If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
Synonyms: methylthioadenosine degradation IV
|Superclasses:||Degradation/Utilization/Assimilation → Nucleosides and Nucleotides Degradation → S-methyl-5'-thioadenosine Degradation|
5'-Methylthioadenosine (MTA) is a side product of the spermidine biosynthesis I and aminopropylcadaverine biosynthesis pathways. Many organisms are able to recycle MTA via the S-methyl-5-thio-α-D-ribose 1-phosphate degradation pathway. However, while the E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase can hydrolyze MTA to adenine and methylthioribose (MTR), MTR can not be further metabolized and is excreted [Hughes06]. No transporter for MTR is currently known.
Excretion of MTR entails a loss of sulfur, which may explain why putrescine rather than spermidine is the major polyamine in E. coli [Sekowska00a].
In early experiments, 5'-methylthioribose was shown to be a normal biosynthetic product that is secreted into the growth medium by E. coli B [Schroeder73].
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Clinch12: Clinch K, Evans GB, Frohlich RF, Gulab SA, Gutierrez JA, Mason JM, Schramm VL, Tyler PC, Woolhouse AD (2012). "Transition state analogue inhibitors of human methylthioadenosine phosphorylase and bacterial methylthioadenosine/S-adenosylhomocysteine nucleosidase incorporating acyclic ribooxacarbenium ion mimics." Bioorg Med Chem 20(17);5181-7. PMID: 22854195
Cornell96: Cornell KA, Swarts WE, Barry RD, Riscoe MK (1996). "Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity." Biochem Biophys Res Commun 228(3);724-32. PMID: 8941345
Cornell98: Cornell KA, Riscoe MK (1998). "Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product." Biochim Biophys Acta 1396(1);8-14. PMID: 9524204
Della85: Della Ragione F, Porcelli M, Carteni-Farina M, Zappia V, Pegg AE (1985). "Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action." Biochem J 232(2);335-41. PMID: 3911944
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Ferro76: Ferro AJ, Barrett A, Shapiro SK (1976). "Kinetic properties and the effect of substrate analogues on 5'-methylthioadenosine nucleosidase from Escherichia coli." Biochim Biophys Acta 438(2);487-94. PMID: 782530
Gutierrez09: Gutierrez JA, Crowder T, Rinaldo-Matthis A, Ho MC, Almo SC, Schramm VL (2009). "Transition state analogs of 5'-methylthioadenosine nucleosidase disrupt quorum sensing." Nat Chem Biol 5(4):251-7. PMID: 19270684
Kim06: Kim Y, Lew CM, Gralla JD (2006). "Escherichia coli pfs transcription: regulation and proposed roles in autoinducer-2 synthesis and purine excretion." J Bacteriol 188(21);7457-63. PMID: 16950920
Lee01: Lee JE, Cornell KA, Riscoe MK, Howell PL (2001). "Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases." Structure (Camb) 9(10);941-53. PMID: 11591349
Lee03: Lee JE, Cornell KA, Riscoe MK, Howell PL (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(10);8761-70. PMID: 12496243
Lee05: Lee JE, Singh V, Evans GB, Tyler PC, Furneaux RH, Cornell KA, Riscoe MK, Schramm VL, Howell PL (2005). "Structural rationale for the affinity of pico- and femtomolar transition state analogues of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase." J Biol Chem 280(18);18274-82. PMID: 15746096
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Lee05b: Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL (2005). "Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis." J Mol Biol 352(3);559-74. PMID: 16109423
Longshaw10: Longshaw AI, Adanitsch F, Gutierrez JA, Evans GB, Tyler PC, Schramm VL (2010). "Design and synthesis of potent "sulfur-free" transition state analogue inhibitors of 5'-methylthioadenosine nucleosidase and 5'-methylthioadenosine phosphorylase." J Med Chem 53(18);6730-46. PMID: 20718423
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