S-methyl-5'-thioinosine phosphorylase
| S-methyl-5'-thioinosine phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.2.44 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
S-methyl-5'-thioinosine phosphorylase (EC 2.4.2.44, MTIP, MTI phosphorylase, methylthioinosine phosphorylase) is an enzyme with systematic name S-methyl-5'-thioinosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase.[1] This enzyme catalyses the phosphorolysis reaction in which orthophosphate (Pi) cleaves a ribose sugar:
This is the second step in the catabolism of 5′-methylthioadenosine in Pseudomonas aeruginosa. The first step is a deamination catalysed by S-methyl-5'-thioadenosine deaminase to give S-methyl-5'-thioinosine, which is the substrate here. The products are S-methyl-5-thio-α-D-ribose 1-phosphate and hypoxanthine.[2]
References
[edit]- ↑ Enzyme 2.4.2.44 at KEGG Pathway Database.
- ↑ Guan R, Ho MC, Almo SC, Schramm VL (February 2011). "Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing". Biochemistry. 50 (7): 1247–54. doi:10.1021/bi101642d. PMC 3040260. PMID 21197954.
External links
[edit]- S-methyl-5'-thioinosine+phosphorylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
