189 related articles for article (PubMed ID: 29516737)
1. Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase.
Kulkarni YS; Liao Q; Byléhn F; Amyes TL; Richard JP; Kamerlin SCL
J Am Chem Soc; 2018 Mar; 140(11):3854-3857. PubMed ID: 29516737
[TBL] [Abstract][Full Text] [Related]
2. Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.
Amyes TL; Richard JP
Biochemistry; 2007 May; 46(19):5841-54. PubMed ID: 17444661
[TBL] [Abstract][Full Text] [Related]
3. Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe.
Richard JP; Cristobal JR; Amyes TL
Acc Chem Res; 2021 May; 54(10):2532-2542. PubMed ID: 33939414
[TBL] [Abstract][Full Text] [Related]
4. Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.
Zhai X; Amyes TL; Wierenga RK; Loria JP; Richard JP
Biochemistry; 2013 Aug; 52(34):5928-40. PubMed ID: 23909928
[TBL] [Abstract][Full Text] [Related]
5. Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change.
Malabanan MM; Amyes TL; Richard JP
J Am Chem Soc; 2011 Oct; 133(41):16428-31. PubMed ID: 21939233
[TBL] [Abstract][Full Text] [Related]
6. Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.
Zhai X; Amyes TL; Richard JP
J Am Chem Soc; 2015 Dec; 137(48):15185-97. PubMed ID: 26570983
[TBL] [Abstract][Full Text] [Related]
7. Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.
Zhai X; Malabanan MM; Amyes TL; Richard JP
J Phys Org Chem; 2014 Apr; 27(4):269-276. PubMed ID: 24729658
[TBL] [Abstract][Full Text] [Related]
8. Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.
Malabanan MM; Go MK; Amyes TL; Richard JP
Biochemistry; 2011 Jun; 50(25):5767-79. PubMed ID: 21553855
[TBL] [Abstract][Full Text] [Related]
9. Specificity in transition state binding: the Pauling model revisited.
Amyes TL; Richard JP
Biochemistry; 2013 Mar; 52(12):2021-35. PubMed ID: 23327224
[TBL] [Abstract][Full Text] [Related]
10. Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clamp.
Malabanan MM; Koudelka AP; Amyes TL; Richard JP
J Am Chem Soc; 2012 Jun; 134(24):10286-98. PubMed ID: 22583393
[TBL] [Abstract][Full Text] [Related]
11. Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.
Kulkarni YS; Liao Q; Petrović D; Krüger DM; Strodel B; Amyes TL; Richard JP; Kamerlin SCL
J Am Chem Soc; 2017 Aug; 139(30):10514-10525. PubMed ID: 28683550
[TBL] [Abstract][Full Text] [Related]
12. Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer.
Reyes AC; Amyes TL; Richard JP
J Am Chem Soc; 2016 Nov; 138(46):15251-15259. PubMed ID: 27792325
[TBL] [Abstract][Full Text] [Related]
13. Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.
Go MK; Koudelka A; Amyes TL; Richard JP
Biochemistry; 2010 Jun; 49(25):5377-89. PubMed ID: 20481463
[TBL] [Abstract][Full Text] [Related]
14. A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
Richard JP
Biochemistry; 2012 Apr; 51(13):2652-61. PubMed ID: 22409228
[TBL] [Abstract][Full Text] [Related]
15. The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.
Reyes AC; Zhai X; Morgan KT; Reinhardt CJ; Amyes TL; Richard JP
J Am Chem Soc; 2015 Jan; 137(3):1372-82. PubMed ID: 25555107
[TBL] [Abstract][Full Text] [Related]
16. Enzyme activation through the utilization of intrinsic dianion binding energy.
Amyes TL; Malabanan MM; Zhai X; Reyes AC; Richard JP
Protein Eng Des Sel; 2017 Mar; 30(3):157-165. PubMed ID: 27903763
[TBL] [Abstract][Full Text] [Related]
17. Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.
Go MK; Amyes TL; Richard JP
Biochemistry; 2009 Jun; 48(24):5769-78. PubMed ID: 19425580
[TBL] [Abstract][Full Text] [Related]
18. Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Richard JP; Amyes TL; Malabanan MM; Zhai X; Kim KJ; Reinhardt CJ; Wierenga RK; Drake EJ; Gulick AM
Biochemistry; 2016 May; 55(21):3036-47. PubMed ID: 27149328
[TBL] [Abstract][Full Text] [Related]
19. Phosphate binding energy and catalysis by small and large molecules.
Morrow JR; Amyes TL; Richard JP
Acc Chem Res; 2008 Apr; 41(4):539-48. PubMed ID: 18293941
[TBL] [Abstract][Full Text] [Related]
20. Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate Isomerase.
Kulkarni YS; Amyes TL; Richard JP; Kamerlin SCL
J Am Chem Soc; 2019 Oct; 141(40):16139-16150. PubMed ID: 31508957
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]