Related Experiment Video
Updated: Jan 25, 2026

Lignin Down-regulation of Zea mays via dsRNAi and Klason Lignin Analysis
Published on: July 23, 2014
Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived
Hwaseok Hong1, Hogyun Seo1, Kyung-Jin Kim2
1School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea; KNU Institute for Microorganisms, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea.
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.
Related Concept Videos
Lysosomal Hydrolases
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA...
Proteins: From Genes to Degradation
Nomenclature of Aryl and Heterocyclic Amines
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation

