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Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group
Published on: August 16, 2017
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Structure and function of the LmbE-like superfamily
Shane Viars1, Jason Valentine2, Marcy Hernick3
1Department of Pharmaceutical Sciences, Appalachian College of Pharmacy, Oakwood, VA 24631, USA. sviars@students.acpharm.org.
Biomolecules
|June 28, 2014
Summary
LmbE-like enzymes, crucial metallohydrolases, utilize a single metal ion for substrate hydrolysis. Their diverse structures and functions, particularly as deacetylases, make them key targets for drug development.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- LmbE-like enzymes are a metallohydrolase superfamily utilizing a single catalytic metal ion.
- They process essential eukaryotic and prokaryotic metabolites, presenting significant drug development potential.
- This review focuses on the structure-function relationships of characterized LmbE-like proteins.
Purpose of the Study:
- To review the known structures and functions of the LmbE-like protein superfamily.
- To highlight the structural and functional diversity within this enzyme group.
- To discuss the implications for drug development.
Main Methods:
- Literature review of characterized LmbE-like proteins.
- Analysis of available crystal structures.
- Examination of substrate diversity and catalytic mechanisms.
Main Results:
- LmbE-like proteins exhibit a novel Rossmann fold, distinct for metallohydrolases.
- The majority function as metal-dependent deacetylases, primarily using zinc.
- A conserved His2-Asp-solvent binding site coordinates the catalytic metal ion.
- Protein dynamics are crucial for active site access and catalysis in some members.
Conclusions:
- The LmbE-like superfamily, though recently identified, displays significant structural and functional diversity.
- Their role in metabolizing key substrates and their unique catalytic mechanisms underscore their importance.
- Further research into LmbE-like enzymes holds promise for novel therapeutic strategies.
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