ReviewProtein science : a publication of the Protein Society1993
Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.
Review in Protein science : a publication of the Protein Society, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed.
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- Structural insights into strigolactone catabolism by carboxylesterases reveal a conserved conformational regulation.Nature communications · 2024Article
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- Sulfonamide Derivatives: Recent Compounds with Potent Anti-alzheimer's Disease Activity.Central nervous system agents in medicinal chemistry · 2024Review
- Tenuous transcriptional threshold of human sex determination. II. SRY exploits water-mediated clamp at the edge of ambiguity.Frontiers in endocrinology · 2022Article
- Accurate prediction of protein torsion angles using evolutionary signatures and recurrent neural network.Scientific reports · 2021Article
- An Overview of Antennal Esterases in Lepidoptera.Frontiers in physiology · 2021Review
- Improved measures for evolutionary conservation that exploit taxonomy distances.Nature communications · 2019Article
- Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics.Biochemistry · 2018Article
- Protein O-mannosyltransferases are required for sterigmatocystin production and developmental processes in Aspergillus nidulans.Current genetics · 2018Article
- 5,6-Benzoflavones as cholesterol esterase inhibitors: synthesis, biological evaluation and docking studies.MedChemComm · 2018Article
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- CombinedFrontiers in chemistry · 2018Article
- Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.Molecules (Basel, Switzerland) · 2017Review
- Proline-Based Carbamates as Cholinesterase Inhibitors.Molecules (Basel, Switzerland) · 2017Article
45 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on the recently determined X-ray structures of Torpedo californica acetylcholinesterase and Geotrichum candidum lipase and on their three-dimensional superposition, an improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained. On the basis of this alignment, 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved. The conservation in the three remaining sequences is somewhat lower. The conserved residues include the active site, disulfide bridges, salt bridges, and residues in the core of the proteins. Most invariant residues are located at the edges of secondary structural elements. A clear structural basis for the preservation of many of these residues can be determined from comparison of the two X-ray structures.
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