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Comment
. 2004 Nov 23;101(47):16399-400.
doi: 10.1073/pnas.0407418101. Epub 2004 Nov 16.

An atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl-CoA synthase

Brian J Bahnson  1
Affiliations
Comment

An atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl-CoA synthase

Brian J Bahnson. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
The mechanism of HMG-CoA synthase has been elucidated by enzyme intermediate structures of the acetylated-enzyme AcAc-CoA complex (blue) and the covalent HMG-CoA-enzyme complex (purple) (7). The overall reaction of acetyl-CoA and AcAc-CoA to produce HMG-CoA is depicted in three phases. (A) Acetylation/deacetylation. The substrates bind to the enzyme with the acetyl-CoA, forming a covalent acetylated-cysteine intermediate. (B) Condensation/cleavage. Upon dissociation of the CoASH, the second substrate AcAc-CoA enters the active site, forming the acetylated-enzyme AcAc-CoA complex shown in blue. The condensation reaction is shown going through an enolate intermediate to form the covalent HMG-CoA-enzyme complex shown in purple. (C) Hydrolysis/dehydration. The final phase of the overall reaction is the hydrolysis of the covalent HMG-CoA-enzyme complex, which occurs through a tetrahedral intermediate to form HMG-CoA as the sole product of the reaction. The chemically challenging step for this reaction is the condensation step that features the formation of a carbon–carbon bond.
See this image and copyright information in PMC

Comment on

References

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Substances

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