ArticleApplied and environmental microbiology2012
Structure-guided expansion of the substrate range of methylmalonyl coenzyme A synthetase (MatB) of Rhodopseudomonas palustris.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 45 citations in OpenAlex.
- Engineering of a Malonyl-CoA Ligase for Production of Fluorinated Polyketide Extender Units.Chembiochem : a European journal of chemical biology · 2024Article
- Switching carbon metabolic flux for enhancing the production of sesquiterpene-based high-density biofuel precursor in Saccharomyces cerevisiae.Biotechnology for biofuels and bioproducts · 2023Article
- Nitrogen Fixation Activity and Genome Analysis of a Moderately Haloalkaliphilic Anoxygenic Phototrophic BacteriumMicroorganisms · 2022Article
- High-yield 'one-pot' biosynthesis of raspberry ketone, a high-value fine chemical.Synthetic biology (Oxford, England) · 2021Article
- Cell-free protein synthesis andRSC advances · 2020Article
- A Disjointed Pathway for Malonate Degradation by Rhodopseudomonas palustris.Applied and environmental microbiology · 2020Article
- Cofactor Selectivity in Methylmalonyl Coenzyme A Mutase, a Model Cobamide-Dependent Enzyme.mBio · 2019Article
- Protein Acetylation in Bacteria.Annual review of microbiology · 2019Review
- Acyltransferases as Tools for Polyketide Synthase Engineering.Antibiotics (Basel, Switzerland) · 2018Review
- In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and NMolecular microbiology · 2018Article
- In silico analysis of class I adenylate-forming enzymes reveals family and group-specific conservations.PloS one · 2018Article
- Engineered Fluorine Metabolism and Fluoropolymer Production in Living Cells.Angewandte Chemie (International ed. in English) · 2017Article
- Synthetic metabolism: metabolic engineering meets enzyme design.Current opinion in chemical biology · 2017Review
- Biotransformation of Rutin Using Crude Enzyme from Rhodopseudomonas palustris.Current microbiology · 2017Article
- Development of a range of fluorescent reagentless biosensors for ATP, based on malonyl-coenzyme A synthetase.PloS one · 2017Article
- Insight into Structure-Function Relationships and Inhibition of the Fatty Acyl-AMP Ligase (FadD32) Orthologs from Mycobacteria.The Journal of biological chemistry · 2016Article
- A Fluorescent, Reagentless Biosensor for ATP, Based on Malonyl-Coenzyme A Synthetase.ACS chemical biology · 2015Article
- Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.Microbiology and molecular biology reviews : MMBR · 2015Review
- Structural insights into the substrate specificity of the Rhodopseudomonas palustris protein acetyltransferase RpPat: identification of a loop critical for recognition by RpPat.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Malonyl coenzyme A (malonyl-CoA) and methylmalonyl-CoA are two of the most commonly used extender units for polyketide biosynthesis and are utilized to synthesize a vast array of pharmaceutically relevant products with antibacterial, antiparasitic, anticholesterol, anticancer, antifungal, and immunosuppressive properties. Heterologous hosts used for polyketide production such as Escherichia coli often do not produce significant amounts of methylmalonyl-CoA, however, requiring the introduction of other pathways for the generation of this important building block. Recently, the bacterial malonyl-CoA synthetase class of enzymes has been utilized to generate malonyl-CoA and methylmalonyl-CoA directly from malonate and methylmalonate. We demonstrate that in the purple photosynthetic bacterium Rhodopseudomonas palustris, MatB (RpMatB) acts as a methylmalonyl-CoA synthetase and is required for growth on methylmalonate. We report the apo (1.7-Å resolution) and ATP-bound (2.0-Å resolution) structure and kinetic analysis of RpMatB, which shows similar activities for both malonate and methylmalonate, making it an ideal enzyme for heterologous polyketide biosynthesis. Additionally, rational, structure-based mutagenesis of the active site of RpMatB led to substantially higher activity with ethylmalonate and butylmalonate, demonstrating that this enzyme is a prime target for expanded substrate specificity.
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Registered trials
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