6jvv
From Proteopedia
Crystal structure of maleylpyruvate hydrolase from Sphingobium.sp SYK-6
Structural highlights
FunctionPublication Abstract from PubMedSphingobium sp. strain SYK-6, an aerobic gram-negative bacillus found in soil, is known for utilizing lignin-derived monoaryls and biaryls as carbon sources and degrading aromatic compounds. The Sphingobium sp. strain SYK-6 genome contains three genes involved in salicylate catabolism: SLG_11260, SLG_11270, and SLG_11280. Here, we report that the gene product of SLG_11280 functions as a maleylpyruvate hydrolase (SsMPH) with Km and Kcat values of 166.2muM and 3.76 min(-1), respectively. This study also reveals the crystal structures of both the apo and pyruvate-manganese ion-bound SsMPH, which revealed that like other fumarylacetoacetate hydrolases, SsMPH dimerizes and has nine unique 310-helices. Molecular docking studies of maleylpyruvate also revealed the likely binding mode of SsMPH and its substrate. Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls.,Hong H, Seo H, Kim KJ Biochem Biophys Res Commun. 2019 May 9. pii: S0006-291X(19)30898-8. doi:, 10.1016/j.bbrc.2019.05.030. PMID:31079929[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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