Adenylosuccinate synthetase

NameAdenylosuccinate synthetase
Synonyms
  • 6.3.4.4
  • adeK
  • AMPSase
  • IMP--aspartate ligase
Gene NamepurA
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019120|Adenylosuccinate synthetase
MGNNVVVLGTQWGDEGKGKIVDLLTERAKYVVRYQGGHNAGHTLVINGEKTVLHLIPSGI
LRENVTSIIGNGVVLSPAALMKEMKELEDRGIPVRERLLLSEACPLILDYHVALDNAREK
ARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFDKETFAEKLKEVMEYHNFQLVNYYKAE
AVDYQKVLDDTMAVADILTSMVVDVSDLLDQARQRGDFVMFEGAQGTLLDIDHGTYPYVT
SSNTTAGGVATGSGLGPRYVDYVLGILKAYSTRVGAGPFPTELFDETGEFLCKQGNEFGA
TTGRRRRTGWLDTVAVRRAVQLNSLSGFCLTKLDVLDGLKEVKLCVAYRMPDGREVTTTP
LAADDWKGVEPIYETMPGWSESTFGVKDRSGLPQAALNYIKRIEELTGVPIDIISTGPDR
TETMILRDPFDA
Number of residuesNone
Molecular Weight47344.585
Theoretical pI5.13
GO Classification
Functions
  • GTP binding
  • magnesium ion binding
  • adenylosuccinate synthase activity
Processes
  • 'de novo' AMP biosynthetic process
  • cellular response to DNA damage stimulus
  • IMP metabolic process
  • purine nucleotide biosynthetic process
  • nucleobase-containing small molecule interconversion
  • adenosine biosynthetic process
Components
  • cytoplasm
  • membrane
  • cytosol
General FunctionMagnesium ion binding
Specific FunctionPlays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP0A7D4
UniProtKB Entry Name
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0019121|Adenylosuccinate synthetase (purA)
ATGGGTAACAACGTCGTCGTACTGGGCACCCAATGGGGTGACGAAGGTAAAGGTAAGATC
GTCGATCTTCTGACTGAACGGGCTAAATATGTTGTACGCTACCAGGGCGGTCACAACGCA
GGCCATACTCTCGTAATCAACGGTGAAAAAACCGTTCTCCATCTTATTCCATCAGGTATT
CTCCGCGAGAATGTAACCAGCATCATCGGTAACGGTGTTGTGCTGTCTCCGGCCGCGCTG
ATGAAAGAGATGAAAGAACTGGAAGACCGTGGCATCCCCGTTCGTGAGCGTCTGCTGCTG
TCTGAAGCATGTCCGCTGATCCTTGATTATCACGTTGCGCTGGATAACGCGCGTGAGAAA
GCGCGTGGCGCGAAAGCGATCGGCACCACCGGTCGTGGTATCGGGCCTGCTTATGAAGAT
AAAGTAGCACGTCGCGGTCTGCGTGTTGGCGACCTTTTCGACAAAGAAACCTTCGCTGAA
AAACTGAAAGAAGTGATGGAATATCACAACTTCCAGTTGGTTAACTACTACAAAGCTGAA
GCGGTTGATTACCAGAAAGTTCTGGATGATACGATGGCTGTTGCCGACATCCTGACTTCT
ATGGTGGTTGACGTTTCTGACCTGCTCGACCAGGCGCGTCAGCGTGGCGATTTCGTCATG
TTTGAAGGTGCGCAGGGTACGCTGCTGGATATCGACCACGGTACTTATCCGTACGTAACT
TCTTCCAACACCACTGCTGGTGGCGTGGCGACCGGTTCCGGCCTGGGCCCGCGTTATGTT
GATTACGTTCTGGGTATCCTCAAAGCTTACTCCACTCGTGTAGGTGCAGGTCCGTTCCCG
ACCGAACTGTTTGATGAAACTGGCGAGTTCCTCTGCAAGCAGGGTAACGAATTCGGCGCA
ACTACGGGGCGTCGTCGTCGTACCGGCTGGCTGGACACCGTTGCCGTTCGTCGTGCGGTA
CAGCTGAACTCCCTGTCTGGCTTCTGCCTGACTAAACTGGACGTTCTGGATGGCCTGAAA
GAGGTTAAACTCTGCGTGGCTTACCGTATGCCGGATGGTCGCGAAGTGACTACCACTCCG
CTGGCAGCTGACGACTGGAAAGGTGTAGAGCCGATTTACGAAACCATGCCGGGCTGGTCT
GAATCCACCTTCGGCGTGAAAGATCGTAGCGGCCTGCCGCAGGCGGCGCTGAACTATATC
AAGCGTATTGAAGAGCTGACTGGTGTGCCGATCGATATCATCTCTACCGGTCCGGATCGT
ACTGAAACCATGATTCTGCGCGACCCGTTCGACGCGTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Wolfe SA, Smith JM: Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12. J Biol Chem. 1988 Dec 15;263(35):19147-53. [3058695 ]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [7610040 ]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [9278503 ]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [16738553 ]
  5. Dong Q, Liu F, Myers AM, Fromm HJ: Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis. J Biol Chem. 1991 Jul 5;266(19):12228-33. [2061308 ]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [9298646 ]
  7. Dong Q, Fromm HJ: Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5'-phosphate. Identification of an active site lysyl residue. J Biol Chem. 1990 Apr 15;265(11):6235-40. [2108156 ]
  8. Liu F, Dong Q, Fromm HJ: Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase. J Biol Chem. 1992 Feb 5;267(4):2388-92. [1733940 ]
  9. Silva MM, Poland BW, Hoffman CR, Fromm HJ, Honzatko RB: Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli. J Mol Biol. 1995 Dec 1;254(3):431-46. [7490761 ]
  10. Poland BW, Lee SF, Subramanian MV, Siehl DL, Anderson RJ, Fromm HJ, Honzatko RB: Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin. Biochemistry. 1996 Dec 10;35(49):15753-9. [8961938 ]
  11. Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB: Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli. J Biol Chem. 1996 Jun 28;271(26):15407-13. [8663109 ]
  12. Poland BW, Fromm HJ, Honzatko RB: Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+. J Mol Biol. 1996 Dec 20;264(5):1013-27. [9000627 ]
  13. Fonne-Pfister R, Chemla P, Ward E, Girardet M, Kreuz KE, Honzatko RB, Fromm HJ, Schar HP, Grutter MG, Cowan-Jacob SW: The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase. Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9431-6. [8790347 ]
  14. Poland BW, Bruns C, Fromm HJ, Honzatko RB: Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli. J Biol Chem. 1997 Jun 13;272(24):15200-5. [9182542 ]
  15. Hanessian S, Lu PP, Sanceau JY, Chemla P, Gohda K, Fonne-Pfister R, Prade L, Cowan-Jacob SW: An Enzyme-Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase. Angew Chem Int Ed Engl. 1999 Nov 2;38(21):3159-3162. [10556888 ]
  16. Choe JY, Poland BW, Fromm HJ, Honzatko RB: Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli. Biochemistry. 1999 May 25;38(21):6953-61. [10346917 ]
  17. Hou Z, Cashel M, Fromm HJ, Honzatko RB: Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase. J Biol Chem. 1999 Jun 18;274(25):17505-10. [10364182 ]
  18. Hou Z, Wang W, Fromm HJ, Honzatko RB: IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli. J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. [11741996 ]
  19. Iancu CV, Zhou Y, Borza T, Fromm HJ, Honzatko RB: Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases. Biochemistry. 2006 Sep 26;45(38):11703-11. [16981730 ]

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