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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.
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References

    1. Campobasso, N., Patel, M., Wilding, I. E., Kallender, H., Rosenberg, M. & Gwynn, M. N. (2004) J. Biol. Chem. 279, 44883–44888. - PubMed
    1. Chun, K. Y., Vinarov, D. A., Zajicek, J. & Miziorko, H. M. (2000) J. Biol. Chem. 275, 17946–17953. - PubMed
    1. Chun, K. Y., Vinarov, D. A. & Miziorko, H. M. (2000) Biochemistry 39, 14670–14681. - PubMed
    1. Greenspan, M. D., Yudkovitz, J. B., Lo, C. Y., Chen, J. S., Alberts, A. W., Hunt, V. M., Chang, M. N., Yang, S. S., Thompson, K. L. & Chiang, Y. C. (1987) Proc. Natl. Acad. Sci. USA 84, 7488–7492. - PMC - PubMed
    1. Miziorko, H. M. & Lane, M. D. (1977) J. Biol. Chem. 252, 1414–1420. - PubMed

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