Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase

Yashraj S. Kulkarni; Qinghua Liao; Fabian Byléhn; Tina L. Amyes; John P. Richard; Shina C.L. Kamerlin

doi:10.1021/jacs.8b00251

Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase

Yashraj S. Kulkarni
, Qinghua Liao
, Fabian Byléhn
, Tina L. Amyes
, John P. Richard
, Shina C.L. Kamerlin

Chemistry

Uppsala University
University College London

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

Abstract

We have previously performed empirical valence bond calculations of the kinetic activation barriers, ΔG^‡_calc, for the deprotonation of complexes between TIM and the whole substrate glyceraldehyde-3-phosphate (GAP, Kulkarni et al. J. Am. Chem. Soc.

Original language	English
Pages (from-to)	3854-3857
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	140
Issue number	11
DOIs	https://doi.org/10.1021/jacs.8b00251
State	Published - Mar 21 2018

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title = "Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase",

abstract = "We have previously performed empirical valence bond calculations of the kinetic activation barriers, ΔG‡calc, for the deprotonation of complexes between TIM and the whole substrate glyceraldehyde-3-phosphate (GAP, Kulkarni et al. J. Am. Chem. Soc.",

author = "Kulkarni, \{Yashraj S.\} and Qinghua Liao and Fabian Byl{\'e}hn and Amyes, \{Tina L.\} and Richard, \{John P.\} and Kamerlin, \{Shina C.L.\}",

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doi = "10.1021/jacs.8b00251",

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T2 - Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase

AU - Kulkarni, Yashraj S.

AU - Liao, Qinghua

AU - Byléhn, Fabian

AU - Amyes, Tina L.

AU - Richard, John P.

AU - Kamerlin, Shina C.L.

PY - 2018/3/21

Y1 - 2018/3/21

N2 - We have previously performed empirical valence bond calculations of the kinetic activation barriers, ΔG‡calc, for the deprotonation of complexes between TIM and the whole substrate glyceraldehyde-3-phosphate (GAP, Kulkarni et al. J. Am. Chem. Soc.

AB - We have previously performed empirical valence bond calculations of the kinetic activation barriers, ΔG‡calc, for the deprotonation of complexes between TIM and the whole substrate glyceraldehyde-3-phosphate (GAP, Kulkarni et al. J. Am. Chem. Soc.

UR - https://www.scopus.com/pages/publications/85044363575

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DO - 10.1021/jacs.8b00251

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SN - 0002-7863

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SP - 3854

EP - 3857

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 11

ER -

Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase

Abstract

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