Backbone and side-chain chemical shift assignments of MarH, a critical intermediary epimerase for biosynthesis of Maremycins in Streptomyces

Biomolecular NMR Assignments - Tập 12 - Trang 335-338 - 2018
Bin Liu1,2, Shiqi Fang1,2, Xiaofang Ma1,2, Zhiqiang Bai1,2, Kaifeng Hu1
1State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming, China
2University of Chinese Academy of Sciences, Beijing, China

Tóm tắt

MarH is an essential epimerase that catalyzes the isomerization of 3R-β-methyl-indolepyruvate (β-MeInPy) to 3S-β-MeInPy, which is the important precursor for biosynthesis of Maremycins. Biophysical study of the structure of MarH would be informative for better understanding of its catalytic mechanism and feasible application of the enzyme in isomerization reaction. Here, we report the backbone and side-chain NMR chemical shift assignments of MarH, which lays a foundation for further structural and mechanical study of the enzyme.

Tài liệu tham khảo

Balkbindseil W, Helmke E, Weyland H, Laatsch H (1995) Maremycin A and B, new diketopiperazines from a marine Streptomyces sp. Liebigs Ann 7:1291–1294 Chan TH, Hill RK (1970) The absolute configuration of indolmycin. J Org Chem 35:3519–3521 Chavez FA, Banerjee A, Sljivic B (2011) Modeling the metal binding site in cupin proteins. In: Pramatarova L (ed) On biomimetics. InTech, Rijeka. https://doi.org/10.5772/18262 Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293 Dunwell JM, Gane PJ (1998) Microbial relatives of seed storage proteins: conservation of motifs in a functionally diverse superfamily of enzymes. J Mol Evol 46:147–154 Dunwell JM, Culham A, Carter CE, Sosaaguirre CR, Goodenough PW (2001) Evolution of functional diversity in the cupin superfamily. Trends Biochem Sci 26:740–746 Dunwell JM, Purvis A, Khuri S (2004) Cupins: the most functionally diverse protein superfamily? Phytochemistry 65:7–17 Kelley LA, Mezulis S, Yates CM, Wass MN, Sternberg MJ (2015) The Phyre2 web portal for protein modelling, prediction and analysis. Nat Protoc 10:845–858 Lee W, Tonelli M, Markley JL (2015) NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy. Bioinformatics 31:1325–1327 Sheehan JC, Mania D, Nakamura S, Stock JA, Maeda K (1968) The structure of telomycin. J Am Chem Soc 90:462–470 Ueda T, Inada M, Okamoto I, Morita N, Tamura O (2008) Synthesis of maremycins A and D1 via cycloaddition of a nitrone with (E)-3-ethylidene-1-methylindolin-2-one. Org Lett 10:2043–2046 Wilkinson B, Micklefield J (2009) Biosynthesis of nonribosomal peptide precursors. Methods Enzymol 458:353–378 Wishart DS et al (1995) 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135–140 Yang S, Bax A (2015) Protein structural information derived from NMR chemical shift with the neural network program TALOS-N. Methods Mol Biol 1260:17–32 Zou Y et al (2013) Stereospecific biosynthesis of β-methyltryptophan from L-tryptophan features a stereochemical switch. Angew Chem Int Ed 52:12951–12955