Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7PBI

4-ethylphenol oxidase from Gulosibacter chungangensis: isoeugenol complex

Summary for 7PBI
Entry DOI10.2210/pdb7pbi/pdb
DescriptorFAD-binding oxidoreductase, FLAVIN-ADENINE DINUCLEOTIDE, ISOEUGENOL (3 entities in total)
Functional Keywordsflavoprotein, biocatalysis, genome mining, enzyme structure, 4-vinylphenol, dehydrogenation, 4-alkylphenol oxidase, oxidoreductase
Biological sourceGulosibacter chungangensis
Total number of polymer chains8
Total formula weight479703.89
Authors
Alvigini, L.,Mattevi, A. (deposition date: 2021-08-02, release date: 2021-09-29, Last modification date: 2024-11-06)
Primary citationAlvigini, L.,Gran-Scheuch, A.,Guo, Y.,Trajkovic, M.,Saifuddin, M.,Fraaije, M.W.,Mattevi, A.
Discovery, Biocatalytic Exploration and Structural Analysis of a 4-Ethylphenol Oxidase from Gulosibacter chungangensis.
Chembiochem, 22:3225-3233, 2021
Cited by
PubMed Abstract: The vanillyl-alcohol oxidase (VAO) family is a rich source of biocatalysts for the oxidative bioconversion of phenolic compounds. Through genome mining and sequence comparisons, we found that several family members lack a generally conserved catalytic aspartate. This finding led us to study a VAO-homolog featuring a glutamate residue in place of the common aspartate. This 4-ethylphenol oxidase from Gulosibacter chungangensis (Gc4EO) shares 42 % sequence identity with VAO from Penicillium simplicissimum, contains the same 8α-N -histidyl-bound FAD and uses oxygen as electron acceptor. However, Gc4EO features a distinct substrate scope and product specificity as it is primarily effective in the dehydrogenation of para-substituted phenols with little generation of hydroxylated products. The three-dimensional structure shows that the characteristic glutamate side chain creates a closely packed environment that may limit water accessibility and thereby protect from hydroxylation. With its high thermal stability, well defined structural properties and high expression yields, Gc4EO may become a catalyst of choice for the specific dehydrogenation of phenolic compounds bearing small substituents.
PubMed: 34523783
DOI: 10.1002/cbic.202100457
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

236963

数据于2025-06-04公开中

PDB statisticsPDBj update infoContact PDBjnumon