Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase

The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO 2 is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO 2 is bound at the base of a narrow hydrophobic substrate...

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Bibliographic Details
Published in:FEBS letters 2011-02, Vol.585 (3), p.459-464
Main Authors: Pandey, Arti S., Mulder, David W., Ensign, Scott A., Peters, John W.
Format: Article
Language:English
Subjects:
1,5-bisphosphate carboxylase/oxidase
2-K-S-CoM
2-ketopropyl coenzyme M
2-ketopropyl coenzyme M oxidoreductase/carboxylase
2-KPCC
Acetoacetate
anions
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biocatalysis
Carbon dioxide
Carbon Dioxide - chemistry
Carbon Dioxide - metabolism
Carboxylase
carboxylation
Catalytic Domain
CHEM
Coenzyme M
coenzyme M (2-mercaptoethanesulfonate)
coenzymes
CoM-SH
Crystallography, X-Ray
Decarboxylation
Disulfide oxidoreductase
DSOR
enzyme substrates
FAD
flavin adenine dinucleotide
hydrophilicity
Hydrophobic and Hydrophilic Interactions
hydrophobicity
Ketone Oxidoreductases - chemistry
Ketone Oxidoreductases - metabolism
Mesna - analogs & derivatives
Mesna - chemistry
Mesna - metabolism
NADP
nicotinamide adenine dinucleotide phosphate
oxidoreductases
Protein Conformation
RMSD
root mean square deviation
Rubisco
water
X-ray diffraction
Xanthobacter - enzymology
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Summary:The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO 2 is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO 2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO 2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H 2O and prevents protonation of the ketopropyl leaving group. 2-KPCC binds to 2-KPCC by x-ray crystallography ( View interaction)
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2010.12.035