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Panoramic view of a superfamily of phosphatases through substrate profiling

2015; National Academy of Sciences; Volume: 112; Issue: 16 Linguagem: Inglês

10.1073/pnas.1423570112

1091-6490

Hua Huang, Chetanya Pandya, Chunliang Liu, Nawar Al-Obaidi, Min Wang, Z. Li, Sarah Toews Keating, Miyuki Aono, James D. Love, Brandon Evans, R.D. Seidel, B. Hillerich, S. Garforth, Steven C. Almo, Patrick S. Mariano, Debra Dunaway‐Mariano, Karen N. Allen, Jeremiah D. Farelli,

Biochemical and Molecular Research

Significance Here, we examine the activity profile of the haloalkanoic acid dehalogenase (HAD) superfamily by screening a customized library against >200 enzymes from a broad sampling of the superfamily. From this dataset, we can infer the function of nearly 35% of the superfamily. Overall, the superfamily was found to show high substrate ambiguity, with 75% of the superfamily utilizing greater than five substrates. In addition, the HAD members with the least amount of structural accessorization of the Rossmann fold were found to be the most specific, suggesting that elaboration of the core domain may have led to increased substrate range of the superfamily.