Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase-Reference-Cited by-同舟云学术

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Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase

Published:2018-06-04 Issue:26 Volume:140 Page:8277-8286
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Zhai Xiang¹,Reinhardt Christopher J.²^ORCID,Malabanan M. Merced³,Amyes Tina L.¹,Richard John P.¹^ORCID

Affiliation:

1. Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000 United States

2. Department of Chemistry, University of Illinois at Urbana−Champaign, 600 S Mathews Avenue, Urbana, Illinois 61801, United States

3. Department of Biochemistry, Vanderbilt University, 842 Robinson Research Building, Nashville, Tennessee 37205, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

http://pubs.acs.org/doi/pdf/10.1021/jacs.8b04367

Reference52 articles.

1. Perfection in enzyme catalysis: the energetics of triosephosphate isomerase

2. To build an enzyme.

3. Triosephosphate isomerase: a highly evolved biocatalyst

4. Reaction energetics of a mutant triose phosphate isomerase in which the active-site glutamate has been changed to aspartate

5. Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine

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1. Accurate Computation of Aqueous pK_as of Biologically Relevant Organic Acids: Overcoming the Challenges Posed by Multiple Conformers, Tautomeric Equilibria, and Disparate Functional Groups with the Fully Black-Box pK-Yay Method;The Journal of Physical Chemistry A;2023-10-20

2. Triosephosphate Isomerase: The Crippling Effect of the P168A/I172A Substitution at the Heart of an Enzyme Active Site;Biochemistry;2023-09-28

3. The Role of Asn11 in Catalysis by Triosephosphate Isomerase;Biochemistry;2023-05-10

4. Capturing the free energy of transition state stabilization: insights from the inhibition of mandelate racemase;Philosophical Transactions of the Royal Society B: Biological Sciences;2023-01-11

5. Kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces;Methods in Enzymology;2023

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