glutaryl-CoA > Crotonoyl-CoA + Carbon dioxide PW_R002483 Oxoadipic acid + Coenzyme A + NAD <> Glutaryl-CoA + Carbon dioxide + NADH + Hydrogen ion