ArticleThe Journal of biological chemistry2017
Direct evidence that an extended hydrogen-bonding network influences activation of pyridoxal 5'-phosphate in aspartate aminotransferase.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase fromInternational journal of molecular sciences · 2025Article
- Vitamin B6 inhibits activity ofJournal of enzyme inhibition and medicinal chemistry · 2024Article
- Isolation and functional verification of an aspartate aminotransferase gene from Neoporphyra haitanensis.BMC plant biology · 2023Article
- An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction.Chemical science · 2022Article
- Second-Shell Amino Acid R266 Helps DetermineBiochemistry · 2021Article
- Discovery of GOT1 Inhibitors from a Marine-DerivedMarine drugs · 2021Article
- Dietary Vitamin B6 Deficiency Impairs Gut Microbiota and Host and Microbial Metabolites in Rats.Biomedicines · 2020Article
- Substrate Binding Stiffens Aspartate Aminotransferase by Altering the Enzyme Picosecond Vibrational Dynamics.ACS omega · 2020Article
- Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Extreme Catalytic Power of Ketosteroid Isomerase Related to the Reversal of Proton Dislocations in Hydrogen-Bond Network.The journal of physical chemistry. B · 2020Article
- Mechanism of Biocatalytic Friedel-Crafts Acylation by Acyltransferase fromACS catalysis · 2020Article
- Article
- Bioinformatic analysis of the fold type I PLP-dependent enzymes reveals determinants of reaction specificity in l-threonine aldolase fromFEBS open bio · 2018Article
- Dimerization misalignment in human glutamate-oxaloacetate transaminase variants is the primary factor for PLP release.PloS one · 2018Article
- Article
- Direct visualization of critical hydrogen atoms in a pyridoxal 5'-phosphate enzyme.Nature communications · 2017Article
- Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis.Scientific reports · 2017Article
- Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pyridoxal 5'-phosphate (PLP) is a fundamental, multifunctional enzyme cofactor used to catalyze a wide variety of chemical reactions involved in amino acid metabolism. PLP-dependent enzymes optimize specific chemical reactions by modulating the electronic states of PLP through distinct active site environments. In aspartate aminotransferase (AAT), an extended hydrogen bond network is coupled to the pyridinyl nitrogen of the PLP, influencing the electrophilicity of the cofactor. This network, which involves residues Asp-222, His-143, Thr-139, His-189, and structural waters, is located at the edge of PLP opposite the reactive Schiff base. We demonstrate that this hydrogen bond network directly influences the protonation state of the pyridine nitrogen of PLP, which affects the rates of catalysis. We analyzed perturbations caused by single- and double-mutant variants using steady-state kinetics, high resolution X-ray crystallography, and quantum chemical calculations. Protonation of the pyridinyl nitrogen to form a pyridinium cation induces electronic delocalization in the PLP, which correlates with the enhancement in catalytic rate in AAT. Thus, PLP activation is controlled by the proximity of the pyridinyl nitrogen to the hydrogen bond microenvironment. Quantum chemical calculations indicate that Asp-222, which is directly coupled to the pyridinyl nitrogen, increases the p
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