4OVI: Phenylacetone Monooxygenase: Oxidised Enzyme In Complex With Apadp

Citation:
Abstract
A general question in biochemistry is the interplay between the chemical properties of cofactors and the surrounding protein matrix. Here, the functions of NADP+ and FAD are explored by investigation of a representative monooxygenase reconstituted with chemically-modified cofactor analogues. Like pieces of a jigsaw puzzle, the enzyme active site juxtaposes the flavin and nicotinamide rings, harnessing their H-bonding and steric properties to finely construct an oxygen-reacting center that restrains the flavin-peroxide intermediate in a catalytically-competent orientation. Strikingly, the regio- and stereoselectivities of the reaction are essentially unaffected by cofactor modifications. These observations indicate a remarkable robustness of this complex multi-cofactor active site, which has implications for enzyme design based on cofactor engineering approaches.
PDB ID: 4OVIDownload
MMDB ID: 120348
PDB Deposition Date: 2013/9/19
Updated in MMDB: 2014/05
Experimental Method:
x-ray diffraction
Resolution: 1.87  Å
Source Organism:
Similar Structures:
Biological Unit for 4OVI: monomeric; determined by software (PISA)
Molecular Components in 4OVI
Label Count Molecule
Protein (1 molecule)
1
Phenylacetone Monooxygenase
Molecule annotation
Chemicals (6 molecules)
1
1
2
1
3
1
4
1
5
1
6
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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