Uncovering structural features that control substrate specificity in a Lactobacillus chlorogenic acid esterase
Omori, K. K.; Okumura, T. L. S.; Carl, N. B.; Dinn, B. T.; Ly, D.; Sacapano, K. N.; Tajii, A.; Owens, C. P.
Show abstract
The structural determinants of chlorogenic acid esterase (CE) substrate specificity are poorly understood. Here, we establish how a Lactobacillus helveticus CE selects for its substrate, chlorogenic acid (CGA). We determine that a Lys residue in an extended loop over the active site imparts substrate specificity by hydrogen bonding to CGA. Mutation of the Lys residue abolishes CGA specificity. Comparison with other bacterial CEs reveals that the extended loop is not conserved. However, the hydrogen bonding functionality to CGA is preserved thanks to other residues. Structural comparison with ferulic acid esterases (FAEs), a related enzyme class, shows that CEs feature a more restricted active site, reflecting the fact that they hydrolyze smaller substrates compared to FAEs.
Matching journals
The top 8 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Itaconate utilisation by the human pathogen Pseudomonas aeruginosa requires uptake via the IctPQM TRAP transporter 94%
- Flexibility of Short-chain dehydrogenase is interconnected to its promiscuity for the reduction of multiple ketone intermediates 94%
- Thioproline formation as a driver of formaldehyde toxicity in Escherichia coli 93%
Similar papers in this journal
- Mechanistic implications of the ternary complex structural models for the photoenzyme protochlorophyllide oxidoreductase. 95%
- Discovery and mechanistic characterization of a probiotic-origin 3β-OH-Δ5-6-cholesterol-5β-reductase directly converting cholesterol to coprostanol 94%
- Paradigms of convergent evolution in enzymes 94%
Similar papers in this journal
- Kinetic Characterization and Computational Modeling of the Escherichia coli Heptosyltransferase II: Exploring the Role of Protein Dynamics in Catalysis for a GT-B Glycosyltransferase 93%
- Structural basis for the allosteric regulation of the SbtA bicarbonate transporter by the PII-like protein, SbtB, from Cyanobium sp. PCC7001 93%
- Phytolacca americana PaGT2 is an ambidextrous polyphenol glucosyltransferase 92%
Similar papers in this journal
- The β-lactam Ticarcillin is a Staphylococcus aureus UDP-N-acetylglucosamine 2-epimerase binder. 94%
- Sucrose phosphorylase from Alteromonas mediterranea: structural insight into the regioselective α-glucosylation of (+)-catechin 93%
- Structural and thermodynamic analyses of human TMED1 (p24γ1) Golgi dynamics 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.