Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls

Hwaseok Hong; Hogyun Seo; Kyung Jin Kim

doi:10.1016/j.bbrc.2019.05.030

Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls

Hwaseok Hong, Hogyun Seo, Kyung Jin Kim

Kyungpook National University

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Sphingobium 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 K_m and K_cat values of 166.2 μM 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.

Original language	English
Pages (from-to)	765-771
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	514
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2019.05.030
State	Published - 30 Jun 2019

Keywords

Crystal structure
Maleylpyruvate hydrolase
Salicylate catabolism
Sphingobium sp. strain SYK-6

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10.1016/j.bbrc.2019.05.030

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title = "Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls",

abstract = "Sphingobium 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 166.2 μM 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.",

keywords = "Crystal structure, Maleylpyruvate hydrolase, Salicylate catabolism, Sphingobium sp. strain SYK-6",

author = "Hwaseok Hong and Hogyun Seo and Kim, {Kyung Jin}",

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year = "2019",

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AU - Hong, Hwaseok

AU - Seo, Hogyun

AU - Kim, Kyung Jin

PY - 2019/6/30

Y1 - 2019/6/30

N2 - Sphingobium 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 166.2 μM 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.

AB - Sphingobium 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 166.2 μM 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.

KW - Crystal structure

KW - Maleylpyruvate hydrolase

KW - Salicylate catabolism

KW - Sphingobium sp. strain SYK-6

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ER -

Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls

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