An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction-Reference-Cited by-同舟云学术

An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction

Published:2022 Issue:34 Volume:13 Page:10057-10065
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Drago Victoria N.¹²,Dajnowicz Steven¹²,Parks Jerry M.³^ORCID,Blakeley Matthew P.⁴^ORCID,Keen David A.⁵^ORCID,Coquelle Nicolas⁴,Weiss Kevin L.²,Gerlits Oksana⁶,Kovalevsky Andrey²^ORCID,Mueser Timothy C.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, University of Toledo, Toledo, OH 43606, USA

2. Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA

3. Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA

4. Large Scale Structures Group, Institut Laue–Langevin, 71 Avenue des Martyrs, 38000 Grenoble, France

5. ISIS Facility, Rutherford Appleton Laboratory, Harwell Campus, Didcot, OX11 0QX, UK

6. Department of Natural Sciences, Tennessee Wesleyan University, Athens, TN 37303, USA

Abstract

The neutron structure of pyridoxal 5′-phosphate-dependent enzyme aspartate aminotransferase with pyridoxamine 5′-phosphate (PMP) reveals a low-barrier hydrogen bond between the amino groups of PMP and catalytic Lys258, preorganizing the active site for catalysis

Funder

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D2SC02285K

Reference52 articles.

1. A genomic overview of pyridoxal‐phosphate‐dependent enzymes

2. Pyridoxal 5′-phosphate dependent reactions: Analyzing the mechanism of aspartate aminotransferase

3. Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations