ArticleScientific reports2017
A half-site multimeric enzyme achieves its cooperativity without conformational changes.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Negative allosteric regulation of protein arginine methyltransferase 1 (PRMT1) through half-of-sites reactivity.The Journal of biological chemistry · 2026Article
- Article
- Potentiating Activity of GmhA Inhibitors on Gram-Negative Bacteria.Journal of medicinal chemistry · 2024Article
- Structural Basis of Sequential and Concerted Cooperativity.Biomolecules · 2022Article
- The 3D-structure, kinetics and dynamics of the E. coli nitroreductase NfsA with NADPFEBS letters · 2022Article
- Intersubunit Coupling Enables Fast COACS central science · 2022Article
- Allosteric signaling in C-linker and cyclic nucleotide-binding domain of HCN2 channels.Biophysical journal · 2021Article
- Biochemical and structural characterization of two cif-like epoxide hydrolases fromCurrent research in structural biology · 2021Article
- Structural and functional characterization of M. tuberculosis sedoheptulose- 7-phosphate isomerase, a critical enzyme involved in lipopolysaccharide biosynthetic pathway.Scientific reports · 2020Article
- Insight into natural inhibitors and bridging docking to dynamic simulation against sugar Isomerase (SIS) domain protein.Journal of molecular modeling · 2020Article
- Proximity-induced caspase-9 activation on a DNA origami-based synthetic apoptosome.Nature catalysis · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Cooperativity is a feature many multimeric proteins use to control activity. Here we show that the bacterial heptose isomerase GmhA displays homotropic positive and negative cooperativity among its four protomers. Most similar proteins achieve this through conformational changes: GmhA instead employs a delicate network of hydrogen bonds, and couples pairs of active sites controlled by a unique water channel. This network apparently raises the Lewis acidity of the catalytic zinc, thus increasing the activity at one active site at the cost of preventing substrate from adopting a reactive conformation at the paired negatively cooperative site - a "half-site" behavior. Our study establishes the principle that multimeric enzymes can exploit this cooperativity without conformational changes to maximize their catalytic power and control. More broadly, this subtlety by which enzymes regulate functions could be used to explore new inhibitor design strategies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.