Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (51) ◽  
pp. 15483-15494 ◽  
Author(s):  
Marco G. Casteleijn ◽  
Markus Alahuhta ◽  
Katrin Groebel ◽  
Ibrahim El-Sayed ◽  
Koen Augustyns ◽  
...  
Keyword(s):  
Active Site ◽  
Functional Role ◽  
Triosephosphate Isomerase

scholarly journals Uncovering the Role of Key Active Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalysed by Wild-Type and Variants of Triosephosphate Isomerase

2019 ◽  
Author(s):  
Yashraj S. Kulkarni ◽  
Tina L. Amyes ◽  
John Richard ◽  
Shina Caroline Lynn Kamerlin
Keyword(s):  
Active Site ◽  
Triosephosphate Isomerase ◽  
Valence Bond ◽  
Side Chains ◽  
Wild Type ◽  
Empirical Valence Bond

Manuscript and supporting information outlining an analysis of an extended Brønsted relationship obtained from empirical valence bond simulations of substrate deprotonation catalyzed by wild-type and mutant variants of triosephosphate isomerase.

Functional Role of the Active Site Glutamate-368 in Rat Short Chain Acyl-CoA Dehydrogenase†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15356-15363 ◽  
Author(s):  
Kevin P. Battaile ◽  
Al-Walid A. Mohsen ◽  
Jerry Vockley
Keyword(s):  
Active Site ◽  
Functional Role ◽  
Short Chain ◽  
Chain Acyl

Triosephosphate Isomerase Requires a Positively Charged Active Site: The Role of Lysine-12

Biochemistry ◽  
1994 ◽  
Vol 33 (10) ◽  
pp. 2809-2814 ◽  
Author(s):  
Patricia J. Lodi ◽  
Louise C. Chang ◽  
Jeremy R. Knowles ◽  
Elizabeth A. Komives
Keyword(s):  
Active Site ◽  
Triosephosphate Isomerase ◽  
Positively Charged

scholarly journals Uncovering the Role of Key Active Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalysed by Wild-Type and Variants of Triosephosphate Isomerase

2019 ◽  
Author(s):  
Yashraj S. Kulkarni ◽  
Tina L. Amyes ◽  
John Richard ◽  
Shina Caroline Lynn Kamerlin
Keyword(s):  
Active Site ◽  
Triosephosphate Isomerase ◽  
Valence Bond ◽  
Side Chains ◽  
Wild Type ◽  
Empirical Valence Bond

Manuscript and supporting information outlining an analysis of an extended Brønsted relationship obtained from empirical valence bond simulations of substrate deprotonation catalyzed by wild-type and mutant variants of triosephosphate isomerase.

Probing the Functional Role of Two Conserved Active Site Aspartates in Mouse Adenosine Deaminase†

Biochemistry ◽  
1996 ◽  
Vol 35 (24) ◽  
pp. 7862-7872 ◽  
Author(s):  
Vera Sideraki ◽  
Khalid A. Mohamedali ◽  
David K. Wilson ◽  
Zengyi Chang ◽  
Rodney E. Kellems ◽  
...  
Keyword(s):  
Adenosine Deaminase ◽  
Active Site ◽  
Functional Role

Uncovering the Role of Key Active Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalysed by Wild-Type and Variants of Triosephosphate Isomerase

2019 ◽  
Author(s):  
Yashraj S. Kulkarni ◽  
Tina L. Amyes ◽  
John Richard ◽  
Shina Caroline Lynn Kamerlin
Keyword(s):  
Active Site ◽  
Triosephosphate Isomerase ◽  
Valence Bond ◽  
Side Chains ◽  
Wild Type ◽  
Empirical Valence Bond

Manuscript and supporting information outlining an analysis of an extended Brønsted relationship obtained from empirical valence bond simulations of substrate deprotonation catalyzed by wild-type and mutant variants of triosephosphate isomerase.

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