ReviewMicrobiology and molecular biology reviews : MMBR2001
Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Review in Microbiology and molecular biology reviews : MMBR, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 579 papers, 1 of them a synthesis that pooled it.
What it found
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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
579 citing papers in PubMed, 1 synthesis or guideline pooled it, 2,090 citations in OpenAlex.
- A meta-analysis of the activity, stability, and mutational characteristics of temperature-adapted enzymes.Bioscience reports · 2021Pooled it
- A versatile Bacillus esterase reveals a carboxylesterase blueprint for PET intermediate degradation.Applied microbiology and biotechnology · 2026Article
- Thermostable Carbohydrate-Active Enzymes for High-Temperature Biomass Conversion: From Molecular Design to Process Integration.International journal of molecular sciences · 2026Review
- Enhancing the Versatility of Polyethylene Terephthalate (PET) Through Strategic Biomolecular Functionalization.Angewandte Chemie (International ed. in English) · 2026Review
- Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom.Proteins · 2026Article
- Screening of hyperthermostable proteins from hyperthermophilic archaeon Palaeococcus pacificus DY20341Extremophiles : life under extreme conditions · 2026Article
- The Maximum Growth Temperature for Eukaryotes Is Thermodynamically Driven but Ecologically Contingent.Life (Basel, Switzerland) · 2026Article
- Effect of Storage Duration on Amylase, Protease, and Lipase Activities in Ultrasound-Assisted Extracted Bovine Pancreatin.Molecules (Basel, Switzerland) · 2026Article
- Development of SpyTag/SpyCatcher-driven thermostable cyclic laccase and its application in lignin and dye degradation and polymerization of phenolic compounds.Science China. Life sciences · 2026Article
- Unlocking the unexplored AMPSphere in marine rare species.Microbiome · 2026Article
- Article
- Combined computational, rational, and empirical design of boiling-resistant keratinase.Applied and environmental microbiology · 2026Article
- Iron-Containing Alcohol Dehydrogenase from Hyperthermophiles.Biotech (Basel (Switzerland)) · 2026Review
- Metabarcoding and metagenomic data across aquatic environmental gradients along the coasts of France and Chile.Scientific data · 2026Article
- Targeted mutagenesis of a thermophilic mevalonate kinase for efficient catalysis at lower temperatures.Protein engineering, design & selection : PEDS · 2026Article
- Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026Article
- Hot life in Antarctica: a novel metabolically versatileISME communications · 2026Article
- Article
- Thermostable Bacterial Esterases From Lipase Family 1.5 Degrade Compostable Polyesters PBAT and PBSA.MicrobiologyOpen · 2025Article
- Extremophile-Derived Bioactives in Cosmeceuticals: Bridging Nutraceuticals and Skincare for Holistic Wellness.Life (Basel, Switzerland) · 2025Review
519 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
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth temperatures of > 80 degrees C), also called hyperthermophilic enzymes, are typically thermostable (i.e., resistant to irreversible inactivation at high temperatures) and are optimally active at high temperatures. These enzymes share the same catalytic mechanisms with their mesophilic counterparts. When cloned and expressed in mesophilic hosts, hyperthermophilic enzymes usually retain their thermal properties, indicating that these properties are genetically encoded. Sequence alignments, amino acid content comparisons, crystal structure comparisons, and mutagenesis experiments indicate that hyperthermophilic enzymes are, indeed, very similar to their mesophilic homologues. No single mechanism is responsible for the remarkable stability of hyperthermophilic enzymes. Increased thermostability must be found, instead, in a small number of highly specific alterations that often do not obey any obvious traffic rules. After briefly discussing the diversity of hyperthermophilic organisms, this review concentrates on the remarkable thermostability of their enzymes. The biochemical and molecular properties of hyperthermophilic enzymes are described. Mechanisms responsible for protein inactivation are reviewed. The molecular mechanisms involved in protein thermostabilization are discussed, including ion pairs, hydrogen bonds, hydrophobic interactions, disulfide bridges, packing, decrease of the entropy of unfolding, and intersubunit interactions. Finally, current uses and potential applications of thermophilic and hyperthermophilic enzymes as research reagents and as catalysts for industrial processes are described.
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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.