4GPE: Crystal Structure of Benzoylformate Decarboxylase Mutant L403M

Citation:
Abstract
It is widely accepted that, in thiamin diphosphate (ThDP)-dependent enzymes, much of the rate acceleration is provided by the cofactor. Inter alia, the reactive conformation of ThDP, known as the V-conformation, has been attributed to the presence of a bulky hydrophobic residue located directly below the cofactor. Here we report the use of site-saturation mutagenesis to generate variants of this residue (Leu403) in benzoylformate decarboxylase. The observed 3 orders of magnitude range in k(cat)/K(m) values suggested that conformational changes in the cofactor could be influencing catalysis. However, X-ray structures of several variants were determined, and there was remarkably little change in ThDP conformation. Rather, it seemed that, once the V-conformation was attained, residue size and hydrophobicity were more important for enzyme activity.
PDB ID: 4GPEDownload
MMDB ID: 110271
PDB Deposition Date: 2012/8/20
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.39  Å
Source Organism:
Similar Structures:
Biological Unit for 4GPE: tetrameric; determined by author and by software (PISA)
Molecular Components in 4GPE
Label Count Molecule
Proteins (4 molecules)
4
Benzoylformate Decarboxylase
Molecule annotation
Chemicals (23 molecules)
1
8
2
3
3
8
4
4
* Click molecule labels to explore molecular sequence information.

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