Adenylosuccinate synthetase

Details

Name
Adenylosuccinate synthetase
Synonyms
  • 6.3.4.4
  • AMPSase
  • IMP--aspartate ligase
Gene Name
Adss
Organism
Plasmodium falciparum
Amino acid sequence
>lcl|BSEQ0019317|Adenylosuccinate synthetase
MNIFDHQIKNVDKGNVVAILGAQWGDEGKGKIIDMLSEYSDITCRFNGGANAGHTISVND
KKYALHLLPCGVLYDNNISVLGNGMVIHVKSLMEEIESVGGKLLDRLYLSNKAHILFDIH
QIIDSIQETKKLKEGKQIGTTKRGIGPCYSTKASRIGIRLGTLKNFENFKNMYSKLIDHL
MDLYNITEYDKEKELNLFYNYHIKLRDRIVDVISFMNTNLENNKKVLIEGANAAMLDIDF
GTYPYVTSSCTTVGGVFSGLGIHHKKLNLVVGVVKSYLTRVGCGPFLTELNNDVGQYLRE
KGHEYGTTTKRPRRCGWLDIPMLLYVKCINSIDMINLTKLDVLSGLEEILLCVNFKNKKT
GELLEKGCYPVEEEISEEYEPVYEKFSGWKEDISTCNEFDELPENAKKYILAIEKYLKTP
IVWIGVGPNRKNMIVKKNFNLN
Number of residues
442
Molecular Weight
50064.525
Theoretical pI
7.71
GO Classification
Functions
adenylosuccinate synthase activity / GTP binding / metal ion binding
Processes
'de novo' AMP biosynthetic process
Components
cytoplasm
General Function
Metal ion binding
Specific Function
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0005295|1323 bp
ATATTTGATCATCAAATAAAAAATGTGGATAAAGGGAATGTAGTTGCAATATTAGGTGCA
CAATGGGGTGATGAAGGGAAAGGAAAAATAATTGATATGTTATCAGAATATTCTGATATT
ACTTGTAGATTTAATGGAGGTGCTAATGCAGGACATACGATATCAGTAAATGATAAGAAA
TATGCTTTACATTTATTACCATGTGGTGTATTATATGATAATAATATAAGTGTATTAGGA
AACGGAATGGTAATACATGTAAAATCATTAATGGAAGAAATTGAATCAGTTGGGGGAAAG
TTGTTAGATAGATTATATTTATCAAATAAAGCACATATATTATTTGATATTCATCAAATT
ATTGATTCAATCCAAGAAACGAAAAAATTGAAAGAAGGAAAACAAATAGGTACAACAAAA
AGAGGTATTGGACCATGTTATTCTACTAAAGCTTCCAGAATAGGTATAAGATTAGGAACT
TTAAAAAATTTTGAAAATTTTAAAAATATGTATAGTAAATTAATAGACCACTTAATGGAT
TTATATAATATAACAGAATATGACAAAGAAAAAGAACTCAACTTATTTTATAATTATCAC
ATAAAGTTAAGAGATAGAATAGTTGATGTTATTTCCTTTATGAATACAAATTTAGAAAAC
AACAAAAAAGTATTAATTGAAGGTGCTAATGCAGCTATGTTAGATATTGATTTTGGAACA
TATCCATATGTAACTAGTAGCTGTACAACAGTTGGTGGGGTTTTCTCAGGACTTGGAATT
CATCATAAAAAACTGAATTTAGTTGTAGGTGTAGTTAAAAGTTACTTAACCAGAGTTGGA
TGTGGCCCTTTCTTAACTGAATTAAATAATGACGTTGGTCAATATTTAAGAGAAAAAGGT
CATGAATATGGAACGACTACCAAGAGACCAAGAAGGTGTGGATGGCTCGACATACCAATG
TTATTATATGTTAAGTGCATTAATAGTATTGATATGATAAACTTAACAAAATTGGATGTT
TTATCTGGATTAGAGGAAATATTATTGTGTGTCAATTTTAAAAATAAAAAAACAGGAGAA
CTGCTTGAAAAGGGTTGCTACCCTGTTGAAGAAGAAATATCAGAAGAATATGAACCTGTT
TATGAAAAATTCAGTGGATGGAAAGAAGACATCTCAACTTGTAATGAATTTGATGAATTA
CCAGAAAATGCAAAAAAATATATTTTAGCTATAGAGAAATATTTAAAAACTCCAATAGTT
TGGATTGGTGTAGGTCCTAATAGAAAAAATATGATAGTTAAAAAGAATTTTAACCTAAAC
TAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9U8D3
UniProtKB Entry NamePURA_PLAFA
GenBank Gene IDAF095282
General References
  1. Jayalakshmi R, Sumathy K, Balaram H: Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli. Protein Expr Purif. 2002 Jun;25(1):65-72. [Article]
  2. Raman J, Mehrotra S, Anand RP, Balaram H: Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase. Mol Biochem Parasitol. 2004 Nov;138(1):1-8. [Article]
  3. Mehrotra S, Mylarappa BN, Iyengar P, Balaram H: Studies on active site mutants of P. falciparum adenylosuccinate synthetase: insights into enzyme catalysis and activation. Biochim Biophys Acta. 2010 Oct;1804(10):1996-2002. doi: 10.1016/j.bbapap.2010.07.015. Epub 2010 Aug 1. [Article]
  4. Eaazhisai K, Jayalakshmi R, Gayathri P, Anand RP, Sumathy K, Balaram H, Murthy MR: Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum. J Mol Biol. 2004 Jan 30;335(5):1251-64. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02109HadacidinexperimentalunknowninhibitorDetails
DB035106-O-Phosphoryl Inosine MonophosphateexperimentalunknownDetails
DB04315Guanosine-5'-DiphosphateexperimentalunknownDetails