7A19

2,3-Dihydroxybenzoate Decarboxylase of Aspergillus oryzae

7A19 の概要

• エントリーDOI: 10.2210/pdb7a19/pdb
• 分子名称: Amidohydrolase 2, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82227.36

構造登録者

Hofer, G.,Keller, W. (登録日: 2020-08-12, 公開日: 2020-10-21, 最終更新日: 2024-01-31)

主引用文献

Hofer, G.,Sheng, X.,Braeuer, S.,Payer, S.E.,Plasch, K.,Goessler, W.,Faber, K.,Keller, W.,Himo, F.,Glueck, S.M.
Metal Ion Promiscuity and Structure of 2,3-Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae.
Chembiochem, 22:652-656, 2021

PubMed Abstract: 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 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 or Mn as the catalytically active metal.

PubMed: 33090643
DOI: 10.1002/cbic.202000600

実験手法

X-RAY DIFFRACTION (1.21 Å)