2AG0

Crystal structure of Benzaldehyde lyase (BAL)- native

Summary for 2AG0

• Entry DOI: 10.2210/pdb2ag0/pdb
• Related: 2AG1
• Descriptor: benzaldehyde lyase, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: thdp dependent fold, tetramer, lyase
• Biological source: Pseudomonas fluorescens
• Total number of polymer chains: 4
• Total formula weight: 237702.90

Authors

Mosbacher, T.G.,Mueller, M.,Schulz, G.E. (deposition date: 2005-07-26, release date: 2006-01-24, Last modification date: 2024-03-13)

Primary citation

Mosbacher, T.G.,Mueller, M.,Schulz, G.E.
Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens
Febs J., 272:6067-6076, 2005

PubMed Abstract: Pseudomonas fluorescens is able to grow on R-benzoin as the sole carbon and energy source because it harbours the enzyme benzaldehyde lyase that cleaves the acyloin linkage using thiamine diphosphate (ThDP) as a cofactor. In the reverse reaction, this lyase catalyses the carboligation of two aldehydes with high substrate and stereospecificity. The enzyme structure was determined by X-ray diffraction at 2.6 A resolution. A structure-based comparison with other proteins showed that benzaldehyde lyase belongs to a group of closely related ThDP-dependent enzymes. The ThDP cofactors of these enzymes are fixed at their two ends in separate domains, suspending a comparatively mobile thiazolium ring between them. While the residues binding the two ends of ThDP are well conserved, the lining of the active centre pocket around the thiazolium moiety varies greatly within the group. Accounting for the known reaction chemistry, the natural substrate R-benzoin was modelled unambiguously into the active centre of the reported benzaldehyde lyase. Due to its substrate spectrum and stereospecificity, the enzyme extends the synthetic potential for carboligations appreciably.

PubMed: 16302970
DOI: 10.1111/j.1742-4658.2005.04998.x

Experimental method

X-RAY DIFFRACTION (2.58 Å)