ArticleProceedings of the National Academy of Sciences of the United States of America1998
Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 82 citations in OpenAlex.
- Current successes and remaining challenges in protein function prediction.Frontiers in bioinformatics · 2023Article
- The Birth of Genomic Enzymology: Discovery of the Mechanistically Diverse Enolase Superfamily.Biochemistry · 2021Article
- Sequence-Based Screening for Rare Enzymes: New Insights into the World of AMDases Reveal a Conserved Motif and 58 Novel Enzymes Clustering in Eight Distinct Families.Frontiers in microbiology · 2016Article
- Functional evolution of PLP-dependent enzymes based on active-site structural similarities.Proteins · 2014Article
- Using catalytic atom maps to predict the catalytic functions present in enzyme active sites.Biochemistry · 2012Article
- Modeling regionalized volumetric differences in protein-ligand binding cavities.Proteome science · 2012Article
- Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate.The Journal of biological chemistry · 2012Article
- FINDSITE: a combined evolution/structure-based approach to protein function prediction.Briefings in bioinformatics · 2009Review
- Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes.Biochemistry · 2009Article
- Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases.Biochemistry · 2006Article
- FAST-NMR: functional annotation screening technology using NMR spectroscopy.Journal of the American Chemical Society · 2006Article
- A domain for editing by an archaebacterial tRNA synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families.Protein science : a publication of the Protein Society · 2004Article
- Finding evolutionary relations beyond superfamilies: fold-based superfamilies.Protein science : a publication of the Protein Society · 2003Article
- The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function.Protein science : a publication of the Protein Society · 2003Article
- Expanding protein universe and its origin from the biological Big Bang.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Mutations in catB, the gene encoding muconate cycloisomerase, activate transcription of the distal ben genes and contribute to a complex regulatory circuit in Acinetobacter sp. strain ADP1.Journal of bacteriology · 2000Article
- Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Muconate lactonizing enzyme (MLE), a component of the beta-ketoadipate pathway of Pseudomonas putida, is a member of a family of related enzymes (the "enolase superfamily") that catalyze the abstraction of the alpha-proton of a carboxylic acid in the context of different overall reactions. New untwinned crystal forms of MLE were obtained, one of which diffracts to better than 2.0-A resolution. The packing of the octameric enzyme in this crystal form is unusual, because the asymmetric unit contains three subunits. The structure of MLE presented here contains no bound metal ion, but is very similar to a recently determined Mn2+-bound structure. Thus, absence of the metal ion does not perturb the structure of the active site. The structures of enolase, mandelate racemase, and MLE were superimposed. A comparison of metal ligands suggests that enolase may retain some characteristics of the ancestor of this enzyme family. Comparison of other residues involved in catalysis indicates two unusual patterns of conservation: (i) that the position of catalytic atoms remains constant, although the residues that contain them are located at different points in the protein fold; and (ii) that the positions of catalytic residues in the protein scaffold are conserved, whereas their identities and roles in catalysis vary.
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