ArticlePlant physiology2007
Two Arabidopsis genes (IPMS1 and IPMS2) encode isopropylmalate synthase, the branchpoint step in the biosynthesis of leucine.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 98 citations in OpenAlex.
- Review
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- Single Cell Multiomics of Hooked Potato Stolons Reveals Parallels to Shoot Apical Meristems in Arabidopsis.Plant biotechnology journal · 2026Article
- Impact of predictive selection of LbCas12a CRISPR RNAs upon on- and off-target editing rates in soybean.Plant direct · 2024Article
- Multiomics comparative analysis of the maize large grain mutant tc19 identified pathways related to kernel development.BMC genomics · 2023Article
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Proteome and Interactome Linked to Metabolism, Genetic Information Processing, and Abiotic Stress in Gametophytes of Two Woodferns.International journal of molecular sciences · 2023Article
- Comparison of plastid proteomes points towards a higher plastidial redox turnover in vascular tissues than in mesophyll cells.Journal of experimental botany · 2023Article
- A common F-box gene regulates the leucine homeostasis of Medicago truncatula and Arabidopsis thaliana.Protoplasma · 2022Article
- Regulation of the Leucine Metabolism inJournal of fungi (Basel, Switzerland) · 2022Article
- Glucosinolate biosynthesis: role of MAM synthase and its perspectives.Bioscience reports · 2021Article
- Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes.Antioxidants (Basel, Switzerland) · 2021Review
- Protein complex formation in methionine chain-elongation and leucine biosynthesis.Scientific reports · 2021Article
- Citramalate synthase yields a biosynthetic pathway for isoleucine and straight- and branched-chain ester formation in ripening apple fruit.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Overexpression of HMG-CoA synthase promotes Arabidopsis root growth and adversely affects glucosinolate biosynthesis.Journal of experimental botany · 2020Article
- Association Mapping of Seed Quality Traits Under Varying Conditions of Nitrogen Application inFrontiers in genetics · 2020Article
- Genomic Origin and Diversification of the Glucosinolate MAM Locus.Frontiers in plant science · 2020Article
- Homeostasis of branched-chain amino acids is critical for the activity of TOR signaling ineLife · 2019Article
- Harnessing evolutionary diversification of primary metabolism for plant synthetic biology.The Journal of biological chemistry · 2019Review
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Heterologous expression of the Arabidopsis (Arabidopsis thaliana) IPMS1 (At1g18500) and IPMS2 (At1g74040) cDNAs in Escherichia coli yields isopropylmalate synthases (IPMSs; EC 2.3.3.13). These enzymes catalyze the first dedicated step in leucine (Leu) biosynthesis, an aldol-type condensation of acetyl-coenzyme A (CoA) and 2-oxoisovalerate yielding isopropylmalate. Most biochemical properties of IPMS1 and IPMS2 are similar: broad pH optimum around pH 8.5, Mg2+ as cofactor, feedback inhibition by Leu, Km for 2-oxoisovalerate of approximately 300 microM, and a Vmax of approximately 2 x 10(3) micromol min(-1) g(-1). However, IPMS1 and IPMS2 differ in their Km for acetyl-CoA (45 microM and 16 microM, respectively) and apparent quaternary structure (dimer and tetramer, respectively). A knockout insertion mutant for IPMS1 showed an increase in valine content but no changes in Leu content; two insertion mutants for IPMS2 did not show any changes in soluble amino acid content. Apparently, in planta each gene can adequately compensate for the absence of the other, consistent with available microarray and reverse transcription-polymerase chain reaction data that show that both genes are expressed in all organs at all developmental stages. Both encoded proteins accept 2-oxo acid substrates in vitro ranging in length from glyoxylate to 2-oxohexanoate, and catalyze at a low rate the condensation of acetyl-CoA and 4-methylthio-2-oxobutyrate, i.e. a reaction involved in glucosinolate chain elongation normally catalyzed by methylthioalkylmalate synthases. The evolutionary relationship between IPMS and methylthioalkylmalate synthase enzymes is discussed in view of their amino acid sequence identity (60%) and overlap in substrate specificity.
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