Identification of Glutamic Acid 381 as a Candidate Active Site Residue ofPseudomonas aeruginosaExoenzyme S†

Biochemistry ◽  
1996 ◽  
Vol 35 (8) ◽  
pp. 2754-2758 ◽  
Author(s):  
Suyan Liu ◽  
Scott M. Kulich ◽  
Joseph T. Barbieri
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Active Site Residue

scholarly journals Evidence that glutamic acid 167 is an active-site residue of Shiga-like toxin I.

1988 ◽  
Vol 85 (8) ◽  
pp. 2568-2572 ◽  
Author(s):  
C. J. Hovde ◽  
S. B. Calderwood ◽  
J. J. Mekalanos ◽  
R. J. Collier
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Active Site Residue

Active-site residue, domain and module swaps in modular polyketide synthases

2003 ◽  
Vol 30 (8) ◽  
pp. 489-494 ◽  
Author(s):  
Francesca Del Vecchio ◽  
Hrvoje Petkovic ◽  
Steven G. Kendrew ◽  
Lindsey Low ◽  
Barrie Wilkinson ◽  
...  
Keyword(s):  
Active Site ◽  
Polyketide Synthases ◽  
Active Site Residue

scholarly journals The Identification of a Glutamic Acid Residue as Part of the Active Site of Ribonuclease T1

1967 ◽  
Vol 242 (20) ◽  
pp. 4682-4690 ◽  
Author(s):  
Kenji Takahashi ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Ribonuclease T1 ◽  
Glutamic Acid Residue

Active site residue involvement in monoamine or diamine oxidation catalysed by pea seedling amine oxidase

FEBS Journal ◽  
2011 ◽  
Vol 278 (8) ◽  
pp. 1232-1243 ◽  
Author(s):  
Maria Luisa Di Paolo ◽  
Michele Lunelli ◽  
Monika Fuxreiter ◽  
Adelio Rigo ◽  
Istvan Simon ◽  
...  
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Active Site Residue ◽  
Pea Seedling

WHICH IS THE PROTON-SHUTTLE IN ISOXANTHOPTERIN DEAMINASE? QM/MM MD UNDERSTANDING

2013 ◽  
Vol 12 (08) ◽  
pp. 1341002 ◽  
Author(s):  
XIN ZHANG ◽  
MING LEI
Keyword(s):  
Crystal Structure ◽  
Molecular Dynamics ◽  
Hydrogen Bonds ◽  
Proton Transfer ◽  
Glutamic Acid ◽  
Active Site ◽  
Nucleophilic Attack ◽  
Zinc Ions ◽  
Initial Model ◽  
Dynamics Simulations

The deamination process of isoxanthopterin catalyzed by isoxanthopterin deaminase was determined using the combined QM(PM3)/MM molecular dynamics simulations. In this paper, the updated PM3 parameters were employed for zinc ions and the initial model was built up based on the crystal structure. Proton transfer and following steps have been investigated in two paths: Asp336 and His285 serve as the proton shuttle, respectively. Our simulations showed that His285 is more effective than Aap336 in proton transfer for deamination of isoxanthopterin. As hydrogen bonds between the substrate and surrounding residues play a key role in nucleophilic attack, we suggested mutating Thr195 to glutamic acid, which could enhance the hydrogen bonds and help isoxanthopterin get close to the active site. The simulations which change the substrate to pterin 6-carboxylate also performed for comparison. Our results provide reference for understanding of the mechanism of deaminase and for enhancing the deamination rate of isoxanthopterin deaminase.

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