ReviewProtein science : a publication of the Protein Society2000
Substrate-assisted catalysis: molecular basis and biological significance.
Review in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 138 citations in OpenAlex.
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- Biosynthesis of peptide-nucleobase hybrids in ribosomal peptides.Nature chemical biology · 2025Article
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- Reflections on the Origin of Coded Protein Biosynthesis.Biomolecules · 2024Review
- The Atypical Cobalamin-DependentJournal of the American Chemical Society · 2022Article
- Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen.International journal of molecular sciences · 2022Review
- Trapping and structural characterisation of a covalent intermediate in vitamin BRSC chemical biology · 2022Article
- Second-Shell Amino Acid R266 Helps DetermineBiochemistry · 2021Article
- The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The Activation and Selectivity of theFrontiers in molecular biosciences · 2021Article
- Turnip yellow mosaic virus protease binds ubiquitin suboptimally to fine-tune its deubiquitinase activity.The Journal of biological chemistry · 2020Article
- Article
- AnACS catalysis · 2019Article
- Principles of chemical geometry underlying chiral selectivity in RNA minihelix aminoacylation.Nucleic acids research · 2018Article
- Mapping Free Energy Pathways for ATP Hydrolysis in theMolecules (Basel, Switzerland) · 2018Article
- The substrate lends a hand.Nature chemical biology · 2018Article
- A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.Science advances · 2018Article
- Structural insights into simocyclinone as an antibiotic, effector ligand and substrate.FEMS microbiology reviews · 2018Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Substrate-assisted catalysis (SAC) is the process by which a functional group in a substrate contributes to catalysis by an enzyme. SAC has been demonstrated for representatives of three major enzyme classes: serine proteases, GTPases, and type II restriction endonucleases, as well as lysozyme and hexose-1-phosphate uridylyltransferase. Moreover, structure-based predictions of SAC have been made for many additional enzymes. Examples of SAC include both naturally occurring enzymes such as type II restriction endonucleases as well as engineered enzymes including serine proteases. In the latter case, a functional group from a substrate can substitute for a catalytic residue replaced by site-directed mutagenesis. From a protein engineering perspective, SAC provides a strategy for drastically changing enzyme substrate specificity or even the reaction catalyzed. From a biological viewpoint, SAC contributes significantly to the activity of some enzymes and may represent a functional intermediate in the evolution of catalysis. This review focuses on advances in engineering enzyme specificity and activity by SAC, together with the biological significance of this phenomenon.
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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.