4UU3

Ferulic acid decarboxylase from Enterobacter sp.

Summary for 4UU3

• Entry DOI: 10.2210/pdb4uu3/pdb
• Related: 4UU2
• Descriptor: FERULIC ACID DECARBOXYLASE (2 entities in total)
• Functional Keywords: lyase
• Biological source: ENTEROBACTER SP.
• Total number of polymer chains: 2
• Total formula weight: 38426.93

Authors

Hromic, A.,Pavkov-Keller, T.,Steinkellner, G.,Lyskowski, A.,Wuensch, C.,Gross, J.,Fuchs, M.,Fauland, K.,Glueck, S.M.,Faber, K.,Gruber, K. (deposition date: 2014-07-24, release date: 2015-06-10, Last modification date: 2024-01-10)

Primary citation

Wuensch, C.,Pavkov-Keller, T.,Steinkellner, G.,Gross, J.,Fuchs, M.,Hromic, A.,Lyskowski, A.,Fauland, K.,Gruber, K.,Glueck, S.M.,Faber, K.
Regioselective Enzymatic Beta-Carboxylation of Para-Hydroxy-Styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases.
Adv. Synth. Catal., 357:1909-, 2015

PubMed Abstract: We report on a 'green' method for the utilization of carbon dioxide as C unit for the regioselective synthesis of ()-cinnamic acids regioselective enzymatic carboxylation of -hydroxystyrenes. Phenolic acid decarboxylases from bacterial sources catalyzed the β-carboxylation of -hydroxystyrene derivatives with excellent regio- and (/)-stereoselectivity by exclusively acting at the β-carbon atom of the C=C side chain to furnish the corresponding ()-cinnamic acid derivatives in up to 40% conversion at the expense of bicarbonate as carbon dioxide source. Studies on the substrate scope of this strategy are presented and a catalytic mechanism is proposed based on molecular modelling studies supported by mutagenesis of amino acid residues in the active site.

PubMed: 26190963
DOI: 10.1002/ADSC.201401028

Experimental method

X-RAY DIFFRACTION (1.15 Å)