Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.3.3.1 (citrate synthase)
4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

VanDemark, P. J. (Cornell University, Ithaca, N.Y.), and P. F. Smith. Evidence for a tricarboxylic acid cycle in Mycoplasma hominis. J. Bacteriol. 88:1602-1607. 1964.-Resting cells of acetate-grown Mycoplasma hominis strain 07 oxidized the various intermediates of the tricarboxylic and glyoxylate cycles, with the exception of sodium citrate and glyoxylate. Extracts of these cells possessed isocitric dehydrogenase, isocitratase, alpha-ketoglutaric dehydrogenase, succinic dehydrogenase, fumarase, malic dehydrogenase, citratase, and acetyl coenzyme A kinase activities. With the assay conditions employed, condensing enzyme, malate synthetase, and phosphotransacetylase activities were negligible. Incubation of sodium acetate-2-C(14) with the various intermediates of the tricarboxylic acid cycle in the presence of cell-free extracts resulted in exchange of the isotope with these compounds as well as the formation of other labeled intermediates of the tricarboxylic acid cycle. Oxidation of sodium acetate-2-C(14) alone resulted in the formation of labeled succinate, fumarate, and malate.
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PMID:EVIDENCE FOR A TRICARBOXYLIC ACID CYCLE IN MYCOPLASMA HOMINIS. 1424 Sep 45

Smith, Paul F. (University of South Dakota, Vermillion), and C. V. Henrikson. Comparative biosynthesis of mevalonic acid by Mycoplasma. J. Bacteriol. 89:146-153. 1965.-Three representative Mycoplasma, M. laidlawii strain B, M. gallisepticum strain J, and M. hominis strain 07, were examined for the presence or absence of enzymes associated with the biosynthetic pathway to mevalonic acid. M. laidlawii served as a control, because it synthesizes carotenoids from acetate. M. laidlawii was shown to contain a specific acetokinase and phosphotransacetylase for the synthesis of acetyl coenzyme A, and a beta-ketothiolase and coenzyme A transferase for the synthesis of acetoacetyl coenzyme A. M. gallisepticum contained a specific acetokinase, phosphotransacetylase, and possibly an aceto coenzyme A kinase forming acetyl coenzyme A; it also contained a beta-ketothiolase, a coenzyme A transferase, and a coenzyme A transphorase forming acetoacetyl coenzyme A directly or indirectly. The beta-ketothiolase of M. gallisepticum was not affected by iodoacetamide, in contrast to the other two strains. M. laidlawii exhibited beta-hydroxy-beta-methylglutaryl coenzyme A condensing enzyme, and M. hominis did not. This activity of M. gallisepticum was masked by thiolase activity. M. laidlawii and M. gallisepticum contained a nicotinamide adenine dinucleotide phosphate-linked beta-hydroxy-beta-methylglutaryl coenzyme A reductase, and M. hominis did not. C(14)-labeled acetate was incorporated into mevalonic acid only by M. laidlawii and M. gallisepticum. The lack of beta-hydroxy-beta-methylglutaryl coenzyme A condensing enzyme and reductase activities in M. hominis explains its growth requirement for sterol. The enzymatic block in M. gallisepticum must occur after mevalonic acid in the biosynthetic pathway to terpenoids.
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PMID:COMPARATIVE BIOSYNTHESIS OF MEVALONIC ACID BY MYCOPLASMA. 1425 55

Ramakrishnan, T. (Yale University, New Haven, Conn.), and Edward A. Adelberg. Regulatory mechanisms in the biosynthesis of isoleucine and valine. II. Identification of two operator genes. J. Bacteriol. 89:654-660. 1965.-A tightly clustered set of five structural genes governs the synthesis of the five enzymes of isoleucine and valine biosynthesis in Escherichia coli. Three of the genes governing transaminase B, dehydrase, and threonine deaminase, are controlled by a single operator locus, designated oprA. The structural gene governing the condensing enzyme is controlled by a second operator locus, designated oprB. Both oprA and oprB have been shown to regulate structural genes which are cis, but not trans, to their own operator. No mutations have yet been found which affect the level of reductoisomerase, but the existence of a third operator controlling the synthesis of this enzyme can be inferred. Enzyme derepression resulting from mutations in oprA confers resistance to high levels of valine. Derepression of the condensing enzyme resulting from mutations in oprB confers resistance to low levels of valine, and to alpha-aminobutyric acid. The significance of these findings with respect to the valine sensitivity of E. coli strain K-12 is discussed.
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PMID:REGULATORY MECHANISMS IN THE BIOSYNTHESIS OF ISOLEUCINE AND VALINE. II. IDENTIFICATION OF TWO OPERATOR GENES. 1427 40

Ramakrishnan, T. (Yale University, New Haven, Conn.), and Edward A. Adelberg. Regulatory mechanisms in the biosynthesis of isoleucine and valine. III. Map order of the structural genes and operator genes. J. Bacteriol. 89:661-664. 1965.-A new method has been employed to determine the map order of the structural genes and operator genes governing the enzymes of the isoleucine-valine biosynthetic pathway. This method relies on the observation that phage transduction of markers carried on an F-genote leads to the establishment in the recipient of F-genotes of various lengths. Using this method, we have established that the order of loci is the following: F/ilvE ilvD ilvA oprA/ilvC/ilvB oprB. The operator locus, oprA, regulates the activity of structural genes ilvE (transaminase B), ilvD (dehydrase), and ilvA (threonine deaminase). The operator locus, oprB, regulates the activity of ilvB (condensing enzyme). An operator for ilvC (reductoisomerase) can be inferred to exist, but has not yet been detected genetically. The loci ilvB and oprB have been shown to be at the extreme right end of the sequence, but their positions relative to each other remain to be established.
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PMID:REGULATORY MECHANISMS IN THE BIOSYNTHESIS OF ISOLEUCINE AND VALINE. 3. MAP ORDER OF THE STRUCTURAL GENES AND OPERATOR GENES. 1427 41

Reeves, Henry C. (Albert Einstein Medical Center, Philadelphia, Pa.) and Samuel J. Ajl. Function of malate synthetase and isocitritase in the growth of bacteria on two-carbon compounds. J. Bacteriol. 83:597-601. 1962.-Escherichia coli, grown in a glucose-citrate medium under anaerobic conditions, is devoid of the enzymes malate synthetase and isocitritase. It has been demonstrated that the adaptation of such cells to aerobic growth in a medium containing acetate as the sole carbon source involves at least two separate events. The first appears to be an adaptation which permits the oxidative dissimilation of acetate and involves primarily the synthesis of condensing enzyme. The second, which also precedes all division, is the synthesis of isocitritase and malate synthetase. Finally, a definite correlation has been found to exist between the synthesis of isocitritase and malate synthetase and the lag period prior to cell proliferation.
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PMID:Function of malate synthetase and isocitritase in the growth of bacteria on two-carbon compounds. 1449 Oct 17

Expression of a cDNA encoding the castor bean ( Ricinus communis L.) oleate Delta12-hydroxylase in the developing seeds of Arabidopsis thaliana (L.) Heynh. results in the synthesis of four novel hydroxy fatty acids. These have been previously identified as ricinoleic acid (12-hydroxy-octadec- cis-9-enoic acid: 18:1-OH), densipolic acid (12-hydroxy-octadec- cis-9,15-enoic acid: 18:2-OH), lesquerolic acid (14-hydroxy-eicos- cis-11-enoic acid: 20:1-OH) and auricolic acid (14-hydroxy-eicos- cis-11,17-enoic acid: 20:2-OH). Using mutant lines of Arabidopsis that lack the activity of the FAE1 condensing enzyme or FAD3 ER Delta-15-desaturase, we have shown that these enzymes are required for the synthesis of C20 hydroxy fatty acids and polyunsaturated hydroxy fatty acids, respectively. Analysis of the seed fatty acid composition of transformed plants demonstrated a dramatic increase in oleic acid (18:1) levels and a decrease in linoleic acid (18:2) content correlating to the levels of hydroxy fatty acid present in the seed. Plants in which FAD2 (ER Delta12-desaturase) activity was absent showed a decrease in 18:1 content and a slight increase in 18:2 levels corresponding to hydroxy fatty acid content. Expression of the castor hydroxylase protein in yeast indicates that this enzyme has a low level of fatty acid Delta12-desaturase activity. Lipase catalysed 1,3-specific lipolysis of triacylglycerol from transformed plants demonstrated that ricinoleic acid is not excluded from the sn-2 position of triacylglycerol, but is the only hydroxy fatty acid present at this position.
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PMID:Heterologous expression of a fatty acid hydroxylase gene in developing seeds of Arabidopsis thaliana. 1452 May 76

Analogues of the antibiotic thiolactomycin, with biphenyl-based 5-substituents, were found to have excellent in vitro inhibitory activity against the recombinant Mycobacterium tuberculosis beta-ketoacyl-ACP synthase mtFabH condensing enzyme. In particular, 5-(4'-benzyloxy-biphen-4-ylmethyl)-4-hydroxy-3,5-dimethyl-5H-thiophen-2-one exhibited approximately a 4-fold increased potency against this key condensing enzyme involved in M. tuberculosis mycolic acid biosynthesis, compared to thiolactomycin.
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PMID:Biphenyl-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme. 1455 58

Chloroacetamide herbicides inhibit very-long-chain fatty acid elongase, and it has been suggested that covalent binding to the active site cysteine of the condensing enzyme is responsible [Pest Manage Sci 56 (2000), 497], but direct evidence was not available. The proposal implied that other condensing enzymes might also be targets, and therefore we have investigated four purified recombinant type III plant polyketide synthases. Chalcone synthase (CHS) revealed a high sensitivity to the chloroacetamide metazachlor, with 50% inhibition after a 10 min pre-incubation with 1-2 molecules per enzyme subunit, and the inactivation was irreversible. Stilbene synthase (STS) inactivation required 20-fold higher amounts, and 4-coumaroyltriacetic acid synthase and pyrone synthase revealed no response at the highest metazachlor concentrations tested. A similar spectrum of differential responses was detected with other herbicides that also inhibit fatty acid elongase (metolachlor and cafenstrole). The data indicate that type III polyketide synthases are potential targets of these herbicides, but each combination has to be investigated individually. The interaction of metazachlor with CHS was investigated by mass spectrometric peptide mapping, after incubation of the enzymes with the herbicides followed by tryptic digestion. A characteristic mass shift and MS/MS sequencing of the respective peptide showed that metazachlor was covalently bound to the cysteine of the active site, and the same was found with STS. This is the first direct evidence that the active site cysteine in condensing enzymes is the primary common target of these herbicides.
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PMID:Covalent binding of chloroacetamide herbicides to the active site cysteine of plant type III polyketide synthases. 1456 70

Substrate specificity of condensing enzymes is a predominant factor determining the nature of fatty acyl chains synthesized by type II fatty acid synthase (FAS) enzyme complexes composed of discrete enzymes. The gene (mtKAS) encoding the condensing enzyme, beta-ketoacyl-[acyl carrier protein] (ACP) synthase (KAS), constituent of the mitochondrial FAS was cloned from Arabidopsis thaliana, and its product was purified and characterized. The mtKAS cDNA complemented the KAS II defect in the E. coli CY244 strain mutated in both fabB and fabF encoding KAS I and KAS II, respectively, demonstrating its ability to catalyze the condensation reaction in fatty acid synthesis. In vitro assays using extracts of CY244 containing all E. coli FAS components, except that KAS I and II were replaced by mtKAS, gave C(4)-C(18) fatty acids exhibiting a bimodal distribution with peaks at C(8) and C(14)-C(16). Previously observed bimodal distributions obtained using mitochondrial extracts appear attributable to the mtKAS enzyme in the extracts. Although the mtKAS sequence is most similar to that of bacterial KAS IIs, sensitivity of mtKAS to the antibiotic cerulenin resembles that of E. coli KAS I. In the first or priming condensation reaction of de novo fatty acid synthesis, purified His-tagged mtKAS efficiently utilized malonyl-ACP, but not acetyl-CoA as primer substrate. Intracellular targeting using green fluorescent protein, Western blot, and deletion analyses identified an N-terminal signal conveying mtKAS into mitochondria. Thus, mtKAS with its broad chain length specificity accomplishes all condensation steps in mitochondrial fatty acid synthesis, whereas in plastids three KAS enzymes are required.
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PMID:Identification and molecular characterization of the beta-ketoacyl-[acyl carrier protein] synthase component of the Arabidopsis mitochondrial fatty acid synthase. 1466 Jun 74

Analogues of the natural antibiotic thiolactomycin, with acetylene-based side chains, have the highest recorded in vitro inhibitory activity against the recombinant Mycobacterium tuberculosis beta-ketoacyl-ACP synthase mtFabH condensing enzyme. In particular, 5-[3-(4-acetyl-phenyl)-prop-2-ynyl]-4-hydroxy-3,5-dimethyl-5H-thiophen-2-one exhibited more than an 18-fold increased potency, compared to thiolactomycin, against this key condensing enzyme, involved in M. tuberculosis mycolic acid biosynthesis. Analogues of the antibiotic thiolactomycin, with acetylene-based side chains, have the highest recorded activity against cloned mtFabH condensing enzyme.
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PMID:Acetylene-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme. 1469 62


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