PMID:24955762

Citation	Korczynska, M, Xiang, DF, Zhang, Z, Xu, C, Narindoshvili, T, Kamat, SS, Williams, HJ, Chang, SS, Kolb, P, Hillerich, B, Sauder, JM, Burley, SK, Almo, SC, Swaminathan, S, Shoichet, BK and Raushel, FM (2014) Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Biochemistry 53:4727-38
Abstract	A novel lactonase from Mycoplasma synoviae 53 (MS53_0025) and Mycoplasma agalactiae PG2 (MAG_6390) was characterized by protein structure determination, molecular docking, gene context analysis, and library screening. The crystal structure of MS53_0025 was determined to a resolution of 2.06 Å. This protein adopts a typical amidohydrolase (β/α)8-fold and contains a binuclear zinc center located at the C-terminal end of the β-barrel. A phosphate molecule was bound in the active site and hydrogen bonds to Lys217, Lys244, Tyr245, Arg275, and Tyr278. Both docking and gene context analysis were used to narrow the theoretical substrate profile of the enzyme, thus directing empirical screening to identify that MS53_0025 and MAG_6390 catalyze the hydrolysis of d-xylono-1,4-lactone-5-phosphate (2) with kcat/Km values of 4.7 × 10(4) and 5.7 × 10(4) M(-1) s(-1) and l-arabino-1,4-lactone-5-phosphate (7) with kcat/Km values of 1.3 × 10(4) and 2.2 × 10(4) M(-1) s(-1), respectively. The identification of the substrate profile of these two phospho-furanose lactonases emerged only when all methods were integrated and therefore provides a blueprint for future substrate identification of highly related amidohydrolase superfamily members.
Links	PubMed PMC4108184 Online version:10.1021/bi500595c
Keywords
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
MYCS5:Q4A724		GO:0050490: 1,4-lactonase activity	ECO:0000314:		F		Table 3 shows kinetic parameters for Ms0025 with various substrates (substrate structures are in Scheme 2). All substrates used are 1,4 lactones.	complete CACAO 10134
MYCS5:Q4A724	enables	GO:0050490: 1,4-lactonase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
MYCAP:A5IZ80		GO:0050490: 1,4-lactonase activity	ECO:0000314:		F		Table 3 shows kinetic parameters for Mag6390 with various substrates	complete CACAO 10135
MYCAP:A5IZ80	enables	GO:0050490: 1,4-lactonase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

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