scholarly journals Solvation Response along the Reaction Coordinate in the Active Site of Ketosteroid Isomerase

2010 ◽  
Vol 132 (18) ◽  
pp. 6474-6480 ◽  
Author(s):  
William Childs ◽  
Steven G. Boxer
Keyword(s):  
Active Site ◽  
Reaction Coordinate ◽  
Ketosteroid Isomerase ◽  
Solvation Response

scholarly journals Mass spectrometric studies of a modified active-site tetrapeptide from delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni.

1982 ◽  
Vol 257 (21) ◽  
pp. 12589-12593
Author(s):  
T M Penning ◽  
D N Heller ◽  
T M Balasubramanian ◽  
C C Fenselau ◽  
P Talalay
Keyword(s):  
Active Site ◽  
Mass Spectrometric ◽  
Ketosteroid Isomerase ◽  
Pseudomonas Testosteroni

scholarly journals Globally Optimized Molecular Embeddings for Dynamic Reaction Solvate Shell Optimization and Active Site Design

2021 ◽  
Author(s):  
Dominik M. Behrens ◽  
Bernd Hartke
Keyword(s):  
Global Optimization ◽  
Active Site ◽  
Solvate Shell ◽  
Dynamic Reaction ◽  
Ketosteroid Isomerase ◽  
Recent Interest ◽  
Site Design ◽  
Shell Optimization

AbstractWe demonstrate how a full QM/MM derivatization of the recently developed GOCAT model can be utilized in the global optimization of molecular embeddings. To this end, we provide two distinct examples: An $$\text {S}_\text {N}2$$ S N 2 reaction, and one enzymatic example of recent interest, the ketosteroid isomerase. These serve us to highlight the advantages of such an approach and sketch the roadmap for further improvements.

scholarly journals Mutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B.

1997 ◽  
Vol 179 (24) ◽  
pp. 7742-7747 ◽  
Author(s):  
S W Kim ◽  
S Joo ◽  
G Choi ◽  
H S Cho ◽  
B H Oh ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Aspartic Acid ◽  
Active Site ◽  
Mutational Analysis ◽  
Ketosteroid Isomerase ◽  
Biotype B

Ultraviolet Resonance Raman Spectroscopy of .DELTA.5-3-Ketosteroid Isomerase Revisited: Substrate Polarization by Active-Site Residues

Biochemistry ◽  
1995 ◽  
Vol 34 (13) ◽  
pp. 4441-4447 ◽  
Author(s):  
Janina C. Austin ◽  
Qinjian Zhao ◽  
Trace Jordan ◽  
Paul Talalay ◽  
Albert S. Mildvan ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Active Site ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Active Site Residues ◽  
Ketosteroid Isomerase ◽  
Ultraviolet Resonance Raman Spectroscopy ◽  
Ultraviolet Resonance Raman

Roles of Active Site Aromatic Residues in Catalysis by Ketosteroid Isomerase fromPseudomonas putidaBiotype B†

Biochemistry ◽  
1999 ◽  
Vol 38 (42) ◽  
pp. 13810-13819 ◽  
Author(s):  
Do-Hyung Kim ◽  
Gyu Hyun Nam ◽  
Do Soo Jang ◽  
Gildon Choi ◽  
Soyoung Joo ◽  
...  
Keyword(s):  
Active Site ◽  
Ketosteroid Isomerase ◽  
Aromatic Residues

Catalytic mechanism of an active-site mutant (D38N) of .DELTA.5-3-ketosteroid isomerase

Biochemistry ◽  
1991 ◽  
Vol 30 (20) ◽  
pp. 4991-4997 ◽  
Author(s):  
Liang Xue ◽  
Athan Kuliopulos ◽  
Albert S. Mildvan ◽  
Paul Talalay
Keyword(s):  
Active Site ◽  
Catalytic Mechanism ◽  
Ketosteroid Isomerase

scholarly journals Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site

2013 ◽  
Vol 110 (28) ◽  
pp. E2552-E2561 ◽  
Author(s):  
P. A. Sigala ◽  
A. T. Fafarman ◽  
J. P. Schwans ◽  
S. D. Fried ◽  
T. D. Fenn ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Proton Transfer ◽  
Active Site ◽  
Ketosteroid Isomerase

scholarly journals Proton Affinity of the Oxyanion Hole in the Active Site of Ketosteroid Isomerase

Biochemistry ◽  
2010 ◽  
Vol 49 (12) ◽  
pp. 2725-2731 ◽  
Author(s):  
William Childs ◽  
Steven G. Boxer
Keyword(s):  
Proton Affinity ◽  
Active Site ◽  
Ketosteroid Isomerase ◽  
Oxyanion Hole

scholarly journals A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase

2020 ◽  
Author(s):  
Yufan Wu ◽  
Stephen Fried ◽  
Steven Boxer
Keyword(s):  
Electric Field ◽  
Electric Fields ◽  
Ground State ◽  
Active Site ◽  
Electrostatic Interactions ◽  
Stark Effect ◽  
Structural Changes ◽  
Enzymatic Catalysis ◽  
Ketosteroid Isomerase ◽  
Computational Enzyme Design

<div><p>Electrostatic interactions play a pivotal role in enzymatic catalysis and are increasingly modeled explicitly in computational enzyme design; nevertheless, they are challenging to measure experimentally. Using vibrational Stark effect (VSE) spectroscopy, we have measured electric fields inside the active site of the enzyme ketosteroid isomerase (KSI). These studies have shown that these fields can be unusually large, but it has been unclear to what extent they specifically stabilize the transition state (TS) relative to a ground state (GS). In the following, we use crystallography and computational modeling to show that KSI’s intrinsic electric field is nearly perfectly oriented to stabilize the geometry of its reaction’s TS. Moreover, we find that this electric field adjusts the orientation of its substrate in the ground state so that the substrate needs to only undergo minimal structural changes upon activation to its TS. This work provides evidence that the active site electric field in KSI is preorganized to facilitate catalysis and provides a template for how electrostatic preorganization can be measured in enzymatic systems. <br></p></div>

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