ArticleProteins2011
The evolution of function in strictosidine synthase-like proteins.
Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
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- Origin and evolution of signaling pathways responsible for ascorbic acid synthesis and catabolism during plant terrestrialization.Horticulture research · 2025Article
- Candidate Genes for the High-Altitude Adaptations of Two Mountain Pine Taxa.International journal of molecular sciences · 2021Article
- Global analysis of adenylate-forming enzymes reveals β-lactone biosynthesis pathway in pathogenicThe Journal of biological chemistry · 2020Article
- A comprehensive in silico analysis of sortase superfamily.Journal of microbiology (Seoul, Korea) · 2019Article
- Functional features of the "finger" domain of the DEG/ENaC channels MEC-4 and UNC-8.American journal of physiology. Cell physiology · 2018Article
- Evolutionary and molecular foundations of multiple contemporary functions of the nitroreductase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Biocuration in the structure-function linkage database: the anatomy of a superfamily.Database : the journal of biological databases and curation · 2017Article
- Caenorhabditis elegans paraoxonase-like proteins control the functional expression of DEG/ENaC mechanosensory proteins.Molecular biology of the cell · 2016Article
- Subunit composition of a DEG/ENaC mechanosensory channel of Caenorhabditis elegans.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks.Biochimica et biophysica acta · 2015Review
- New insights about enzyme evolution from large scale studies of sequence and structure relationships.The Journal of biological chemistry · 2014Review
- Hydrolysis of DFP and the nerve agent (S)-sarin by DFPase proceeds along two different reaction pathways: implications for engineering bioscavengers.The journal of physical chemistry. B · 2014Article
- Root parasitic plant Orobanche aegyptiaca and shoot parasitic plant Cuscuta australis obtained Brassicaceae-specific strictosidine synthase-like genes by horizontal gene transfer.BMC plant biology · 2014Article
- The Structure-Function Linkage Database.Nucleic acids research · 2014Article
- Protein similarity networks reveal relationships among sequence, structure, and function within the Cupin superfamily.PloS one · 2013Article
- Crystal structure of perakine reductase, founding member of a novel aldo-keto reductase (AKR) subfamily that undergoes unique conformational changes during NADPH binding.The Journal of biological chemistry · 2012Article
- Inference of functional properties from large-scale analysis of enzyme superfamilies.The Journal of biological chemistry · 2012Review
- Enzyme informatics.Current topics in medicinal chemistry · 2012Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The exponential growth of sequence data provides abundant information for the discovery of new enzyme reactions. Correctly annotating the functions of highly diverse proteins can be difficult, however, hindering use of this information. Global analysis of large superfamilies of related proteins is a powerful strategy for understanding the evolution of reactions by identifying catalytic commonalities and differences in reaction and substrate specificity, even when only a few members have been biochemically or structurally characterized. A comparison of >2500 sequences sharing the six-bladed β-propeller fold establishes sequence, structural, and functional links among the three subgroups of the functionally diverse N6P superfamily: the arylesterase-like and senescence marker protein-30/gluconolactonase/luciferin-regenerating enzyme-like (SGL) subgroups, representing enzymes that catalyze lactonase and related hydrolytic reactions, and the so-called strictosidine synthase-like (SSL) subgroup. Metal-coordinating residues were identified as broadly conserved in the active sites of all three subgroups except for a few proteins from the SSL subgroup, which have been experimentally determined to catalyze the quite different strictosidine synthase (SS) reaction, a metal-independent condensation reaction. Despite these differences, comparison of conserved catalytic features of the arylesterase-like and SGL enzymes with the SSs identified similar structural and mechanistic attributes between the hydrolytic reactions catalyzed by the former and the condensation reaction catalyzed by SS. The results also suggest that despite their annotations, the great majority of these >500 SSL sequences do not catalyze the SS reaction; rather, they likely catalyze hydrolytic reactions typical of the other two subgroups instead. This prediction was confirmed experimentally for one of these proteins.
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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.