IAG-nucleoside hydrolase

Details

Name
IAG-nucleoside hydrolase
Synonyms
Not Available
Gene Name
Not Available
Organism
Trypanosoma vivax
Amino acid sequence
>lcl|BSEQ0022072|IAG-nucleoside hydrolase
MAKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVTGKIMCLMHNN
MNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPENVELWDKIKAENEKYEGQQL
LADLVMNSEEKVTICVTGPLSNVAWCIDKYGEKFTSKVEECVIMGGAVDVRGNVFLPSTD
GTAEWNIYWDPASAKTVFGCPGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGT
MWAMCTHCELLRDGDGYYAWDALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAE
KYPLTFVARNPEAEFFLDMLLRSARAC
Number of residues
327
Molecular Weight
36330.44
Theoretical pI
4.43
GO Classification
Functions
hydrolase activity / metal ion binding
General Function
Metal ion binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0006408|984 bp
ATGGCAAAGAATGTCGTGCTGGACCATGATGGAAATCTAGACGACTTTGTCGCTATGGTG
TTGCTGGCTTCCAACACGGAGAAGGTACGACTTATTGGGGCACTCTGTACCGATGCGGAT
TGCTTCGTTGAGAATGGTTTCAACGTCACTGGGAAGATAATGTGCCTGATGCACAACAAC
ATGAATCTTCCATTGTTTCCTATCGGCAAATCAGCGGCGACCGCCGTCAATCCCTTCCCG
AAAGAATGGCGGTGCCTGGCCAAGAACATGGATGATATGCCGATTCTCAACATACCAGAG
AATGTGGAACTGTGGGATAAAATAAAGGCTGAGAATGAAAAGTACGAAGGACAGCAACTG
CTTGCGGATTTGGTGATGAATTCGGAAGAAAAGGTTACGATTTGTGTCACTGGGCCACTC
TCCAACGTTGCCTGGTGCATTGACAAGTACGGCGAGAAGTTCACATCAAAGGTGGAGGAA
TGCGTCATCATGGGAGGTGCTGTTGATGTTCGTGGCAACGTGTTTCTCCCAAGCACTGAT
GGTACGGCGGAGTGGAACATTTACTGGGACCCTGCGTCGGCTAAGACTGTCTTTGGTTGC
CCAGGCCTTCGCCGCATCATGTTCTCGCTCGACTCAACAAACACTGTTCCGGTTAGGTCT
CCCTACGTCCAACGCTTTGGCGAACAAACAAACTTTCTTCTTTCCATTCTTGTGGGTACA
ATGTGGGCAATGTGCACACACTGTGAGTTATTGCGTGATGGGGATGGCTACTACGCCTGG
GACGCACTCACTGCGGCCTACGTTGTCGACCAGAAGGTTGCTAATGTGGACCCTGTCCCT
ATTGACGTGGTGGTGGACAAGCAGCCGAATGAAGGCGCGACAGTGCGGACCGACGCGGAG
AAGTACCCACTCACATTTGTGGCGAGGAACCCCGAGGCCGAATTCTTTTTGGACATGCTC
CTACGGAGTGCGCGTGCTTGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9GPQ4
UniProtKB Entry NameQ9GPQ4_TRYVI
GenBank Gene IDAF311701
General References
  1. Versees W, Decanniere K, Pelle R, Depoorter J, Brosens E, Parkin DW, Steyaert J: Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax. J Mol Biol. 2001 Apr 13;307(5):1363-79. [Article]
  2. Versees W, Decanniere K, Van Holsbeke E, Devroede N, Steyaert J: Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax. J Biol Chem. 2002 May 3;277(18):15938-46. Epub 2002 Feb 19. [Article]
  3. Versees W, Loverix S, Vandemeulebroucke A, Geerlings P, Steyaert J: Leaving group activation by aromatic stacking: an alternative to general acid catalysis. J Mol Biol. 2004 Apr 16;338(1):1-6. [Article]
  4. Versees W, Barlow J, Steyaert J: Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis. J Mol Biol. 2006 Jun 2;359(2):331-46. Epub 2006 Mar 29. [Article]
  5. Vandemeulebroucke A, De Vos S, Van Holsbeke E, Steyaert J, Versees W: A flexible loop as a functional element in the catalytic mechanism of nucleoside hydrolase from Trypanosoma vivax. J Biol Chem. 2008 Aug 8;283(32):22272-82. doi: 10.1074/jbc.M803705200. Epub 2008 Jun 2. [Article]
  6. Versees W, Goeminne A, Berg M, Vandemeulebroucke A, Haemers A, Augustyns K, Steyaert J: Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors. Biochim Biophys Acta. 2009 Jun;1794(6):953-60. doi: 10.1016/j.bbapap.2009.02.011. Epub 2009 Mar 10. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04335Inosineexperimental, investigationalunknownDetails
DB045463-DeazaadenosineexperimentalunknownDetails