Methylthioribulose 1-phosphate dehydratase
In enzymology, a methylthioribulose 1-phosphate dehydratase (EC 4.2.1.109) is an enzyme that catalyzes the chemical reaction
- S-methyl-5-thio-D-ribulose 1-phosphate 5-(methylthio)-2,3-dioxopentyl phosphate + H2O
| methylthioribulose 1-phosphate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC number | 4.2.1.109 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Hence, this enzyme has one substrate, S-methyl-5-thio-D-ribulose 1-phosphate, and two products, 5-(methylthio)-2,3-dioxopentyl phosphate and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is S-methyl-5-thio-D-ribulose-1-phosphate 4-hydro-lyase [5-(methylthio)-2,3-dioxopentyl-phosphate-forming]. Other names in common use include 1-PMT-ribulose dehydratase, and S-methyl-5-thio-D-ribulose-1-phosphate hydro-lyase. This enzyme participates in methionine metabolism.
References
- Kang, W; Hong, S. H.; Lee, H. M.; Kim, N. Y.; Lim, Y. C.; Le Le, T. M.; Lim, B; Kim, H. C.; Kim, T. Y.; Ashida, H; Yokota, A; Hah, S. S.; Chun, K. H.; Jung, Y. K.; Yang, J. K. (2014). "Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme". Proceedings of the National Academy of Sciences. 111 (1): E54-61. doi:10.1073/pnas.1308768111. PMC 3890807. PMID 24367089.
- Furfine ES, Abeles RH (1988). "Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae". J. Biol. Chem. 263 (20): 9598–606. PMID 2838472.
- Wray JW, Abeles RH (1995). "The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases". J. Biol. Chem. 270 (7): 3147–53. doi:10.1074/jbc.270.7.3147. PMID 7852397.
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