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2,3-Dihydroxybenzoic Acid Decarboxylase from Fusarium oxysporum: Crystal Structures and Substrate Recognition Mechanism.

Song M, Zhang X, Liu W, Feng J, Cui Y, Yao P, Wang M, Guo RT, Wu Q, Zhu D
Chembiochem 21 2950-2956 (2020)
Related entries: 6m53, 7bpc

Cited: 6 times
EuropePMC logo PMID: 32421914

Abstract

A 2,3-dihydroxybenzoic acid decarboxylase from Fusarium oxysporum (2,3-DHBD_Fo) has a relatively high catalytic efficiency for the decarboxylation of 2,3-dihydroxybenzoic acid (DHBA) and carboxylation of catechol, thus it has a different substrate spectrum from other benzoic acid decarboxylases. We have determined the structures of 2,3-DHBD_Fo in its apo form and complexes with catechol or 2,5-dihydroxybenzoic acid at 1.55, 1.97, and 2.45 Å resolution, respectively. The crystal structures of 2,3-DHBD_Fo show that the enzyme exists as a homotetramer, and each active center has a Zn2+ ion coordinated by E8, H167, D291 and three water molecules. This is different from 2,6-DHBD from Rhizobium sporomusa, in which the Zn2+ ion is also coordinated with H10. Surprisingly, mutation of A10 of 2,3-DHBD_Fo to His resulted in almost complete loss of the enzyme activity. Enzyme-substrate docking and site-directed mutation studies indicate that residue R233Δ interacts with the 3-hydroxy group of 2,3-DHBA, and plays an important role in substrate recognition for this enzyme, thus revealing the molecular basis 2,3-dihydroxybenzoic acid decarboxylase.

Reviews - 7bp1 mentioned but not cited (1)

  1. Enzymatic Conversion of CO2: From Natural to Artificial Utilization. Bierbaumer S, Nattermann M, Schulz L, Zschoche R, Erb TJ, Winkler CK, Tinzl M, Glueck SM. Chem Rev 123 5702-5754 (2023)


Reviews citing this publication (2)

  1. Bright Side of Fusarium oxysporum: Secondary Metabolites Bioactivities and Industrial Relevance in Biotechnology and Nanotechnology. Ibrahim SRM, Sirwi A, Eid BG, Mohamed SGA, Mohamed GA. J Fungi (Basel) 7 943 (2021)
  2. Mechanisms of metal-dependent non-redox decarboxylases from quantum chemical calculations. Sheng X, Himo F. Comput Struct Biotechnol J 19 3176-3186 (2021)

Articles citing this publication (3)

  1. Metal Ion Promiscuity and Structure of 2,3-Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae. Hofer G, Sheng X, Braeuer S, Payer SE, Plasch K, Goessler W, Faber K, Keller W, Himo F, Glueck SM. Chembiochem 22 652-656 (2021)
  2. De novo biosynthesis of 2-hydroxyterephthalic acid, the monomer for high-performance hydroxyl modified PBO fiber, by enzymatic Kolbe-Schmitt reaction with CO2 fixation. Zhou Y, Zhang S, Huang S, Fan X, Su H, Tan T. Biotechnol Biofuels Bioprod 16 179 (2023)
  3. The catalytic mechanism of direction-dependent interactions for 2,3-dihydroxybenzoate decarboxylase. Fan Y, Wu S, Shi J, Li X, Yang Y, Feng Y, Xue S. Appl Microbiol Biotechnol (2023)


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