2.02012-05-31 09:55:42 -06002015-09-13 12:56:05 -0600ECMDB00034M2MDB000010AdenineAdenine is a purine base. Adenine is found in both DNA and RNA. Adenine is a fundamental component of adenine nucleotides. Adenine forms adenosine, a nucleoside, when attached to ribose, and deoxyadenosine when attached to deoxyribose; it forms adenosine triphosphate (ATP), a nucleotide, when three phosphate groups are added to adenosine. Adenosine triphosphate is used in cellular metabolism as one of the basic methods of transferring chemical energy between chemical reactions.1,6-Dihydro-6-iminopurine1H-Purin-6-amine1H-Purine-6-amine3,6-Dihydro-6-iminopurine6-Amino-1H-purine6-Amino-3H-purine6-Amino-7H-purine6-Amino-9H-purine6-Amino-Purine6-Aminopurine9H-Purin-6-amine9H-Purin-6-yl-amin9H-Purin-6-ylamine9H-Purine-6-amineAdeAdeninAdenineAdeninimineVitamin B4C5H5N5135.1267135.0544951857H-purin-6-aminevitamin B473-24-5NC1=C2NC=NC2=NC=N1InChI=1S/C5H5N5/c6-4-3-5(9-1-7-3)10-2-8-4/h1-2H,(H3,6,7,8,9,10)GFFGJBXGBJISGV-UHFFFAOYSA-NSolidCytosolExtra-organismPeriplasmlogp-0.38logs-1.07solubility1.15e+01 g/lmelting_point360 oClogp-0.57pka_strongest_acidic10.29pka_strongest_basic3.64iupac7H-purin-6-amineaverage_mass135.1267mono_mass135.054495185smilesNC1=C2NC=NC2=NC=N1formulaC5H5N5inchiInChI=1S/C5H5N5/c6-4-3-5(9-1-7-3)10-2-8-4/h1-2H,(H3,6,7,8,9,10)inchikeyGFFGJBXGBJISGV-UHFFFAOYSA-Npolar_surface_area80.48refractivity38.22polarizability12.29rotatable_bond_count0acceptor_count4donor_count2physiological_charge0formal_charge0Purine metabolismec00230Cysteine and methionine metabolismec00270Pantothenate and CoA biosynthesisThe 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].PW000828ec00770MetabolicPhosphonate and phosphinate metabolismec00440Two-component systemec02020Metabolic pathwayseco01100Collection of Reactions without pathwaysPW001891MetabolicQuorum SensingBacterial Autoinducer 2 (AI-2) mediates the quorum sensing 2 system. AI-2 is catalyzed by the luxS enzyme. This enzyme is found in E.coli and S.typhimurium.
In E. coli and most pathogenic bacteria that form AI-2 are spontaneous transformations that include cyclization to (2R,4S)-2-methyl-2,4-dihydroxydihydrofuran-3-one and hydration to the final autoinducer (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran. This product is released from the cell through the AI-2 transporter (tqsA).
As the level of AI-2 increases, other cells detect it and import it through the autoinducer-2 ABC transporter (lsrACDB). AI-2 is then degraded in the cells by phosphorylating the AI-2 which is then isomerized to P-HPD which follows by the transfer of and acetyl group to coenzyme A and releases dihydroxyacetone phosphatePW000836SignalingS-adenosyl-L-methionine biosynthesisS-adenosyl-L-methionine biosynthesis(SAM) is synthesized in the cytosol of the cell from L-methionine and ATP. This reaction is catalyzed by methionine adenosyltransferase. L methione is taken up from the environment through a complex reaction coupled transport and then proceeds too synthesize the s adenosylmethionine through a adenosylmethionine synthase. The S-adenosylmethionine then interacts with a hydrogen ion through a adenosylmethionine decarboxylase resulting in a carbon dioxide and a S-adenosyl 3-methioninamine.This compound interacts with a putrescine through a spermidine synthase resulting in a spermidine, a hydrogen ion and a S-methyl-5'-thioadenosine. The latter compound is degraded by interacting with a water molecule through a 5' methylthioadenosine nucleosidase resulting in a adenine and a S-methylthioribose which is then release into the environmentPW000837MetabolicpreQ0 metabolismPreQ0 or 7-cyano-7-carbaguanine is biosynthesized by degrading GTP.
GTP first interacts with water through a GTP cyclohydrolase resulting in the release of a formate, a hydrogen ion and a 7,8-dihydroneopterin 3'-triphosphate. The latter compound then interacts with water through a 6-carboxy-5,6,7,8-tetrahydropterin synthase resulting in a acetaldehyde, triphosphate, 2 hydrogen ion and 6-carboxy-5,6,7,8-tetrahydropterin. The latter compound then reacts spontaneously with a hydrogen ion resulting in the release of a ammonium molecule and a 7-carboxy-7-deazaguanine. This compound then interacts with ATP and ammonium through 7-cyano-7-deazaguanine synthase resulting in the release of water, phosphate, ADP, hydrogen ion and a 7-cyano-7-carbaguanine.
The degradation of 7-cyano-7-deazaguanine can lead to produce a preQ1 or a queuine by reacting with 3 hydrogen ions and 2 NADPH through a 7-cyano-7-deazaguanine reductase. PreQ1 then interacts with a guanine 34 in tRNA through a tRNA-guanine transglycosylase resulting in a release of a guanine and a 7-aminomethyl-7-deazaguanosine 34 in tRNA. This nucleic acid then interacts with SAM through a S-adenosylmethionine tRNA ribosyltransferase-isomerase resulting in a release of a hydrogen ion, L-methionine, adenine and an epoxyqueuosinePW001893MetabolicCitrate lyase activationThe citrate lyase activation starts with a 3-dephospho-CoA reacting with ATP and a hydrogen ion through a triphosphoribosyl-dephospho-CoA synthase resulting in a adenine and a 2'-(5'-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA. The latter compound in turn reacts with with a citrate lyase acyl-carrier protein through a apo-citrate lyase phosphoribosyl-dephospho-CoA transferase resulting in the release of a pyrophosphate and a hydrogen ion and a holo citrate lyase acyl-carrier protein.This protein complex can either react with a hydrogen ion and a acetate resulting in the release of a water and an acetyl-holo citrate lyase acyl-carrier protein.
The holo acyl-carrier protein creacts with an ATP and an acetate through a citrate lyase synthase resulting in the release of an AMP, a pyrophosphate and an acetyl-holo citrate lyase acyl-ccarrier protein.
The holo citrate lyase acyl-carrier protein can also interact with an S-acetyl phosphopantethiene resulting in the release of a 4-phosphopantethiene and an acetyl-holo citrate lyase acyl-carrier protein.PW002075Metabolicadenine and adenosine salvage IThe salvage of adenine begins with adenine being transporter into the cytosol through a adeP hydrogen symporter. Once in the cytosol adenine is degraded by reacting with a ribose-1-phosphate through an adenosine phosphorylase resulting in the release of a phosphate and adenosine. Adenosine is then deaminated by reacting with water, a hydrogen ion and an adenosine deaminase resulting in the release of an ammonium and a inosine . Inosine then reacts with a phosphate through a inosine phosphorylase resulting in the release of a ribose 1-phosphate and a hypoxanthine. Hypoxanthine reacts with a PRPP through a hypoxanthine phosphoribosyltransferase resulting in the release of a pyrophosphate and a IMP molecule.PW002069Metabolicadenine and adenosine salvage IIThe salvage of adenine begins with adenine being transporter into the cytosol through a adeP hydrogen symporter. Once in the cytosol adenine is degraded by reacting with a ribose-1-phosphate through an adenosine phosphorylase resulting in the release of a phosphate and adenosine. Adenosine is then deaminated by reacting with water, a hydrogen ion and an adenosine deaminase resulting in the release of an ammonium and a inosine . Inosine can then be phosphorylated through an ATP driven inosine kinase resulting in the release of an ADP, a hydrogen ion and a IMPPW002071Metabolicadenine and adenosine salvage IIIAdenosine is first incorporated into the cytosol through either a nupG or a nupC transporter. Once in the cytosol, adenosine is degraded into adenine by reacting with a water and a adenosine nucleosidase, releasing a D-ribofuranose and a adenine. The adenine then reacts with a PRPP through a adenine phosphoribosyltransferase resulting in the release of a pyrophosphate and an AMPPW002072Metabolicmethylphosphonate degradation IThe pathway of methylphosphonate degradation starts with methylphosphonate being degrade by an ATP driven methylphosphonate degradation complex resulting in a alpha-D-ribose-1-methylphosphonate-5-triphosphate. This compound in turn is degraded by a water driven RPnTP hydrolase resulting in the release of a hydrogen ion, a pyrophosphate and a alpha-Dribose-1-methylphosphonate 5-phosphate. The latter compound is then involved with a carbon-phosphorous lyase resulting in the release of a methane and a 5-phospho-alpha-D-ribose 1,2-cyclic phosphate. This compound in turn gets degraded by a water driven 5-phospho-alpha-D-ribosyl 1,2-cyclic phosphate phosphodiesterase resulting in the release of a hydrogen ion and a alpha-D-ribose 1,5-biphosphate.PW002065Metabolicpurine deoxyribonucleosides degradationPW002077Metabolicpurine ribonucleosides degradationPurine ribonucleoside degradation leads to the production of alpha-D-ribose-1-phosphate.
Xanthosine is transported into the cytosol through a xapB. Once in the cytosol xanthosine interacts with phosphate through a xanthosine phosphorylase resulting in the release of a xanthine and a alpha-D-ribose-1-phosphate.
Adenosine is transported through a nupC or a nupG transporter, once inside the cytosol it can either react with a phosphate through a adenosine phosphorylase resultin in the release of a adenine and an alpha-D-ribose-1-phosphate. Adenosine reacts with water and hydrogen ion through a adenosine deaminase resulting in the release of ammonium and inosine. Inosine reacts with phosphate through a inosine phosphorylase resulting in the release of a hypoxanthine and an alpha-D-ribose-1-phosphate.
Guanosine reacts with a phosphate through a guanosine phosphorylase resulting in the release of a guanine and a alpha-D-ribose-1-phosphate.PW002076MetabolicS-adenosyl-L-methionine cycleThe S-adenosyl-L-methionine cycle starts with S-adenosyl-L-methionine reacting with (a demethylated methyl donor ) dimethylglycine resulting in the release of a hydrogen ion, a betain (a methylated methyl donor) and a S-adenosyl-L-homocysteine. The s-adenosyl-L-homocysteine reacts with a water molecule through a S-adenosylhomocysteine nucleosidase resulting in the release of a adenine and a ribosyl-L-homocysteine. This compound in turn reacts with a s-ribosylhomocysteine lyase resulting in the release of a l-homocysteine and a autoinducer 2. The L-homocysteine reacts with a N5-methyl-tetrahydropteroyl tri-L-glutamate through a methionine synthase resulting in the release of a tetrahydropteroyl tri-L-glutamate and a methione. The methionine in turn reacts with a water molecule and ATP molecule through a methionine adenosyltransferase resulting in the release of a diphosphate, a phosphate and a s-adenosyl-L-methionine.PW002080MetabolicSpermidine biosynthesis and metabolismSpermidine metabolism starts with S-adenosyl-L-methionine reacting with a hydrogen ion through a adenosylmethionine decarboxylase resulting in the release of a carbon dioxide and a S-adenosyl 3-(methylthio)propylamine. The later compound in turn reacts with putrescine resulting in the release of a hydrogen ion, a spermidine and a S-methyl-5'-thioadenosine. S-methyl-5'-thioadenosine in turn reacts with a water molecule through a 5-methylthioadenosine nucleosidase resulting in the release of a adenine and a S-methyl-5-thio-D-ribose which in in turn is released into the environment. PW002085Metabolicmethylphosphonate degradationPWY0-1533adenine and adenosine salvage IIIPWY-6609adenine and adenosine salvage VPWY-6611purine ribonucleosides degradation to ribose-1-phosphatePWY0-1296adenine and adenosine salvage IIPWY-6605purine deoxyribonucleosides degradationPWY0-1297queuosine biosynthesisPWY-67002'-(5'-phosphoribosyl)-3'-dephospho-CoA biosynthesis I (citrate lyase)P2-PWY<i>S</i>-adenosyl-L-methionine cycle IPWY-6151autoinducer AI-2 biosynthesis IPWY-6153adenosine nucleotides degradation IIIPWY-6617<i>S</i>-methyl-5'-thioadenosine degradation IVPWY0-1391Specdb::CMs288Specdb::CMs289Specdb::CMs290Specdb::CMs1580Specdb::CMs1634Specdb::CMs1639Specdb::CMs3464Specdb::CMs30172Specdb::CMs30472Specdb::CMs30821Specdb::CMs30964Specdb::CMs30965Specdb::CMs30966Specdb::CMs32043Specdb::CMs155635Specdb::EiMs411Specdb::NmrOneD1043Specdb::NmrOneD2599Specdb::NmrOneD3302Specdb::NmrOneD5412Specdb::NmrOneD5413Specdb::NmrOneD5414Specdb::NmrOneD5415Specdb::NmrOneD5416Specdb::NmrOneD5417Specdb::NmrOneD5418Specdb::NmrOneD5419Specdb::NmrOneD5420Specdb::NmrOneD5421Specdb::NmrOneD5422Specdb::NmrOneD5423Specdb::NmrOneD5424Specdb::NmrOneD5425Specdb::NmrOneD5426Specdb::NmrOneD5427Specdb::NmrOneD5428Specdb::NmrOneD5429Specdb::NmrOneD5430Specdb::NmrOneD5431Specdb::MsMs2622Specdb::MsMs2628Specdb::MsMs2629Specdb::MsMs438799Specdb::MsMs439015Specdb::MsMs439016Specdb::MsMs440031Specdb::MsMs440100Specdb::MsMs2226196Specdb::MsMs2226223Specdb::MsMs2228463Specdb::MsMs2228526Specdb::MsMs2228579Specdb::MsMs2228590Specdb::MsMs2230819Specdb::MsMs2230838Specdb::MsMs2230891Specdb::MsMs2231003Specdb::MsMs2233177Specdb::MsMs2233440Specdb::MsMs2235516Specdb::MsMs2256339Specdb::MsMs2258262Specdb::MsMs57Specdb::MsMs58Specdb::NmrTwoD938Specdb::NmrTwoD1101HMDB00034190185C0014716708ADENINEANEAdenineKeseler, I. 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Journal of the Chemical Society (1943), 386-7.http://hmdb.ca/system/metabolites/msds/000/000/024/original/HMDB00034.pdf?1358893297Hypoxanthine phosphoribosyltransferaseP0A9M2HPRT_ECOLIhpthttp://ecmdb.ca/proteins/P0A9M2.xmlPurine nucleoside phosphorylase deoD-typeP0ABP8DEOD_ECOLIdeoDhttp://ecmdb.ca/proteins/P0ABP8.xmlAMP nucleosidaseP0AE12AMN_ECOLIamnhttp://ecmdb.ca/proteins/P0AE12.xml5'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseP0AF12MTNN_ECOLImtnNhttp://ecmdb.ca/proteins/P0AF12.xmlRiboflavin synthase alpha chainP0AFU8RISA_ECOLIribEhttp://ecmdb.ca/proteins/P0AFU8.xmlNon-specific ribonucleoside hydrolase rihCP22564RIHC_ECOLIrihChttp://ecmdb.ca/proteins/P22564.xmlAdenine deaminaseP31441ADEC_ECOLIadehttp://ecmdb.ca/proteins/P31441.xmlPyrimidine-specific ribonucleoside hydrolase rihBP33022RIHB_ECOLIrihBhttp://ecmdb.ca/proteins/P33022.xmlAdenine phosphoribosyltransferaseP69503APT_ECOLIapthttp://ecmdb.ca/proteins/P69503.xml2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthaseP77231CITG_ECOLIcitGhttp://ecmdb.ca/proteins/P77231.xmlAlpha-ketoglutarate-dependent dioxygenase AlkBP05050alkBhttp://ecmdb.ca/proteins/P05050.xmlS-adenosylmethionine:tRNA ribosyltransferase-isomeraseP0A7F9QUEA_ECOLIqueAhttp://ecmdb.ca/proteins/P0A7F9.xmlAlpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnLP16679PHNL_ECOLIphnLhttp://ecmdb.ca/proteins/P16679.xmlAlpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnIP16687PHNI_ECOLIphnIhttp://ecmdb.ca/proteins/P16687.xmlAlpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnHP16686PHNH_ECOLIphnHhttp://ecmdb.ca/proteins/P16686.xmlAlpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnGP16685PHNG_ECOLIphnGhttp://ecmdb.ca/proteins/P16685.xmlXanthine permease XanPP0AGM9XANP_ECOLIxanPhttp://ecmdb.ca/proteins/P0AGM9.xmlProbable adenine permease PurPP31466PURP_ECOLIpurPhttp://ecmdb.ca/proteins/P31466.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlAlpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnGP16685PHNG_ECOLIphnGhttp://ecmdb.ca/proteins/P16685.xmlAdenosine + Water > Adenine + RiboseR01245S-Adenosylhomocysteine + Water <> Adenine + S-Ribosyl-L-homocysteineR00194ADENOSYLHOMOCYSTEINE-NUCLEOSIDASE-RXN5'-Methylthioadenosine + Water > 5-Methylthioribose + AdenineR01401METHYLTHIOADENOSINE-NUCLEOSIDASE-RXN5'-Deoxyadenosine + Water > 5'-Deoxyribose + AdenineRXN0-6550Adenine + Phosphoribosyl pyrophosphate <> Adenosine monophosphate + PyrophosphateR00190ADENPRIBOSYLTRAN-RXNAdenosine triphosphate + Dephospho-CoA > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine2.7.8.25-RXNAdenosine monophosphate + Water <> Adenine + D-Ribose-5-phosphateR00182AMP-NUCLEOSID-RXNAdenine + Hydrogen ion + Water > Hypoxanthine + AmmoniumAdenosine + Phosphate <> Adenine + Ribose-1-phosphateADENPHOSPHOR-RXNDeoxyadenosine + Phosphate <> Deoxyribose 1-phosphate + AdenineR02557Adenosine monophosphate + Pyrophosphate <> Adenine + Phosphoribosyl pyrophosphateR00190Adenine + Water <> Hypoxanthine + AmmoniaR01244Adenosine + Water <> Adenine + RiboseR012455'-Methylthioadenosine + Water <> Adenine + 5-MethylthioriboseR01401Adenosine + Phosphate <> Adenine + alpha-D-Ribose 1-phosphateR01561Methylphosphonate + Adenosine triphosphate > α-D-ribose-1-methylphosphonate-5-triphosphate + AdenineRXN0-6732Hydrogen ion + Dephospho-CoA + Adenosine triphosphate > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine2.7.8.25-RXNWater + Adenine > Ammonia + HypoxanthineR01244ADENINE-DEAMINASE-RXNAdenosine + Water > D-ribose + AdenineADENOSINE-NUCLEOSIDASE-RXNS-Ribosyl-L-homocysteine + Adenine < S-Adenosylhomocysteine + WaterR00194ADENOSYLHOMOCYSTEINE-NUCLEOSIDASE-RXNPyrophosphate + Adenosine monophosphate < Phosphoribosyl pyrophosphate + AdenineADENPRIBOSYLTRAN-RXNWater + Adenosine monophosphate > D-Ribose-5-phosphate + AdenineAMP-NUCLEOSID-RXNDeoxyadenosine + Phosphate <> Adenine + deoxyribose-1-phosphateDEOXYADENPHOSPHOR-RXNN1-Methyladenine + Oxygen + Oxoglutaric acid > Hydrogen ion + Adenine + Carbon dioxide + Formaldehyde + Succinic acidRXN0-9841-Ethyladenine + Oxygen + Oxoglutaric acid > Adenine + Carbon dioxide + Acetaldehyde + Succinic acidRXN0-986Adenosine monophosphate + Pyrophosphate > Adenine + Phosphoribosyl pyrophosphateS-Adenosylhomocysteine + Water > S-Ribosyl-L-homocysteine + Adenine5'-Methylthioadenosine + Water > S-methyl-5-thio-D-ribose + AdenineS-adenosyl-L-methionine + 7-Aminomethyl-7-deazaguanosine > L-Methionine + Adenine + epoxyqueuosineAdenosine triphosphate + Dephospho-CoA <> 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + AdenineR09675 Adenosine triphosphate + Methylphosphonate <> alpha-D-Ribose 1-methylphosphonate 5-triphosphate + AdenineR10185 S-Adenosylhomocysteine + Water > Adenine + S-ribosyl-L-homocysteine + S-ribosyl-L-homocysteinePW_R0030675'-S-methyl-5'-thioadenosine + Water > 5-Methylthioribose + AdeninePW_R0051677-aminomethyl-7-deazaguanosine34 in tRNA + S-adenosyl-L-methionine > Hydrogen ion + L-Methionine + Adenine + epoxyqueuosinePW_R005185S-Adenosylhomocysteine + Water > AdeninePW_R006077Adenosine + Water > beta-D-ribofuranose + AdeninePW_R006054Methylphosphonate + Adenosine triphosphate > Adenine + alpha-D-Ribose 1-methylphosphonate 5-triphosphatePW_R006035Adenine + Ribose-1-phosphate > Phosphate + AdenosinePW_R006047Adenosine + Phosphate > Adenine + Ribose-1-phosphatePW_R006066Deoxyadenosine + Phosphate > Adenine + Deoxyribose 1-phosphatePW_R006069Adenine + Phosphoribosyl pyrophosphate > Pyrophosphate + Adenosine monophosphatePW_R006055Adenosine triphosphate + Methylphosphonate <> alpha-D-Ribose 1-methylphosphonate 5-triphosphate + AdenineAdenosine monophosphate + Water <> Adenine + D-Ribose-5-phosphateGutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseShake flask and filter culture1.47uM0.037 oCK12 NCM3722Mid-Log Phase58800Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolShake flask and filter culture1.47uM0.037 oCK12 NCM3722Mid-Log Phase58800Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateShake flask and filter culture1.47uM0.037 oCK12 NCM3722Mid-Log Phase58800Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.1956162148 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h102.0uM0.037 oCBW25113Stationary Phase, glucose limited4080000Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597.17379776Luria-Bertani (LB) mediaShake flask34.5uMtrue10.037 oCBL21 DE3Stationary phase cultures (overnight culture)13800040000Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911