5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Details

Name
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Synonyms
  • 3.2.2.9
  • 5'-methylthioadenosine nucleosidase
  • AdoHcy nucleosidase
  • MTA nucleosidase
  • MTA/SAH nucleosidase
  • mtn
  • P46
  • pfs
  • S-adenosylhomocysteine nucleosidase
  • SAH nucleosidase
  • SRH nucleosidase
  • yadA
Gene Name
mtnN
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0003973|5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGAT
LLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFK
ADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAH
VCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
Number of residues
232
Molecular Weight
24353.725
Theoretical pI
4.9
GO Classification
Functions
adenosylhomocysteine nucleosidase activity / methylthioadenosine nucleosidase activity
Processes
L-methionine biosynthetic process from methylthioadenosine / L-methionine biosynthetic process from S-adenosylmethionine / nucleoside catabolic process
Components
cytosol
General Function
Methylthioadenosine nucleosidase activity
Specific Function
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0021317|5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN)
ATGAAAATCGGCATCATTGGTGCAATGGAAGAAGAAGTTACGCTGCTGCGTGACAAAATC
GAAAACCGTCAAACTATCAGTCTCGGCGGTTGCGAAATCTATACCGGCCAACTGAATGGA
ACCGAGGTTGCGCTTCTGAAATCGGGCATCGGTAAAGTCGCTGCGGCGCTGGGTGCCACT
TTGCTGTTGGAACACTGCAAGCCAGATGTGATTATTAACACCGGTTCTGCCGGTGGCCTG
GCACCAACGTTGAAAGTGGGCGATATCGTTGTCTCGGACGAAGCACGTTATCACGACGCG
GATGTCACGGCATTTGGTTATGAATACGGTCAGTTACCAGGCTGTCCGGCAGGCTTTAAA
GCTGACGATAAACTGATCGCTGCCGCTGAGGCCTGCATTGCCGAACTGAATCTTAACGCT
GTACGTGGCCTGATTGTTAGCGGCGACGCTTTCATCAACGGTTCTGTTGGTCTGGCGAAA
ATCCGCCACAACTTCCCACAGGCCATTGCTGTAGAGATGGAAGCGACGGCAATCGCCCAT
GTCTGCCACAATTTCAACGTCCCGTTTGTTGTCGTACGCGCCATCTCCGACGTGGCCGAT
CAACAGTCTCATCTTAGCTTCGATGAGTTCCTGGCTGTTGCCGCTAAACAGTCCAGCCTG
ATGGTTGAGTCACTGGTGCAGAAACTTGCACATGGCTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AF12
UniProtKB Entry NameMTNN_ECOLI
GenBank Protein ID2981267
GenBank Gene IDU24438
General References
  1. Wurgler SM, Richardson CC: Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2740-4. [Article]
  2. Cornell KA, Riscoe MK: Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product. Biochim Biophys Acta. 1998 Mar 4;1396(1):8-14. [Article]
  3. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [Article]
  4. 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. [Article]
  5. 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. [Article]
  6. Della Ragione F, Porcelli M, Carteni-Farina M, Zappia V, Pegg AE: Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action. Biochem J. 1985 Dec 1;232(2):335-41. [Article]
  7. Cornell KA, Swarts WE, Barry RD, Riscoe MK: Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity. Biochem Biophys Res Commun. 1996 Nov 21;228(3):724-32. [Article]
  8. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  9. Lee JE, Luong W, Huang DJ, Cornell KA, Riscoe MK, Howell PL: Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis. Biochemistry. 2005 Aug 23;44(33):11049-57. [Article]
  10. Lee JE, Cornell KA, Riscoe MK, Howell PL: Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure. 2001 Oct;9(10):941-53. [Article]
  11. Lee JE, Cornell KA, Riscoe MK, Howell PL: Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis. J Biol Chem. 2003 Mar 7;278(10):8761-70. Epub 2002 Dec 20. [Article]
  12. Singh V, Evans GB, Lenz DH, Mason JM, Clinch K, Mee S, Painter GF, Tyler PC, Furneaux RH, Lee JE, Howell PL, Schramm VL: Femtomolar transition state analogue inhibitors of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli. J Biol Chem. 2005 May 6;280(18):18265-73. Epub 2005 Mar 4. [Article]
  13. Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL: Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis. J Mol Biol. 2005 Sep 23;352(3):559-74. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02158(2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediolexperimentalunknownDetails
DB02281FormycinexperimentalunknownDetails
DB00173Adenineapproved, nutraceuticalunknownDetails
DB029335'-Deoxy-5'-(Methylthio)-TubercidinexperimentalunknownDetails
DB08606(3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OLexperimentalunknownDetails