2.0 2012-05-31 14:01:44 -0600 2015-06-03 15:54:36 -0600 ECMDB04002 M2MDB000550 2-Acetolactate 2-Acetolactate is involved in the butanoate metabolism and pantothenate and CoA biosynthesis pathways. 2-Acetolactic acid C5H8O4 132.1146 132.042258744 2-hydroxy-2-methyl-3-oxobutanoic acid 2-acetyllactic acid CC(=O)C(C)(O)C(O)=O InChI=1S/C5H8O4/c1-3(6)5(2,9)4(7)8/h9H,1-2H3,(H,7,8) NMDWGEGFJUBKLB-UHFFFAOYSA-N Solid Cytoplasm Periplasm logp -0.65 ALOGPS logs 0.33 ALOGPS solubility 2.86e+02 g/l ALOGPS logp -0.28 ChemAxon pka_strongest_acidic 3.45 ChemAxon pka_strongest_basic -4.6 ChemAxon iupac 2-hydroxy-2-methyl-3-oxobutanoic acid ChemAxon average_mass 132.1146 ChemAxon mono_mass 132.042258744 ChemAxon smiles CC(=O)C(C)(O)C(O)=O ChemAxon formula C5H8O4 ChemAxon inchi InChI=1S/C5H8O4/c1-3(6)5(2,9)4(7)8/h9H,1-2H3,(H,7,8) ChemAxon inchikey NMDWGEGFJUBKLB-UHFFFAOYSA-N ChemAxon polar_surface_area 74.6 ChemAxon refractivity 28.59 ChemAxon polarizability 11.82 ChemAxon rotatable_bond_count 2 ChemAxon acceptor_count 4 ChemAxon donor_count 2 ChemAxon physiological_charge -1 ChemAxon formal_charge 0 ChemAxon Butanoate metabolism ec00650 Valine, leucine and isoleucine biosynthesis ec00290 C5-Branched dibasic acid metabolism ec00660 Pantothenate and CoA biosynthesis The CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate. The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate. On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine. Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid. Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine. The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA. Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A. . The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III. The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth. The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06]. PW000828 ec00770 Metabolic Metabolic pathways eco01100 2-Oxopent-4-enoate metabolism The pathway starts with trans-cinnamate interacting with a hydrogen ion, an oxygen molecule, and a NADH through a cinnamate dioxygenase resulting in a NAD and a cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diol which then interact together through a 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase resulting in the release of a hydrogen ion, an NADH molecule and a 2,3 dihydroxy-trans-cinnamate. The second way by which the 2,3 dihydroxy-trans-cinnamate is acquired is through a 3-hydroxy-trans-cinnamate interacting with a hydrogen ion, a NADH and an oxygen molecule through a 3-(3-hydroxyphenyl)propionate 2-hydroxylase resulting in the release of a NAD molecule, a water molecule and a 2,3-dihydroxy-trans-cinnamate. The compound 2,3 dihydroxy-trans-cinnamate then interacts with an oxygen molecule through a 2,3-dihydroxyphenylpropionate 1,2-dioxygenase resulting in a hydrogen ion and a 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. The latter compound then interacts with a water molecule through a 2-hydroxy-6-oxononatrienedioate hydrolase resulting in a release of a hydrogen ion, a fumarate molecule and (2Z)-2-hydroxypenta-2,4-dienoate. The latter compound reacts spontaneously to isomerize into a 2-oxopent-4-enoate. This compound is then hydrated through a 2-oxopent-4-enoate hydratase resulting in a 4-hydroxy-2-oxopentanoate. This compound then interacts with a 4-hydroxy-2-ketovalerate aldolase resulting in the release of a pyruvate, and an acetaldehyde. The acetaldehyde then interacts with a coenzyme A and a NAD molecule through a acetaldehyde dehydrogenase resulting in a hydrogen ion, a NADH and an acetyl-coa which can be incorporated into the TCA cycle PW001890 Metabolic 2-Oxopent-4-enoate metabolism 2 The pathway starts with trans-cinnamate interacting with a hydrogen ion, an oxygen molecule, and a NADH through a cinnamate dioxygenase resulting in a NAD and a Cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol which then interact together through a 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase resulting in the release of a hydrogen ion, an NADH molecule and a 2,3 dihydroxy-trans-cinnamate. The second way by which the 2,3 dihydroxy-trans-cinnamate is acquired is through a 3-hydroxy-trans-cinnamate interacting with a hydrogen ion, a NADH and an oxygen molecule through a 3-(3-hydroxyphenyl)propionate 2-hydroxylase resulting in the release of a NAD molecule, a water molecule and a 2,3-dihydroxy-trans-cinnamate. The compound 2,3 dihydroxy-trans-cinnamate then interacts with an oxygen molecule through a 2,3-dihydroxyphenylpropionate 1,2-dioxygenase resulting in a hydrogen ion and a 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. The latter compound then interacts with a water molecule through a 2-hydroxy-6-oxononatrienedioate hydrolase resulting in a release of a hydrogen ion, a fumarate molecule and (2Z)-2-hydroxypenta-2,4-dienoate. The latter compound reacts spontaneously to isomerize into a 2-oxopent-4-enoate. This compound is then hydrated through a 2-oxopent-4-enoate hydratase resulting in a 4-hydroxy-2-oxopentanoate. This compound then interacts with a 4-hydroxy-2-ketovalerate aldolase resulting in the release of a pyruvate, and an acetaldehyde. The acetaldehyde then interacts with a coenzyme A and a NAD molecule through a acetaldehyde dehydrogenase resulting in a hydrogen ion, a NADH and an acetyl-coa which can be incorporated into the TCA cycle PW002035 Metabolic Specdb::CMs 3070 Specdb::CMs 39108 Specdb::CMs 130949 Specdb::CMs 138683 Specdb::NmrOneD 91832 Specdb::NmrOneD 91833 Specdb::NmrOneD 91834 Specdb::NmrOneD 91835 Specdb::NmrOneD 91836 Specdb::NmrOneD 91837 Specdb::NmrOneD 91838 Specdb::NmrOneD 91839 Specdb::NmrOneD 91840 Specdb::NmrOneD 91841 Specdb::NmrOneD 91842 Specdb::NmrOneD 91843 Specdb::NmrOneD 91844 Specdb::NmrOneD 91845 Specdb::NmrOneD 91846 Specdb::NmrOneD 91847 Specdb::NmrOneD 91848 Specdb::NmrOneD 91849 Specdb::NmrOneD 91850 Specdb::NmrOneD 91851 Specdb::MsMs 25931 Specdb::MsMs 25932 Specdb::MsMs 25933 Specdb::MsMs 32489 Specdb::MsMs 32490 Specdb::MsMs 32491 Specdb::MsMs 2360447 Specdb::MsMs 2360448 Specdb::MsMs 2360449 Specdb::MsMs 2605106 Specdb::MsMs 2605107 Specdb::MsMs 2605108 HMDB06833 22 21 C00900 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 Yurtsever D. (2007). Fatty acid methyl ester profiling of Enterococcus and Esherichia coli for microbial source tracking. M.sc. Thesis. Villanova University: U.S.A Acetolactate synthase isozyme 3 large subunit P00893 ILVI_ECOLI ilvI http://ecmdb.ca/proteins/P00893.xml Acetolactate synthase isozyme 3 small subunit P00894 ILVH_ECOLI ilvH http://ecmdb.ca/proteins/P00894.xml Ketol-acid reductoisomerase P05793 ILVC_ECOLI ilvC http://ecmdb.ca/proteins/P05793.xml Acetolactate synthase isozyme 1 large subunit P08142 ILVB_ECOLI ilvB http://ecmdb.ca/proteins/P08142.xml Acetolactate synthase isozyme 1 small subunit P0ADF8 ILVN_ECOLI ilvN http://ecmdb.ca/proteins/P0ADF8.xml Acetolactate synthase isozyme 2 small subunit P0ADG1 ILVM_ECOLI ilvM http://ecmdb.ca/proteins/P0ADG1.xml 2-Acetolactate + Carbon dioxide <>2 Pyruvic acid R00006 2-Acetolactate + Thiamine pyrophosphate <> 2-(a-Hydroxyethyl)thiamine diphosphate + Pyruvic acid R03050 2-Acetolactate + NADPH + Hydrogen ion <> 2,3-Dihydroxyisovaleric acid + NADP R03051 2 Pyruvic acid > 2-Acetolactate + Carbon dioxide R00006 Pyruvic acid > Carbon dioxide + 2-Acetolactate PW_R005828 2 2-Acetolactate + Carbon dioxide <>2 Pyruvic acid