5O3M

Crystal structure of apo Klebsiella pneumoniae 3,4-dihydroxybenzoic acid decarboxylase (AroY)

Summary for 5O3M

• Entry DOI: 10.2210/pdb5o3m/pdb
• Descriptor: Protocatechuate decarboxylase, pentane-1,5-diol (3 entities in total)
• Functional Keywords: decarboxylase, prfmn, ubid, lyase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 6
• Total formula weight: 338481.04

Authors

Marshall, S.A.,Leys, D. (deposition date: 2017-05-24, release date: 2017-09-13, Last modification date: 2024-05-08)

Primary citation

Payer, S.E.,Marshall, S.A.,Barland, N.,Sheng, X.,Reiter, T.,Dordic, A.,Steinkellner, G.,Wuensch, C.,Kaltwasser, S.,Fisher, K.,Rigby, S.E.J.,Macheroux, P.,Vonck, J.,Gruber, K.,Faber, K.,Himo, F.,Leys, D.,Pavkov-Keller, T.,Glueck, S.M.
Regioselective para-Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase.
Angew. Chem. Int. Ed. Engl., 56:13893-13897, 2017

PubMed Abstract: The utilization of CO as a carbon source for organic synthesis meets the urgent demand for more sustainability in the production of chemicals. Herein, we report on the enzyme-catalyzed para-carboxylation of catechols, employing 3,4-dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD enzyme family. Crystal structures and accompanying solution data confirmed that AroY utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation to form the catalytically competent prFMN species. This study reports on the in vitro reconstitution and activation of a prFMN-dependent enzyme that is capable of directly carboxylating aromatic catechol substrates under ambient conditions. A reaction mechanism for the reversible decarboxylation involving an intermediate with a single covalent bond between a quinoid adduct and cofactor is proposed, which is distinct from the mechanism of prFMN-associated 1,3-dipolar cycloadditions in related enzymes.

PubMed: 28857436
DOI: 10.1002/anie.201708091

Experimental method

X-RAY DIFFRACTION (2.23 Å)