ArticleBiochemistry2021
Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications.
Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Beyond the β-α-β Fold: Characterization of a SnoaL Domain in the Tautomerase Superfamily.Biochemistry · 2025Article
- Conversion of Inactive Non-Pro1 Tautomerase Superfamily Members into Active Tautomerases: Analysis of the Pro1 Mutants.Biochemistry · 2025Article
- Expanding the viewpoint: Leveraging sequence information in enzymology.Current opinion in chemical biology · 2023Review
- Kinetic, Inhibition, and Structural Characterization of a Malonate Semialdehyde Decarboxylase-like Protein fromBiochemistry · 2022Article
- Comparative Metabolic Pathways Analysis and Subtractive Genomics Profiling to Prioritize Potential Drug Targets AgainstFrontiers in microbiology · 2021Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
The tautomerase superfamily (TSF) is a collection of enzymes and proteins that share a simple β-α-β structural scaffold. Most members are constructed from a single-core β-α-β motif or two consecutively fused β-α-β motifs in which the N-terminal proline (Pro-1) plays a key and unusual role as a catalytic residue. The cumulative evidence suggests that a gene fusion event took place in the evolution of the TSF followed by duplication (of the newly fused gene) to result in the diversification of activity that is seen today. Analysis of the sequence similarity network (SSN) for the TSF identified several linking proteins ("linkers") whose similarity links subgroups of these contemporary proteins that might hold clues about structure-function relationship changes accompanying the emergence of new activities. A previously uncharacterized pair of linkers (designated N1 and N2) was identified in the SSN that connected the 4-oxalocrotonate tautomerase (4-OT) and
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Registered trials
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