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Journal articles on the topic 'Isopropylmalate synthase'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

Koon, N., C. J. Squire, and E. N. Baker. "Structural studies of isopropylmalate synthase fromMycobacterium tuberculosis." Acta Crystallographica Section A Foundations of Crystallography 64, a1 (2008): C639. http://dx.doi.org/10.1107/s0108767308079178.

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2

Kohlhaw, Gunter B. "Leucine Biosynthesis in Fungi: Entering Metabolism through the Back Door." Microbiology and Molecular Biology Reviews 67, no. 1 (2003): 1–15. http://dx.doi.org/10.1128/mmbr.67.1.1-15.2003.

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SUMMARY After exploring evolutionary aspects of branched-chain amino acid biosynthesis, the review focuses on the extended leucine biosynthetic pathway as it operates in Saccharomyces cerevisiae. First, the genes and enzymes specific for the leucine pathway are considered: LEU4 and LEU9 (encoding the α-isopropylmalate synthase isoenzymes), LEU1 (isopropylmalate isomerase), and LEU2 (β-isopropylmalate dehydrogenase). Emphasis is given to the unusual distribution of the branched-chain amino acid pathway enzymes between mitochondrial matrix and cytosol, on the newly defined role of Leu5p, and on

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3

Li, Fuli, Christoph H. Hagemeier, Henning Seedorf, Gerhard Gottschalk, and Rudolf K. Thauer. "Re-Citrate Synthase from Clostridium kluyveri Is Phylogenetically Related to Homocitrate Synthase and Isopropylmalate Synthase Rather Than to Si-Citrate Synthase." Journal of Bacteriology 189, no. 11 (2007): 4299–304. http://dx.doi.org/10.1128/jb.00198-07.

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ABSTRACT The synthesis of citrate from acetyl-coenzyme A and oxaloacetate is catalyzed in most organisms by a Si-citrate synthase, which is Si-face stereospecific with respect to C-2 of oxaloacetate. However, in Clostridium kluyveri and some other strictly anaerobic bacteria, the reaction is catalyzed by a Re-citrate synthase, whose primary structure has remained elusive. We report here that Re-citrate synthase from C. kluyveri is the product of a gene predicted to encode isopropylmalate synthase. C. kluyveri is also shown to contain a gene for Si-citrate synthase, which explains why cell extr

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4

Xu, Hai, Yuzhen Zhang, Xiaokui Guo, et al. "Isoleucine Biosynthesis in Leptospira interrogans Serotype lai Strain 56601 Proceeds via a Threonine-Independent Pathway." Journal of Bacteriology 186, no. 16 (2004): 5400–5409. http://dx.doi.org/10.1128/jb.186.16.5400-5409.2004.

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ABSTRACT Three leuA-like protein-coding sequences were identified in Leptospira interrogans. One of these, the cimA gene, was shown to encode citramalate synthase (EC 4.1.3.-). The other two encoded α-isopropylmalate synthase (EC 4.1.3.12). Expressed in Escherichia coli, the citramalate synthase was purified and characterized. Although its activity was relatively low, it was strictly specific for pyruvate as the keto acid substrate. Unlike the citramalate synthase of the thermophile Methanococcus jannaschii, the L. interrogans enzyme is temperature sensitive but exhibits a much lower Km (0.04

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5

Drevland, Randy M., Abdul Waheed, and David E. Graham. "Enzymology and Evolution of the Pyruvate Pathway to 2-Oxobutyrate in Methanocaldococcus jannaschii." Journal of Bacteriology 189, no. 12 (2007): 4391–400. http://dx.doi.org/10.1128/jb.00166-07.

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ABSTRACT The archaeon Methanocaldococcus jannaschii uses three different 2-oxoacid elongation pathways, which extend the chain length of precursors in leucine, isoleucine, and coenzyme B biosyntheses. In each of these pathways an aconitase-type hydrolyase catalyzes an hydroxyacid isomerization reaction. The genome sequence of M. jannaschii encodes two homologs of each large and small subunit that forms the hydrolyase, but the genes are not cotranscribed. The genes are more similar to each other than to previously characterized isopropylmalate isomerase or homoaconitase enzyme genes. To identif

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6

de Carvalho, Luiz Pedro S., та John S. Blanchard. "Kinetic and Chemical Mechanism of α-Isopropylmalate Synthase fromMycobacterium tuberculosis†". Biochemistry 45, № 29 (2006): 8988–99. http://dx.doi.org/10.1021/bi0606602.

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7

Yoshida, Ayako, Minoru Yoshida, Tomohisa Kuzuyama, Makoto Nishiyama, and Saori Kosono. "Protein acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27." Extremophiles 23, no. 4 (2019): 377–88. http://dx.doi.org/10.1007/s00792-019-01090-y.

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8

Zhang, Zilong, Jian Wu, Wei Lin та ін. "Subdomain II of α-Isopropylmalate Synthase Is Essential for Activity". Journal of Biological Chemistry 289, № 40 (2014): 27966–78. http://dx.doi.org/10.1074/jbc.m114.559716.

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9

de Carvalho, Luiz P. S., Argyrides Argyrou та John S. Blanchard. "Slow-onset Feedback Inhibition: Inhibition ofMycobacteriumtuberculosisα-Isopropylmalate Synthase byl-Leucine". Journal of the American Chemical Society 127, № 28 (2005): 10004–5. http://dx.doi.org/10.1021/ja052513h.

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10

Beltzer, J. P., S. R. Morris, and G. B. Kohlhaw. "Yeast LEU4 encodes mitochondrial and nonmitochondrial forms of alpha-isopropylmalate synthase." Journal of Biological Chemistry 263, no. 1 (1988): 368–74. http://dx.doi.org/10.1016/s0021-9258(19)57402-6.

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11

Larson, Erica M., та Alexander Idnurm. "Two Origins for the Gene Encoding α-Isopropylmalate Synthase in Fungi". PLoS ONE 5, № 7 (2010): e11605. http://dx.doi.org/10.1371/journal.pone.0011605.

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12

HAGELSTEIN, Petra, and Gernot SCHULTZ. "Leucine Synthesis in Spinach Chloroplasts: Partial Characterization of 2-Isopropylmalate Synthase." Biological Chemistry Hoppe-Seyler 374, no. 7-12 (1993): 1105–8. http://dx.doi.org/10.1515/bchm3.1993.374.7-12.1105.

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13

Yoshida, Ayako, Saori Kosono, and Makoto Nishiyama. "Characterization of two 2-isopropylmalate synthase homologs from Thermus thermophilus HB27." Biochemical and Biophysical Research Communications 501, no. 2 (2018): 465–70. http://dx.doi.org/10.1016/j.bbrc.2018.05.013.

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14

Drain, P., and P. Schimmel. "Multiple new genes that determine activity for the first step of leucine biosynthesis in Saccharomyces cerevisiae." Genetics 119, no. 1 (1988): 13–20. http://dx.doi.org/10.1093/genetics/119.1.13.

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Abstract The first step in the biosynthesis of leucine is catalyzed by alpha-isopropylmalate (alpha-IPM) synthase. In the yeast Saccharomyces cerevisiae, LEU4 encodes the isozyme responsible for the majority of alpha-IPM synthase activity. Yeast strains that bear disruption alleles of LEU4, however, are Leu+ and exhibit a level of synthase activity that is 20% of the wild type. To identify the gene or genes that encode this remaining activity, a leu4 disruption strain was mutagenized. The mutations identified define three new complementation groups, designated leu6, leu7 and leu8. Each of thes

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15

Koon, Nayden, Christopher J. Squire та Edward N. Baker. "Crystallization and preliminary X-ray analysis of α-isopropylmalate synthase fromMycobacterium tuberculosis". Acta Crystallographica Section D Biological Crystallography 60, № 6 (2004): 1167–69. http://dx.doi.org/10.1107/s0907444904009783.

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16

Hunter, Michael F. C., та Emily J. Parker. "Modifying the determinants of α-ketoacid substrate selectivity inmycobacterium tuberculosisα-isopropylmalate synthase". FEBS Letters 588, № 9 (2014): 1603–7. http://dx.doi.org/10.1016/j.febslet.2014.02.053.

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17

Frantom, Patrick A. "Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily". Archives of Biochemistry and Biophysics 519, № 2 (2012): 202–9. http://dx.doi.org/10.1016/j.abb.2011.10.009.

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18

Junk, D. J. "Isolation and expression analysis of the isopropylmalate synthase gene family of Arabidopsis thaliana." Journal of Experimental Botany 53, no. 379 (2002): 2453–54. http://dx.doi.org/10.1093/jxb/erf112.

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19

Chanchaem, W., та P. Palittapongarnpim. "A variable number of tandem repeats result in polymorphic α -isopropylmalate synthase inMycobacterium tuberculosis". Tuberculosis 82, № 1 (2002): 1–6. http://dx.doi.org/10.1054/tube.2001.0314.

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20

Casalone, Enrico, Claudia Barberio, Duccio Cavalieri, and Mario Polsinelli. "Identification by functional analysis of the gene encoding ?-isopropylmalate synthase II (LEU9) inSaccharomyces cerevisiae." Yeast 16, no. 6 (2000): 539–45. http://dx.doi.org/10.1002/(sici)1097-0061(200004)16:6<539::aid-yea547>3.0.co;2-k.

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21

Kouchi, Hiroshi. "GmN56, a Novel Nodule-Specific cDNA from Soybean Root Nodules Encodes a Protein Homologous to Isopropylmalate Synthase and Homocitrate Synthase." Molecular Plant-Microbe Interactions 8, no. 1 (1995): 172. http://dx.doi.org/10.1094/mpmi-8-0172.

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22

Huisman, Frances H. A., Nayden Koon, Esther M. M. Bulloch та ін. "Removal of the C-Terminal Regulatory Domain of α-Isopropylmalate Synthase Disrupts Functional Substrate Binding". Biochemistry 51, № 11 (2012): 2289–97. http://dx.doi.org/10.1021/bi201717j.

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23

de Carvalho, Luiz Pedro S., Patrick A. Frantom, Argyrides Argyrou та John S. Blanchard. "Kinetic Evidence for Interdomain Communication in the Allosteric Regulation of α-Isopropylmalate Synthase fromMycobacterium tuberculosis†". Biochemistry 48, № 9 (2009): 1996–2004. http://dx.doi.org/10.1021/bi801707t.

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24

Chanchaem, Wimon, and Prasit Palittapongarnpim. "The significance and effect of tandem repeats within theMycobacterium tuberculosis leuAgene on Î±-isopropylmalate synthase." FEMS Microbiology Letters 286, no. 2 (2008): 166–70. http://dx.doi.org/10.1111/j.1574-6968.2008.01268.x.

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25

Singh, Kulwant, та Vinod Bhakuni. "Cation induced differential effect on structural and functional properties of Mycobacterium tuberculosis α-Isopropylmalate synthase". BMC Structural Biology 7, № 1 (2007): 39. http://dx.doi.org/10.1186/1472-6807-7-39.

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26

Huisman, Frances H. A., Michael F. C. Hunter, Sean R. A. Devenish, Juliet A. Gerrard та Emily J. Parker. "The C-terminal regulatory domain is required for catalysis by Neisseria meningitidis α-isopropylmalate synthase". Biochemical and Biophysical Research Communications 393, № 1 (2010): 168–73. http://dx.doi.org/10.1016/j.bbrc.2010.01.114.

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27

Wiegel, J. "Leucine biosynthesis in Alcaligenes eutrophus H16: Influence of amino acid additions on the formation of active ?-isopropylmalate synthase and ?-acetohydroxy acid synthase." Archives of Microbiology 142, no. 2 (1985): 194–99. http://dx.doi.org/10.1007/bf00447067.

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28

Pandey, Preeti, Andrew M. Lynn та Pradipta Bandyopadhyay. "Identification of inhibitors against α-Isopropylmalate Synthase of Mycobacterium tuberculosis using docking-MM/PBSA hybrid approach". Bioinformation 13, № 05 (2017): 144–48. http://dx.doi.org/10.6026/97320630013144.

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29

Yoshikawa, Shigetoshi, Isamu Oguri, Kimio Kondo, Mikio Fukuzawa, makoto Shimosaka, and Mitsuo Okazaki. "Enhanced formation of isoamyl alcohol inZygosaccharomyces rouxiidue to elimination of feedback inhibition of Î±-isopropylmalate synthase." FEMS Microbiology Letters 127, no. 1-2 (1995): 139–43. http://dx.doi.org/10.1111/j.1574-6968.1995.tb07463.x.

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30

Suizu, Tetsuyoshi, Kyoko Kotani, Katsuhiro Yasui, Eiji Ichikawa, Akitsugu Kawato та Satoshi Imayasu. "Introduction of a feed back resistant α-isopropylmalate synthase gene of Saccharomyces cerevisiae into sake yeast". Journal of Fermentation and Bioengineering 77, № 2 (1994): 119–24. http://dx.doi.org/10.1016/0922-338x(94)90309-3.

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31

Field, Ben, Caroline Furniss, Andrew Wilkinson, and Richard Mithen. "Expression of a Brassica Isopropylmalate Synthase Gene in Arabidopsis Perturbs Both Glucosinolate and Amino Acid Metabolism." Plant Molecular Biology 60, no. 5 (2006): 717–27. http://dx.doi.org/10.1007/s11103-005-5547-y.

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32

Allers, Thorsten, Hien-Ping Ngo, Moshe Mevarech, and Robert G. Lloyd. "Development of Additional Selectable Markers for the Halophilic Archaeon Haloferax volcanii Based on the leuB and trpA Genes." Applied and Environmental Microbiology 70, no. 2 (2004): 943–53. http://dx.doi.org/10.1128/aem.70.2.943-953.2004.

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ABSTRACT Since most archaea are extremophilic and difficult to cultivate, our current knowledge of their biology is confined largely to comparative genomics and biochemistry. Haloferax volcanii offers great promise as a model organism for archaeal genetics, but until now there has been a lack of a wide variety of selectable markers for this organism. We describe here isolation of H. volcanii leuB and trpA genes encoding 3-isopropylmalate dehydrogenase and tryptophan synthase, respectively, and development of these genes as a positive selection system. ΔleuB and ΔtrpA mutants were constructed i

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33

Frantom, Patrick A., Yuliya Birman, Brittani N. Hays та Ashley K. Casey. "An evolutionarily conserved alternate metal ligand is important for activity in α-isopropylmalate synthase from Mycobacterium tuberculosis". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1844, № 10 (2014): 1784–89. http://dx.doi.org/10.1016/j.bbapap.2014.07.013.

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34

He, Yongqi, Jinping Cheng, Ying He, et al. "Influence of isopropylmalate synthase OsIPMS1 on seed vigour associated with amino acid and energy metabolism in rice." Plant Biotechnology Journal 17, no. 2 (2018): 322–37. http://dx.doi.org/10.1111/pbi.12979.

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35

de Kraker, Jan-Willem, Katrin Luck, Susanne Textor, James G. Tokuhisa, and Jonathan Gershenzon. "Two Arabidopsis Genes (IPMS1 and IPMS2) Encode Isopropylmalate Synthase, the Branchpoint Step in the Biosynthesis of Leucine." Plant Physiology 143, no. 2 (2006): 970–86. http://dx.doi.org/10.1104/pp.106.085555.

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36

Kumar, Garima, та Patrick A. Frantom. "Evolutionarily Distinct Versions of the Multidomain Enzyme α-Isopropylmalate Synthase Share Discrete Mechanisms of V-Type Allosteric Regulation". Biochemistry 53, № 29 (2014): 4847–56. http://dx.doi.org/10.1021/bi500702u.

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37

Yoshikawa, S. "Enhanced formation of isoamyl alcohol in Zygosaccharomyces rouxii due to elimination of feedback inhibition of α-isopropylmalate synthase". FEMS Microbiology Letters 127, № 1-2 (1995): 139–43. http://dx.doi.org/10.1016/0378-1097(95)00053-8.

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38

Kamisaka, Yasushi, Nao Tomita, Kazuyoshi Kimura, Kumiko Kainou та Hiroshi Uemura. "DGA1 (diacylglycerol acyltransferase gene) overexpression and leucine biosynthesis significantly increase lipid accumulation in the Δsnf2 disruptant of Saccharomyces cerevisiae". Biochemical Journal 408, № 1 (2007): 61–68. http://dx.doi.org/10.1042/bj20070449.

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We previously found that SNF2, a gene encoding a transcription factor forming part of the SWI/SNF (switching/sucrose non-fermenting) chromatin-remodelling complex, is involved in lipid accumulation, because the Δsnf2 disruptant of Saccharomyces cerevisiae has a higher lipid content. The present study was conducted to identify other factors that might further increase lipid accumulation in the Δsnf2 disruptant. First, expression of LEU2 (a gene encoding β-isopropylmalate dehydrogenase), which was used to select transformed strains by complementation of the leucine axotroph, unexpectedly increas

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39

López, Geovani, Héctor Quezada, Mariana Duhne та ін. "Diversification of Paralogous α-Isopropylmalate Synthases by Modulation of Feedback Control and Hetero-Oligomerization in Saccharomyces cerevisiae". Eukaryotic Cell 14, № 6 (2015): 564–77. http://dx.doi.org/10.1128/ec.00033-15.

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ABSTRACTProduction of α-isopropylmalate (α-IPM) is critical for leucine biosynthesis and for the global control of metabolism. The budding yeastSaccharomyces cerevisiaehas two paralogous genes,LEU4andLEU9, that encode α-IPM synthase (α-IPMS) isozymes. Little is known about the biochemical differences between these two α-IPMS isoenzymes. Here, we show that the Leu4 homodimer is a leucine-sensitive isoform, while the Leu9 homodimer is resistant to such feedback inhibition. Theleu4Δ mutant, which expresses only the feedback-resistant Leu9 homodimer, grows slowly with either glucose or ethanol and

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40

Casey, Ashley K., Joshua Baugh та Patrick A. Frantom. "The Slow-Onset Nature of Allosteric Inhibition in α-Isopropylmalate Synthase from Mycobacterium tuberculosis Is Mediated by a Flexible Loop". Biochemistry 51, № 24 (2012): 4773–75. http://dx.doi.org/10.1021/bi300671u.

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41

Chang, Li-Fen L., Paula R. Gatzek та Gunter B. Kohlhaw. "Total deletion of yeast LEU4: Further evidence for a second α-isopropylmalate synthase and evidence for tight LEU4-MET4 linkage". Gene 33, № 3 (1985): 333–39. http://dx.doi.org/10.1016/0378-1119(85)90241-0.

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42

de Carvalho, Luiz Pedro S., та John S. Blanchard. "Kinetic analysis of the effects of monovalent cations and divalent metals on the activity of Mycobacterium tuberculosis α-isopropylmalate synthase". Archives of Biochemistry and Biophysics 451, № 2 (2006): 141–48. http://dx.doi.org/10.1016/j.abb.2006.03.030.

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43

Huisman, Frances H. A., Christopher J. Squire та Emily J. Parker. "Amino-acid substitutions at the domain interface affect substrate and allosteric inhibitor binding in α-isopropylmalate synthase from Mycobacterium tuberculosis". Biochemical and Biophysical Research Communications 433, № 2 (2013): 249–54. http://dx.doi.org/10.1016/j.bbrc.2013.02.092.

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44

Casey, Ashley K., Erica L. Schwalm, Brittani N. Hays та Patrick A. Frantom. "V-Type Allosteric Inhibition Is Described by a Shift in the Rate-Determining Step for α-Isopropylmalate Synthase from Mycobacterium tuberculosis". Biochemistry 52, № 39 (2013): 6737–39. http://dx.doi.org/10.1021/bi401186v.

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45

Sugimoto, Nobuko, Philip Engelgau, A. Daniel Jones, Jun Song, and Randolph Beaudry. "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 118, no. 3 (2021): e2009988118. http://dx.doi.org/10.1073/pnas.2009988118.

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A plant pathway that initiates with the formation of citramalate from pyruvate and acetyl-CoA by citramalate synthase (CMS) is shown to contribute to the synthesis of α-ketoacids and important odor-active esters in apple (Malus × domestica) fruit. Microarray screening led to the discovery of a gene with high amino acid similarity to 2-isopropylmalate synthase (IPMS). However, functional analysis of recombinant protein revealed its substrate preference differed substantially from IPMS and was more typical of CMS. MdCMS also lacked the regulatory region present in MdIPMS and was not sensitive to

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46

Kitainda, Vivian, and Joseph M. Jez. "Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes." Antioxidants 10, no. 9 (2021): 1500. http://dx.doi.org/10.3390/antiox10091500.

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Plants evolved specialized metabolic pathways through gene duplication and functional divergence of enzymes involved in primary metabolism. The results of this process are varied pathways that produce an array of natural products useful to both plants and humans. In plants, glucosinolates are a diverse class of natural products. Glucosinolate function stems from their hydrolysis products, which are responsible for the strong flavors of Brassicales plants, such as mustard, and serve as plant defense molecules by repelling insects, fighting fungal infections, and discouraging herbivory. Addition

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47

dos Santos, Margarida Moreira, Andreas Karoly Gombert, Bjarke Christensen, Lisbeth Olsson, and Jens Nielsen. "Identification of In Vivo Enzyme Activities in the Cometabolism of Glucose and Acetate by Saccharomyces cerevisiae by Using 13C-Labeled Substrates." Eukaryotic Cell 2, no. 3 (2003): 599–608. http://dx.doi.org/10.1128/ec.2.3.599-608.2003.

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ABSTRACT A detailed characterization of the central metabolic network of Saccharomyces cerevisiae CEN.PK 113-7D was carried out during cometabolism of different mixtures of glucose and acetate, using aerobic C-limited chemostats in which one of these two substrates was labeled with 13C. To confirm the role of malic enzyme, an isogenic strain with the corresponding gene deleted was grown under the same conditions. The labeling patterns of proteinogenic amino acids were analyzed and used to estimate metabolic fluxes and/or make inferences about the in vivo activities of enzymes of the central ca

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48

Casey, Ashley K., Michael A. Hicks, Jordyn L. Johnson, Patricia C. Babbitt та Patrick A. Frantom. "Mechanistic and Bioinformatic Investigation of a Conserved Active Site Helix in α-Isopropylmalate Synthase fromMycobacterium tuberculosis, a Member of the DRE-TIM Metallolyase Superfamily". Biochemistry 53, № 18 (2014): 2915–25. http://dx.doi.org/10.1021/bi500246z.

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49

Schaufelberger, Myriam, Florian Galbier, Aline Herger, et al. "Mutations in the Arabidopsis ROL17/isopropylmalate synthase 1 locus alter amino acid content, modify the TOR network, and suppress the root hair cell development mutant lrx1." Journal of Experimental Botany 70, no. 8 (2019): 2313–23. http://dx.doi.org/10.1093/jxb/ery463.

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50

Frantom, Patrick A., Hui-Min Zhang, Mark R. Emmett, Alan G. Marshall та John S. Blanchard. "Mapping of the Allosteric Network in the Regulation of α-Isopropylmalate Synthase fromMycobacterium tuberculosisby the Feedback Inhibitorl-Leucine: Solution-Phase H/D Exchange Monitored by FT-ICR Mass Spectrometry". Biochemistry 48, № 31 (2009): 7457–64. http://dx.doi.org/10.1021/bi900851q.

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