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Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: Role of enzyme dynamics

Publication ,  Journal Article
Ping, L; Yang, W; Pedersen, LC; Negishi, M; Pedersen, LG
Published in: International Journal of Quantum Chemistry
November 15, 2006

The enzymatic transfer of a sulfuryl group from the ubiquitous biological source of sulfate 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to estrogen is investigated by the pseudo-bond quantum mechanical/molecular mechanical method (QM/MM) method. Calculations of the reaction path are performed starting with models based on two crystal structures, which differ in information about the cofactor and substrates. In addition, a subsequent relaxation of the enzyme was performed with the found transition state frozen, followed by redetermination of the path. An activation barrier of 22 kcal/mol is estimated. The reaction mechanism features a proton transfer from the estrogen to a catalytic histidine followed by the rate determining SO 3 transfer. The mechanism found is largely dissociative. © 2006 Wiley Periodicals, Inc.

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Published In

International Journal of Quantum Chemistry

DOI

EISSN

1097-461X

ISSN

0020-7608

Publication Date

November 15, 2006

Volume

106

Issue

14

Start / End Page

2981 / 2998

Related Subject Headings

  • Chemical Physics
  • 3407 Theoretical and computational chemistry
  • 3406 Physical chemistry
  • 0307 Theoretical and Computational Chemistry
  • 0306 Physical Chemistry (incl. Structural)
 

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Ping, L., Yang, W., Pedersen, L. C., Negishi, M., & Pedersen, L. G. (2006). Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: Role of enzyme dynamics. International Journal of Quantum Chemistry, 106(14), 2981–2998. https://doi.org/10.1002/qua.21123
Ping, L., W. Yang, L. C. Pedersen, M. Negishi, and L. G. Pedersen. “Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: Role of enzyme dynamics.” International Journal of Quantum Chemistry 106, no. 14 (November 15, 2006): 2981–98. https://doi.org/10.1002/qua.21123.
Ping L, Yang W, Pedersen LC, Negishi M, Pedersen LG. Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: Role of enzyme dynamics. International Journal of Quantum Chemistry. 2006 Nov 15;106(14):2981–98.
Ping, L., et al. “Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: Role of enzyme dynamics.” International Journal of Quantum Chemistry, vol. 106, no. 14, Nov. 2006, pp. 2981–98. Scopus, doi:10.1002/qua.21123.
Ping L, Yang W, Pedersen LC, Negishi M, Pedersen LG. Searching for the minimum energy path in the sulfuryl transfer reaction catalyzed by human estrogen sulfotransferase: Role of enzyme dynamics. International Journal of Quantum Chemistry. 2006 Nov 15;106(14):2981–2998.
Journal cover image

Published In

International Journal of Quantum Chemistry

DOI

EISSN

1097-461X

ISSN

0020-7608

Publication Date

November 15, 2006

Volume

106

Issue

14

Start / End Page

2981 / 2998

Related Subject Headings

  • Chemical Physics
  • 3407 Theoretical and computational chemistry
  • 3406 Physical chemistry
  • 0307 Theoretical and Computational Chemistry
  • 0306 Physical Chemistry (incl. Structural)