ReviewProtein science : a publication of the Protein Society2011
Structural classification and properties of ketoacyl synthases.
Review in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 62 citations in OpenAlex.
- FabH (β-Ketoacyl-ACP Synthase III) -- Promising Novel Antibacterial Target and Its Inhibitors.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026Review
- Structural basis of VLCFA chain-length determination by the KCS6-CER2 complex in plants.Science advances · 2025Article
- Divergent functional traits and gene expression profiles in native and encroaching plant species across an alpine elevational gradient.Frontiers in plant science · 2025Article
- Properties and predicted functions of large genes and proteins of apicomplexan parasites.NAR genomics and bioinformatics · 2024Article
- Identification of QTLs associated with very-long chain fatty acid (VLCFA) content via linkage mapping and BSA-seq in peanut.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024Article
- The genome of antibiotic-producing colonies of the Pelagophyte alga Chrysophaeum taylorii reveals a diverse and non-canonical capacity for secondary metabolism.Scientific reports · 2023Article
- Article
- Ketosynthase mutants enable short-chain fatty acid biosynthesis in E. coli.Metabolic engineering · 2023Article
- Evolutionary investigations of the biosynthetic diversity in the skin microbiome usingMicrobial genomics · 2023Article
- Mining Fatty Acid Biosynthesis for New Antimicrobials.Annual review of microbiology · 2022Review
- Functional characterization of key polyketide synthases by integrated metabolome and transcriptome analysis on curcuminoid biosynthesis inSynthetic and systems biotechnology · 2022Article
- Genome-wide approaches delineate the additive, epistatic, and pleiotropic nature of variants controlling fatty acid composition in peanut (Arachis hypogaea L.).G3 (Bethesda, Md.) · 2022Article
- Article
- Overexpression of CcNAC1 gene promotes early flowering and enhances drought tolerance of jute (Corchorus capsularis L.).Protoplasma · 2021Article
- A Review of Nervonic Acid Production in Plants: Prospects for the Genetic Engineering of High Nervonic Acid Cultivars Plants.Frontiers in plant science · 2021Review
- Molecular Programming of Drought-ChallengedFrontiers in microbiology · 2021Article
- Kinetic, Structural, and Mutational Analysis of Acyl-CoA Carboxylase FromFrontiers in molecular biosciences · 2020Article
- 3-Ketoacyl-ACP synthase (KAS) III homologues and their roles in natural product biosynthesis.MedChemComm · 2019Review
- Chimeric 6-methylsalicylic acid synthase with domains of acyl carrier protein and methyltransferase from Pseudallescheria boydii shows novel biosynthetic activity.Microbial biotechnology · 2019Article
- Transcriptomic Analysis of Leaf Sheath Maturation in Maize.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ketoacyl synthases (KSs) catalyze condensing reactions combining acyl-CoA or acyl-acyl carrier protein (acyl-ACP) with malonyl-CoA to form 3-ketoacyl-CoA or with malonyl-ACP to form 3-ketoacyl-ACP. In each case, the resulting acyl chain is two carbon atoms longer than before, and CO2 and either CoA or ACP are formed. KSs also join other activated molecules in the polyketide synthesis cycle. Our classification of KSs by their primary and tertiary structures instead of by their substrates and the reactions that they catalyze enhances insights into this enzyme group. KSs fall into five families separated by their characteristic primary structures, each having members with the same catalytic residues, mechanisms, and tertiary structures. KS1 members, overwhelmingly named 3-ketoacyl-ACP synthase III or its variants, are produced predominantly by bacteria. Members of KS2 are mainly produced by plants, and they are usually long-chain fatty acid elongases/condensing enzymes and 3-ketoacyl-CoA synthases. KS3, a very large family, is composed of bacterial and eukaryotic 3-ketoacyl-ACP synthases I and II, often found in multidomain fatty acid and polyketide synthases. Most of the chalcone synthases, stilbene synthases, and naringenin-chalcone synthases in KS4 are from eukaryota. KS5 members are all from eukaryota, most are produced by animals, and they are mainly fatty acid elongases. All families except KS3 are split into subfamilies whose members have statistically significant differences in their primary structures. KS1 through KS4 appear to be part of the same clan. KS sequences, tertiary structures, and family classifications are available on the continuously updated ThYme (Thioester-active enzYme) database.
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