4G2C

DyP2 from Amycolatopsis sp. ATCC 39116

Summary for 4G2C

• Entry DOI: 10.2210/pdb4g2c/pdb
• Descriptor: DyP2, PROTOPORPHYRIN IX CONTAINING FE, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: dye peroxidase, oxidoreductase
• Biological source: Amycolatopsis sp. ATCC 39116
• Total number of polymer chains: 2
• Total formula weight: 110625.49

Authors

Brown, M.E.,Barros, T.,Chang, M.C.Y. (deposition date: 2012-07-11, release date: 2012-10-24, Last modification date: 2023-09-13)

Primary citation

Brown, M.E.,Barros, T.,Chang, M.C.
Identification and characterization of a multifunctional dye peroxidase from a lignin-reactive bacterium.
Acs Chem.Biol., 7:2074-2081, 2012

PubMed Abstract: Plant biomass represents a renewable feedstock that has not yet been fully tapped because of the difficulty in accessing the carbon in its structural biopolymers. Lignin is an especially challenging substrate, but select microbes have evolved complex systems of enzymes for its breakdown through a radical-mediated oxidation process. Fungal systems are well-characterized for their ability to depolymerize lignin, but the ability of bacteria to react with this substrate remains elusive. We have therefore focused on elucidating strategies used by lignin-reactive soil bacteria and describing their oxidative enzyme systems. We now report the identification and characterization of an unusual C-type dye-decolorizing peroxidase from Amycolatopsis sp. 75iv2 (DyP2), which belongs to a family of heme peroxidases reported to be involved in bacterial lignin degradation. Biochemical studies indicate that DyP2 has novel function for this family, with versatile and high activity both as a peroxidase and Mn peroxidase (k(cat)/K(M) ≈ 10(5)-10(6) M(-1) s(-1)). It also has a Mn-dependent oxidase mode of action that expands its substrate scope. Crystallographic studies of DyP2 at 2.25 Å resolution show the existence of a Mn binding pocket and support its key role in catalysis.

PubMed: 23054399
DOI: 10.1021/cb300383y

Experimental method

X-RAY DIFFRACTION (2.25 Å)