Relevant bibliographies by topics / Isopropylmalate synthase

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Isopropylmalate synthase'

Author: Grafiati
Published: 4 June 2021
Last updated: 13 February 2022

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Journal articles on the topic "Isopropylmalate synthase"

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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Isopropylmalate synthase"

1

Huisman, Frances Helen Adam. "Studies into the allosteric regulation of α-isopropylmalate synthase". Thesis, University of Canterbury. Chemistry Department, 2012. http://hdl.handle.net/10092/7599.

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α-Isopropylmalate synthase (α-IPMS) catalyses the first committed step in leucine biosynthesis in bacteria, including Neisseria meningitidis and Mycobacterium tuberculosis. It catalyses the condensation of α-ketoisovalerate (α-KIV) and acetyl coenzyme A (AcCoA) to form α-isopropylmalate (α-IPM). Like many key enzymes in biosynthesis, α-IPMS is inhibited by the end-product of the biosynthetic pathway, in this case leucine. α-IPMS is homodimeric, with monomers consisting of a (β/α)8-barrel catalytic domain, two subdomains and a C-terminal regulatory domain, responsible for binding leucine and pr
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Hunter, Michael Forbes Clifford. "Controlling the substrate specificity of α-isopropylmalate synthase and related enzymes". Thesis, University of Canterbury. Department of Chemistry, 2013. http://hdl.handle.net/10092/8727.

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The enzyme α-isopropylmalate synthase (IPMS) catalyses the reaction between acetyl coenzyme A (AcCoA) and α-ketoisovalerate (KIV) to produce free coenzyme A and α isopropylmalate (IPM). This reaction is a key control point in the biosynthesis of a leucine, a pathway absent in animals but present in plants, fungi and bacteria. As a result, IPMS is a antibiotic and herbicidal target that has been validated by knockout studies for M. tuberculosis, the causative agent of tuberculosis. Engineered IPMSs have also been used in the fermentative production of long chain alcohols for use as fuels. IP
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Clarke, Tyler Brooke. "Studies on the inhibitor selectivity and inhibitory signal transfer of a-Isopropylmalate synthase." Thesis, University of Canterbury. Chemistry, 2013. http://hdl.handle.net/10092/11303.

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α-Isopropylmalate synthase (α-IPMS) is responsible for catalysing the first committed step in leucine biosynthesis. This pathway is found in plants and microorganisms, including pathogenic bacteria such as Mycobacterium tuberculosis and Neisseria meningitidis. α-IPMS catalyses a Claisen condensation reaction between α-ketoisovalerate (KIV) and acetyl coenzyme A (AcCoA) to form the product α-isopropylmalate (IPM). This enzyme undergoes feedback inhibition by the end product of the pathway, leucine. This regulation allows the control of the rate leucine biosynthesis. This project focuses on the
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Bückle-Vallant, Verena Marie [Verfasser]. "2-Ketoisocaproate synthesis in Corynebacterium glutamicum and role of the key enzyme isopropylmalate synthase / Verena Marie Bückle-Vallant." Ulm : Universität Ulm. Fakultät für Naturwissenschaften, 2014. http://d-nb.info/1053380704/34.

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Book chapters on the topic "Isopropylmalate synthase"

1

Schomburg, Dietmar, and Margit Salzmann. "2-Isopropylmalate synthase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_102.

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2

Kohlhaw, Gunter B. "[52] α-Isopropylmalate synthase from yeast." In Methods in Enzymology. Elsevier, 1988. http://dx.doi.org/10.1016/s0076-6879(88)66054-x.

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You might also be interested in the extended bibliographies on the topic 'Isopropylmalate synthase' for particular source types:
Journal articles
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