ReviewFrontiers in bioengineering and biotechnology2017
The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.
Review in Frontiers in bioengineering and biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 2 of them syntheses that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
125 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art.Molecules (Basel, Switzerland) · 2023Pooled it
- Lipases: An Overview.Methods in molecular biology (Clifton, N.J.) · 2027Review
- Lipase ITB 2.1: a structure- and function-validated model for anti-obesity drug screening.Molecular diversity · 2026Article
- Microbial lipases: advances in metagenomics and artificial intelligence for enzyme discovery and engineering.Archives of microbiology · 2026Review
- Dairy Spoilage Bacteria and Their Lipases: Prevalence Patterns and Molecular Traits.Foods (Basel, Switzerland) · 2026Article
- Bottom-up reconstruction of synthetic pyrenoids provides insights into the mechanisms and evolution of carbon concentration by EPYC1 proteins.Nature plants · 2026Article
- Removal of Fat from Surfaces by Lipase-Enhanced Purified Water.ACS omega · 2026Article
- From Brewing to Plastic Degradation: Uncovering the Polyurethanase Potential ofJournal of the American Chemical Society · 2026Article
- Enzymatic Hydrolysis of Triacetin and L-Lactide in Emulsified Microparticles Within a Cellulose Hydrogel Dispersion.International journal of molecular sciences · 2026Article
- Purification and Characterization of an Alkaline Lipase fromACS omega · 2026Article
- Exploring the influence of lid region residues on fatty acid selectivity in a lipase originating from Rhizopus oryzae.The FEBS journal · 2026Article
- Revealing the Impact of pH on Lipase Structure and Surface Propensity at the Air-Water Interface and in Aqueous Aerosols.The journal of physical chemistry letters · 2026Article
- Germinated Brown Rice: A Natural Source of Bioactive Compounds Boosting Human Health.International journal of food science · 2026Review
- Dock-and-lock binding of SxIP ligands is required for stable and selective EB1 interactions.eLife · 2025Article
- Synthetic pancreatic lipase inhibitors in obesity treatment: current updates onRSC medicinal chemistry · 2025Review
- Investigation of the potential of phytochemicals derived from citrus peels to inhibit digestive enzymes: an overture to the management of lifestyle diseases.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Immobilized inclusion bodies of recombinant cold-adaptive lipase from Antarctic Pseudomonas sp. as catalysts.Applied microbiology and biotechnology · 2025Article
- Revealing the essential role of the lid in mclPHA intracellular depolymerase from Pseudomonas putida KT2440.Applied microbiology and biotechnology · 2025Article
- Pancreatic Lipase in Eutectogels as Emerging Materials: Exploring Their Properties and Potential Applications in Biosensing.Biosensors · 2025Article
65 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipases are important industrial enzymes. Most of the lipases operate at lipid-water interfaces enabled by a mobile lid domain located over the active site. Lid protects the active site and hence responsible for catalytic activity. In pure aqueous media, the lid is predominantly closed, whereas in the presence of a hydrophobic layer, it is partially opened. Hence, the lid controls the enzyme activity. In the present review, we have classified lipases into different groups based on the structure of lid domains. It has been observed that thermostable lipases contain larger lid domains with two or more helices, whereas mesophilic lipases tend to have smaller lids in the form of a loop or a helix. Recent developments in lipase engineering addressing the lid regions are critically reviewed here. After on, the dramatic changes in substrate selectivity, activity, and thermostability have been reported. Furthermore, improved computational models can now rationalize these observations by relating it to the mobility of the lid domain. In this contribution, we summarized and critically evaluated the most recent developments in experimental and computational research on lipase lids.
Indexed as
Identifiers
What OpenQuestion holds
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.