Identification
Name:5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Synonyms:
  • MTA/SAH nucleosidase
  • MTAN
  • 5'-methylthioadenosine nucleosidase
  • MTA nucleosidase
  • P46
  • S-adenosylhomocysteine nucleosidase
  • AdoHcy nucleosidase
  • SAH nucleosidase
  • SRH nucleosidase
Gene Name:mtnN
Enzyme Class:
Biological Properties
General Function:Involved in adenosylhomocysteine 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
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
SMPDB Reactions:
Thumb+ThumbThumb+ S-ribosyl-L-homocysteine+Thumb
5'-S-methyl-5'-thioadenosine+ThumbThumb+Thumb
5'-S-methyl-5'-thioadenosine + Water5-Methylthioribose + Adenine
ReactionCard
Thumb+ThumbThumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB24231 S-ribosyl-L-homocysteineMetaboCard
ECMDB211745'-DeoxyadenosineMetaboCard
ECMDB211755'-DeoxyriboseMetaboCard
ECMDB011735'-MethylthioadenosineMetaboCard
ECMDB010875-MethylthioriboseMetaboCard
ECMDB00034AdenineMetaboCard
ECMDB00939S-AdenosylhomocysteineMetaboCard
ECMDB20190S-Ribosyl-L-homocysteineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenosylhomocysteine nucleosidase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing N-glycosyl compounds
methylthioadenosine nucleosidase activity
Process
amino acid salvage
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
cellular nitrogen compound metabolic process
L-methionine salvage from methylthioadenosine
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside catabolic process
nucleoside metabolic process
Gene Properties
Blattner:b0159
Gene OrientationCounterclockwise
Centisome Percentage:3.85
Left Sequence End178455
Right Sequence End179153
Gene Sequence:
>699 bp
ATGCAAAAAAACGCTGCGCATACTTATGCCATTTCCAGCTTGTTGGTGCTTTCACTAACC
GGCTGCGCCTGGATACCCTCCACGCCGCTGGTGCAGGGGGCGACCAGTGCACAACCGGTT
CCCGGTCCGACGCCCGTCGCCAACGGTTCTATTTTCCAGTCTGCTCAGCCGATTAACTAT
GGCTATCAACCGCTGTTTGAAGATCGTCGACCACGCAATATTGGCGATACGCTGACCATC
GTGTTGCAGGAGAACGTCAGCGCCAGCAAAAGCTCCTCTGCGAATGCCAGCCGTGACGGT
AAAACTAATTTTGGCTTTGATACTGTGCCGCGCTATTTGCAGGGGCTGTTTGGTAACGCT
CGTGCCGATGTCGAAGCCTCCGGTGGTAACACGTTCAACGGAAAGGGCGGGGCCAATGCC
AGCAATACCTTTAGCGGCACGTTGACGGTGACGGTTGACCAGGTACTGGTCAACGGCAAC
CTGCATGTGGTGGGTGAAAAACAGATTGCCATTAATCAGGGTACCGAATTTATTCGCTTC
TCTGGCGTGGTTAATCCACGCACTATCAGCGGCAGCAATACCGTACCGTCTACTCAGGTG
GCGGATGCGCGCATTGAATACGTAGGCAATGGCTACATTAACGAAGCGCAAAATATGGGC
TGGTTGCAGCGTTTCTTCCTTAACCTGTCGCCAATGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:232
Protein Molecular Weight:24354
Protein Theoretical pI:5
PDB File:1Y6R
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGAT
LLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFK
ADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAH
VCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
References
External Links:
ResourceLink
Uniprot ID:P0AF12
Uniprot Name:MTNN_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674831
PDB ID:1Y6R
Ecogene ID:EG11090
Ecocyc:EG11090
ColiBase:b0159
Kegg Gene:b0159
EchoBASE ID:EB1082
CCDB:MTNN_ECOLI
BacMap:16128152
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Cornell, K. A., Riscoe, M. K. (1998). "Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product." Biochim Biophys Acta 1396:8-14. Pubmed: 9524204
  • Cornell, K. A., Swarts, W. E., Barry, R. D., Riscoe, M. K. (1996). "Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity." Biochem Biophys Res Commun 228:724-732. Pubmed: 8941345
  • Della Ragione, F., Porcelli, M., Carteni-Farina, M., Zappia, V., Pegg, A. E. (1985). "Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action." Biochem J 232:335-341. Pubmed: 3911944
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Lee, J. E., Cornell, K. A., Riscoe, M. K., Howell, P. L. (2001). "Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases." Structure 9:941-953. Pubmed: 11591349
  • Lee, J. E., Cornell, K. A., Riscoe, M. K., Howell, P. L. (2003). "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 278:8761-8770. Pubmed: 12496243
  • Lee, J. E., Smith, G. D., Horvatin, C., Huang, D. J., Cornell, K. A., Riscoe, M. K., Howell, P. L. (2005). "Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis." J Mol Biol 352:559-574. Pubmed: 16109423
  • Singh, V., Evans, G. B., Lenz, D. H., Mason, J. M., Clinch, K., Mee, S., Painter, G. F., Tyler, P. C., Furneaux, R. H., Lee, J. E., Howell, P. L., Schramm, V. L. (2005). "Femtomolar transition state analogue inhibitors of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli." J Biol Chem 280:18265-18273. Pubmed: 15749708
  • Wurgler, S. M., Richardson, C. C. (1990). "Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli." Proc Natl Acad Sci U S A 87:2740-2744. Pubmed: 2157212