2-phosphosulfolactate phosphatase
| 2-phosphosulfolactate phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.71 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme 2-phosphosulfolactate phosphatase (EC 3.1.3.71) catalyzes the reaction
-O-phospho-3-sulfolactic_acid.svg.png)
-2-hydroxy-3-sulfopropanoic_acid.svg.png)
The enzyme characterised from Methanococcus jannaschii, hydrolyses (2R)-O-phospho-3-sulfolactic acid to (R)-2-hydroxy-3-sulfopropanoic acid and orthophosphate (Pi). The reaction is part of the biosynthesis of coenzyme M in this archaeal methanogen.[1][2][3]
This enzyme is a hydrolase, specifically one acting on phosphoric monoester bonds. The systematic name (R)-2-phospho-3-sulfolactate phosphohydrolase. Other names in use include (2R)-phosphosulfolactate phosphohydrolase, and ComB phosphatase.[4]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1VR0.[5]
References
- ↑ Graham DE, Graupner M, Xu H, White RH (2001). "Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg2+-dependent acid phosphatases". Eur. J. Biochem. 268 (19): 5176–88. doi:10.1046/j.0014-2956.2001.02451.x. PMID 11589710.
- ↑ Wu, Hsin-Hua; Pun, Michael D.; Wise, Courtney E.; et al. (2022). "The pathway for coenzyme M biosynthesis in bacteria". Proceedings of the National Academy of Sciences. 119 (36) e2207190119. doi:10.1073/pnas.2207190119. PMC 9457059. PMID 36037354.
- ↑ Saranya, Sivashanmuga Vadivel; Chellapandi, Paulchamy (2025). "Convergent Evolution of Coenzyme Metabolism in Methanosarcina mazei: Insights into Primitive Life and Metabolic Adaptations". Journal of Basic Microbiology. 65 (7) e70015. doi:10.1002/jobm.70015. PMID 40051064.
- ↑ Enzyme 3.1.3.71 at KEGG Pathway Database.
- ↑ Didonato, Michael; Krishna, S. Sri; Schwarzenbacher, Robert; et al. (2006). "Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6 Å resolution reveals a new fold with a novel active site". Proteins: Structure, Function, and Bioinformatics. 65 (3): 771–776. doi:10.1002/prot.20978. PMID 16927339.
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