| EC |
3.1.3.87 |
| Accepted name: |
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase |
| Reaction: |
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate |
| Other name(s): |
HK-MTPenyl-1-P phosphatase; MtnX; YkrX; 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate phosphohydrolase; 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate phosphohydrolase |
| Systematic name: |
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate phosphohydrolase |
| Comments: |
The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2]. In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 5.3.2.5, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039] |
| 2. |
Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286–290. [DOI] [PMID: 14551435] |
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| [EC 3.1.3.87 created 2012] |
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