| Version |
2.5 |
| Creation Date |
2008-08-14 18:18:54 |
| Update Date |
2010-07-13 13:37:51 |
| Accession Number |
HMDB06880 |
| Secondary Accession Numbers |
HMDB06947 |
| Common Name |
Acetyl adenylate |
| Description |
Acetyl adenylate is an intermediate in acetyl-CoA synthesis. It is converted from acetate via the enzyme acetyl-CoA synthetase. It is involved in the non-enzymatic acetylation of histones in chromatin (PMID:8619849). In microbes acetyl adenylate also plays a role in the direction of flagellar rotation (PMID:2901103) |
| Synonyms |
- 5'-O-[acetoxy(hydroxy)phosphoryl]adenosine
- Acetyl adenylate
- Acetyl amp
- Acetyladenylate
- [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-yl]methoxy-hydroxy-phosphoryl] acetate
|
| Chemical IUPAC Name |
[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-yl]methoxy-hydroxy-phosphoryl] acetate |
| Chemical Formula |
C12H16N5O8P |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Nucleosides and Nucleoside conjugates
|
| Class |
- Nucleotides
- Purines and Purine Derivatives
|
| Sub Class |
- Miscellaneous nucleosides
|
| Family |
|
| Species |
- secondary alcohol
- 1,2-diol
- primary amine
- primary aromatic amine
- phosphoric acid ester
- aromatic compound
- heterocyclic compound
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
389.258 |
| Monoisotopic Molecular Weight |
389.073639 |
| Isomeric SMILES |
CC(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=CN=C2N |
| Canonical SMILES |
CC(=O)OP(O)(=O)OCC1OC(C(O)C1O)N1C=NC2=C1N=CN=C2N |
| KEGG Compound ID |
C05993  |
| BioCyc ID |
ACETYL_AMP  |
| BiGG ID |
Not Available |
| Wikipedia Link |
Not Available |
| NuGOwiki Link |
HMDB06880  |
| Metagene Link |
HMDB06880  |
| METLIN ID |
Not Available |
| PubChem Compound |
440867  |
| PubChem Substance |
8267  |
| ChEBI ID |
37666  |
| CAS Registry Number |
13015-87-7 |
| InChI Identifier |
InChI=1/C12H16N5O8P/c1-5(18)25-26(21,22)23-2-6-8(19)9(20)12(24-6)17-4-16-7-10(13)14-3-15-11(7)17/h3-4,6,8-9,12,19-20H,2H2,1H3,(H,21,22)(H2,13,14,15)/t6-,8-,9-,12-/m1/s1 |
| Synthesis Reference |
Not Available |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
3.02 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.3 [Predicted by PubChem via XLOGP]; -2.44 [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
Not Available |
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Not Available |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Not Available |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
Not Available |
| Biofluid Location |
Not Available |
| Tissue Location |
Not Available |
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- WEBSTER LT Jr: STUDIES OF THE ACETYL COENZYME A SYNTHETASE REACTION. I. ISOLATION AND CHARACTERIZATION OF ENZYME-BOUND ACETYL ADENYLATE. J Biol Chem. 1963 Dec;238:4010-5. [PubMed
]
- Webster LT Jr: Studies of the acetyl coenzyme A synthetase reaction. V. The requirement for monovalent and divalent cations in partial reactions involving enzyme-bound acetyl adenylate. J Biol Chem. 1967 Mar 25;242(6):1232-40. [PubMed
]
- Hilscher LW, Hanson CD, Russell DH, Raushel FM: Measurement of positional isotope exchange rates in enzyme-catalyzed reactions by fast atom bombardment mass spectrometry: application to argininosuccinate synthetase. Biochemistry. 1985 Oct 8;24(21):5888-93. [PubMed
]
- Schmellenkamp H, Eggerer H: Mechanism of enzymic acetylation of des-acetyl citrate lyase. Proc Natl Acad Sci U S A. 1974 May;71(5):1987-91. [PubMed
]
- Ramponi G, Manao G, Camici G: Nonenzymatic acetylation of histones with acetyl phosphate and acetyl adenylate. Biochemistry. 1975 Jun 17;14(12):2681-5. [PubMed
]
- Camici G, Manao G, Ramponi G: Nonenzymatic reactivation of des-acetyl citrate lyase by acetyl adenylate. First example of enzyme activation by chemotrophic modification. Physiol Chem Phys. 1975;7(5):409-14. [PubMed
]
- Shewmaker CK, Wagner TE: Analysis of binding interactions between histone core complex and simian virus 40 DNA. A comparison of acetylated versus non-acetylated histone core complexes. Eur J Biochem. 1980 Jun;107(2):505-10. [PubMed
]
- Cohen BN, Blue WT, Wagner TE: Chemically induced gene expression. Manipulation of the transforming ability of simian virus 40 minichromatin by specific chemical hyperacetylation of histones H3 and H4. Eur J Biochem. 1980 Jun;107(2):511-8. [PubMed
]
- Krajewski WA, Luchnik AN: Relationship of histone acetylation to DNA topology and transcription. Mol Gen Genet. 1991 Dec;230(3):442-8. [PubMed
]
- Krajewski WA: Effect of nonenzymatic histone acetylation on chromatin high-order folding. Biochem Biophys Res Commun. 1996 Apr 16;221(2):295-9. [PubMed
]
- Wolfe AJ, Conley MP, Berg HC: Acetyladenylate plays a role in controlling the direction of flagellar rotation. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6711-5. [PubMed
]
|
| Metabolic Enzymes |
- Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
- ACSS2 protein
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5271 |
| Enzyme 1 Name |
Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor |
| Enzyme 1 Synonyms |
- Acetate--CoA ligase 2
- Acetyl-CoA synthetase 2
- Acyl- CoA synthetase short-chain family member 1
|
| Enzyme 1 Gene Name |
ACSS1 |
| Enzyme 1 Protein Sequence |
>Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
|
| Enzyme 1 Number of Residues |
689 |
| Enzyme 1 Molecular Weight |
74857 |
| Enzyme 1 Theoretical pI |
7.11 |
| Enzyme 1 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Lipid transport and metabolism |
| Enzyme 1 Specific Function |
Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2) |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
56203089  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9NUB1  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ACS2L_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1439 bp
CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA
|
| Enzyme 1 GenBank Gene ID |
AL035661  |
| Enzyme 1 GeneCard ID |
ACSS1  |
| Enzyme 1 GenAtlas ID |
ACSS1  |
| Enzyme 1 HGNC ID |
HGNC:16091  |
| Enzyme 1 Chromosome Location |
20 |
| Enzyme 1 Locus |
20p11.23-p11.21 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
13088 |
| Enzyme 2 Name |
ACSS2 protein |
| Enzyme 2 Synonyms |
Not Available |
| Enzyme 2 Gene Name |
ACSS2 |
| Enzyme 2 Protein Sequence |
>ACSS2 protein
PMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLK
ELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDL
WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDF
HAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFY
TAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQ
TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMR
TVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA
LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDY
IQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
|
| Enzyme 2 Number of Residues |
534 |
| Enzyme 2 Molecular Weight |
59347 |
| Enzyme 2 Theoretical pI |
5.68 |
| Enzyme 2 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
Not Available |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
Not Available |
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
40226463  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q96FY7  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
Q96FY7_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
Not Available |
| Enzyme 2 GenBank Gene ID |
BC010141  |
| Enzyme 2 GeneCard ID |
Q96FY7  |
| Enzyme 2 GenAtlas ID |
ACSS2  |
| Enzyme 2 HGNC ID |
HGNC:15814  |
| Enzyme 2 Chromosome Location |
Not Available |
| Enzyme 2 Locus |
Not Available |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |