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Metal Ion Promiscuity and Structure of 2,3‐Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae
Author(s) -
Hofer Gerhard,
Sheng Xiang,
Braeuer Simone,
Payer Stefan E.,
Plasch Katharina,
Goessler Walter,
Faber Kurt,
Keller Walter,
Himo Fahmi,
Glueck Silvia M.
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000600
Subject(s) - chemistry , aspergillus oryzae , cofactor , regioselectivity , decarboxylation , carboxylation , metal , substrate (aquarium) , biocatalysis , active site , pyruvate decarboxylase , stereochemistry , combinatorial chemistry , enzyme , organic chemistry , catalysis , reaction mechanism , oceanography , alcohol dehydrogenase , geology
Broad substrate tolerance and excellent regioselectivity, as well as independence from sensitive cofactors have established benzoic acid decarboxylases from microbial sources as efficient biocatalysts. Robustness under process conditions makes them particularly attractive for preparative‐scale applications. The divalent metal‐dependent enzymes are capable of catalyzing the reversible non‐oxidative (de)carboxylation of a variety of electron‐rich (hetero)aromatic substrates analogously to the chemical Kolbe‐Schmitt reaction. Elemental mass spectrometry supported by crystal structure elucidation and quantum chemical calculations verified the presence of a catalytically relevant Mg 2+ complexed in the active site of 2,3‐dihydroxybenoic acid decarboxylase from Aspergillus oryzae (2,3‐DHBD_ Ao ). This unique example with respect to the nature of the metal is in contrast to mechanistically related decarboxylases, which generally have Zn 2+ or Mn 2+ as the catalytically active metal.