2-phosphosulfolactate phosphatase

Class of enzymes 2-phosphosulfolactate phosphatase 3.1.3.71 0050532 The enzyme 2-phosphosulfolactate phosphatase (EC 3.1.3.71) catalyzes the reaction 60% Q27104241 (2R)-O-phospho-3-sulfolactic acid H2O Pi Q27093349 (R)-2-hydroxy-3-sulfopropanoic acid 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.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 5176–88 11589710 10.1046/j.0014-2956.2001.02451.x 19 free Wu Hsin-Hua Pun Michael D. Wise Courtney E. Streit Bennett R. Mus Florence Berim Anna Kincannon William M. Islam Abdullah Partovi Sarah E. Gang David R. Dubois Jennifer L. Lubner Carolyn E. Berkman Clifford E. Lange B. Markus Peters John W. 3 The pathway for coenzyme M biosynthesis in bacteria Proceedings of the National Academy of Sciences 2022 119 36 e2207190119 10.1073/pnas.2207190119 free 36037354 9457059 Saranya Sivashanmuga Vadivel Chellapandi Paulchamy Convergent Evolution of Coenzyme Metabolism in Methanosarcina mazei: Insights into Primitive Life and Metabolic Adaptations Journal of Basic Microbiology 2025 65 7 e70015 10.1002/jobm.70015 40051064 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.3.1.3.71 Structural studies As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VR0.Didonato Michael Krishna S. Sri Schwarzenbacher Robert McMullan Daniel Agarwalla Sanjay Brittain Scott M. Miller Mitchell D. Abdubek Polat Ambing Eileen Axelrod Herbert L. Canaves Jaume M. Chiu Hsiu-Ju Deacon Ashley M. Duan Lian Elsliger Marc-André Godzik Adam Grzechnik Slawomir K. Hale Joanna Hampton Eric Haugen Justin Jaroszewski Lukasz Jin Kevin K. Klock Heath E. Knuth Mark W. Koesema Eric Kreusch Andreas Kuhn Peter Lesley Scott A. Levin Inna Morse Andrew T. 3 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 2006 65 3 771–776 10.1002/prot.20978 16927339 References Biology no Category:EC 3.1.3 Category:Enzymes of known structure