scholarly journals Expression regulation of MALATE SYNTHASE involved in glyoxylate cycle during protocorm development in Phalaenopsis aphrodite (Orchidaceae)

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Wan-Lin Wu ◽  
Yu-Yun Hsiao ◽  
Hsiang-Chia Lu ◽  
Chieh-Kai Liang ◽  
Chih-Hsiung Fu ◽  
...  
Keyword(s):  
Glyoxylate Cycle ◽  
Expression Regulation ◽  
Malate Synthase ◽  
Phalaenopsis Aphrodite

Co-ordinate regulation of genes involved in storage lipid mobilization in Arabidopsis thaliana

2001 ◽  
Vol 29 (2) ◽  
pp. 283-286 ◽  
Author(s):  
E. L. Rylott ◽  
M. A. Hooks ◽  
I. A. Graham
Keyword(s):  
Arabidopsis Thaliana ◽  
Enzyme Activities ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Molecular Genetic ◽  
Regulation Of Gene Expression ◽  
Growth Period ◽  
Malate Synthase ◽  
The Glyoxylate Cycle

Molecular genetic approaches in the model plant Arabidopsis thaliana (ColO) are shedding new light on the role and control of the pathways associated with the mobilization of lipid reserves during oilseed germination and post-germinative growth. Numerous independent studies have reported on the expression of individual genes encoding enzymes from the three major pathways: β-oxidation, the glyoxylate cycle and gluconeogenesis. However, a single comprehensive study of representative genes and enzymes from the different pathways in a single plant species has not been done. Here we present results from Arabidopsis that demonstrate the co-ordinate regulation of gene expression and enzyme activities for the acyl-CoA oxidase- and 3-ketoacyl-CoA thiolasemediated steps of β-oxidation, the isocitrate lyase and malate synthase steps of the glyoxylate cycle and the phosphoenolpyruvate carboxykinase step of gluconeogenesis. The mRNA abundance and enzyme activities increase to a peak at stage 2, 48 h after the onset of seed germination, and decline thereafter either to undetectable levels (for malate synthase and isocitrate lyase) or low basal levels (for the genes of β-oxidation and gluconeogenesis). The co-ordinate induction of all these genes at the onset of germination raises the possibility that a global regulatory mechanism operates to induce the expression of genes associated with the mobilization of storage reserves during the heterotrophic growth period.

scholarly journals The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3S)-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3S)- Malyl-CoA Thioesterase

2010 ◽  
Vol 192 (5) ◽  
pp. 1249-1258 ◽  
Author(s):  
Tobias J. Erb ◽  
Lena Frerichs-Revermann ◽  
Georg Fuchs ◽  
Birgit E. Alber
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Coenzyme A ◽  
Glyoxylate Cycle ◽  
Condensation Reaction ◽  
Malate Synthase ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Claisen Condensation ◽  
Enzyme Functions ◽  
The Glyoxylate Cycle

ABSTRACT Assimilation of acetyl coenzyme A (acetyl-CoA) is an essential process in many bacteria that proceeds via the glyoxylate cycle or the ethylmalonyl-CoA pathway. In both assimilation strategies, one of the final products is malate that is formed by the condensation of acetyl-CoA with glyoxylate. In the glyoxylate cycle this reaction is catalyzed by malate synthase, whereas in the ethylmalonyl-CoA pathway the reaction is separated into two proteins: malyl-CoA lyase, a well-known enzyme catalyzing the Claisen condensation of acetyl-CoA with glyoxylate and yielding malyl-CoA, and an unidentified malyl-CoA thioesterase that hydrolyzes malyl-CoA into malate and CoA. In this study the roles of Mcl1 and Mcl2, two malyl-CoA lyase homologs in Rhodobacter sphaeroides, were investigated by gene inactivation and biochemical studies. Mcl1 is a true (3S)-malyl-CoA lyase operating in the ethylmalonyl-CoA pathway. Notably, Mcl1 is a promiscuous enzyme and catalyzes not only the condensation of acetyl-CoA and glyoxylate but also the cleavage of β-methylmalyl-CoA into glyoxylate and propionyl-CoA during acetyl-CoA assimilation. In contrast, Mcl2 was shown to be the sought (3S)-malyl-CoA thioesterase in the ethylmalonyl-CoA pathway, which specifically hydrolyzes (3S)-malyl-CoA but does not use β-methylmalyl-CoA or catalyze a lyase or condensation reaction. The identification of Mcl2 as thioesterase extends the enzyme functions of malyl-CoA lyase homologs that have been known only as “Claisen condensation” enzymes so far. Mcl1 and Mcl2 are both related to malate synthase, an enzyme which catalyzes both a Claisen condensation and thioester hydrolysis reaction.

The fine structure and selected histochemistry of ungerminated basidiospores of Agrocybe acericola

1996 ◽  
Vol 74 (5) ◽  
pp. 780-787 ◽  
Author(s):  
Donald G. Ruch ◽  
Kiki Nurtjahja
Keyword(s):  
Fine Structure ◽  
Acid Phosphatase ◽  
Glyoxylate Cycle ◽  
Outer Wall ◽  
Spore Wall ◽  
Malate Synthase ◽  
Marker Enzyme ◽  
Wall Ultrastructure ◽  
Membrane Bound ◽  
The Glyoxylate Cycle

The basidiospore wall of Agrocybe acericola is composed of two distinct layers that are continuous around the spores. At the germ pore, the outer wall is very thin and the inner wall becomes thicker. The plasma membrane is appressed to the inner wall and lacks distinct invaginations. The protoplasm is densely packed with ribosomes. Spores contain very little lipid distributed at each end. Mitochondria are well defined and distributed throughout the cytoplasm. Spores are binucleate, with the two nuclei lying on a line nearly perpendicular to the long axis of the cell. Various sizes of single membrane-bound vacuoles are widely distributed in the cytoplasm. These vacuoles were shown to contain acid phosphatase, indicating lysosomal activity. Microbody-like organelles are observed, which are probably glyoxysomes, since assays of malate synthase, a marker enzyme of the glyoxylate cycle, are positive. Keywords: Agrocybe, spore wall ultrastructure, basidiospore ultrastructure, glyoxylate cycle, malate synthase, acid phosphatase.

The malate synthase of Paracoccidioides brasiliensis Pb01 is required in the glyoxylate cycle and in the allantoin degradation pathway

2009 ◽  
pp. 1-12
Author(s):  
Patricia Fernanda Zambuzzi-Carvalho ◽  
Aline Helena Da Silva Cruz ◽  
Ludier Kesser Santos-Silva ◽  
Alfredo Miranda Goes ◽  
Celia Maria De Almeida Soares ◽  
...  
Keyword(s):  
Paracoccidioides Brasiliensis ◽  
Glyoxylate Cycle ◽  
Degradation Pathway ◽  
Malate Synthase ◽  
The Glyoxylate Cycle

scholarly journals Identification of RamA, a Novel LuxR-Type Transcriptional Regulator of Genes Involved in Acetate Metabolism of Corynebacterium glutamicum

2006 ◽  
Vol 188 (7) ◽  
pp. 2554-2567 ◽  
Author(s):  
Annette Cramer ◽  
Robert Gerstmeir ◽  
Steffen Schaffer ◽  
Michael Bott ◽  
Bernhard J. Eikmanns
Keyword(s):  
Corynebacterium Glutamicum ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Transcriptional Regulator ◽  
Malate Synthase ◽  
Acetate Kinase ◽  
Acetate Metabolism ◽  
Promoter Regions ◽  
Cell Extracts ◽  
Peptide Mass

ABSTRACT In Corynebacterium glutamicum, the acetate-activating enzymes phosphotransacetylase and acetate kinase and the glyoxylate cycle enzymes isocitrate lyase and malate synthase are coordinately up-regulated in the presence of acetate in the growth medium. This regulation is due to transcriptional control of the respective pta-ack operon and the aceA and aceB genes, brought about at least partly by the action of the negative transcriptional regulator RamB. Using cell extracts of C. glutamicum and employing DNA affinity chromatography, mass spectrometry, and peptide mass fingerprinting, we identified a LuxR-type transcriptional regulator, designated RamA, which binds to the pta-ack and aceA/aceB promoter regions. Inactivation of the ramA gene in the genome of C. glutamicum resulted in mutant RG2. This mutant was unable to grow on acetate as the sole carbon and energy source and, in comparison to the wild type of C. glutamicum, showed very low specific activities of phosphotransacetylase, acetate kinase, isocitrate lyase, and malate synthase, irrespective of the presence of acetate in the medium. Comparative transcriptional cat fusion experiments revealed that this deregulation takes place at the level of transcription. By electrophoretic mobility shift analysis, purified His-tagged RamA protein was shown to bind specifically to the pta-ack and the aceA/aceB promoter regions, and deletion and mutation studies revealed in both regions two binding motifs each consisting of tandem A/C/TG4-6T/C or AC4-5A/G/T stretches separated by four or five arbitrary nucleotides. Our data indicate that RamA represents a novel LuxR-type transcriptional activator of genes involved in acetate metabolism of C. glutamicum.

scholarly journals Physiological Ecology of Stenoxybacter acetivorans, an Obligate Microaerophile in Termite Guts

2007 ◽  
Vol 73 (21) ◽  
pp. 6829-6841 ◽  
Author(s):  
John T. Wertz ◽  
John A. Breznak
Keyword(s):  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Glyoxylate Cycle ◽  
Reticulitermes Flavipes ◽  
Peripheral Region ◽  
Malate Synthase ◽  
Rrna Gene ◽  
Potential Contribution ◽  
Cell Extracts

ABSTRACT Stenoxybacter acetivorans is a newly described, obligately microaerophilic β-proteobacterium that is abundant in the acetate-rich hindgut of Reticulitermes. Here we tested the hypotheses that cells are located in the hypoxic, peripheral region of Reticulitermes flavipes hindguts and use acetate to fuel their O2-consuming respiratory activity in situ. Physical fractionation of R. flavipes guts, followed by limited-cycle PCR with S. acetivorans-specific 16S rRNA gene primers, indicated that cells of this organism were indeed located primarily among the microbiota colonizing the hindgut wall. Likewise, reverse transcriptase PCR of hindgut RNA revealed S. acetivorans-specific transcripts for acetate-activating enzymes that were also found in cell extracts (acetate kinase and phosphotransacetylase), as well as transcripts of ccoN, which encodes the O2-reducing subunit of high-affinity cbb 3-type cytochrome oxidases. However, S. acetivorans strains did not possess typical enzymes of the glyoxylate cycle (isocitrate lyase and malate synthase A), suggesting that they may use an alternate pathway to replenish tricarboxylic acid cycle intermediates or they obtain such compounds (or their precursors) in situ. Respirometric measurements indicated that much of the O2 consumption by R. flavipes worker larvae was attributable to their guts, and the potential contribution of S. acetivorans to O2 consumption by extracted guts was about 0.2%, a value similar to that obtained for other hindgut bacteria examined. Similar measurements obtained with guts of larvae prefed diets to disrupt major members of the hindgut microbiota implied that most of the O2 consumption observed with extracted guts was attributable to protozoans, a group of microbes long thought to be “strict anaerobes.”

STUDIES ON RUMEN COLIFORM ORGANISMS: II. UTILIZATION OF ACETATE BY ESCHERICHIA COLI 64 ISOLATED FROM THE RUMEN FLUID OF A COW FED ALFALFA HAY

1967 ◽  
Vol 47 (3) ◽  
pp. 199-209 ◽  
Author(s):  
C. R. Krishnamurti ◽  
L. W. McElroy
Keyword(s):  
Sodium Acetate ◽  
Isocitrate Lyase ◽  
Protein Hydrolysate ◽  
Rumen Fluid ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
E Coli ◽  
Spectrophotometric Methods ◽  
Acetate Medium ◽  
The Glyoxylate Cycle

When cells of E. coli 64 were harvested in their exponential phase of growth in an acetate medium and incubated aerobically with sodium acetate-2-C14, about 33% of the label appeared in CO2 after 1 hr. Of the radioactivity in the cells, 72% was recovered in the protein hydrolysate, 8% in the nucleic acid, 6% in the lipid and 14% in the ethanol-soluble fractions. The radioactivity in the protein hydrolysate of cells incubated with sodium acetate-2-C14 was approximately 20 times that in the hydrolysate of cells incubated with C14O2 as the carbon source. By spectrophotometric methods, it was demonstrated that cell-free extracts of cells grown on acetate contained acetate kinase and phosphate acetyltransferase, plus, as demonstrated by spectrophotometric and isotopic methods, isocitrate lyase and malate synthase which are characteristic of the glyoxylate cycle. The enzymes of the glyoxylate cycle could not be demonstrated in cell-free extracts of E. coli 64 grown on glucose under either aerobic or anaerobic conditions. Possible functions that E. coli 64 may have in the maintenance of anaerobiosis in the rumen and utilization of acetate through the glyoxylate pathway are discussed.

scholarly journals Correlation of dicarboxylic acid cycle with tricarboxylic acid cycle in highly productive pigs

2020 ◽  
Vol 58 (2) ◽  
pp. 215-225
Author(s):  
K. S. Ostrenko ◽  
V. P. Galochkina ◽  
V. О. Lemiasheuski ◽  
A. V. Agafonova ◽  
A. N. Ovcharova ◽  
...  
Keyword(s):  
Dicarboxylic Acid ◽  
Lower Layer ◽  
Tricarboxylic Acid Cycle ◽  
Glyoxylate Cycle ◽  
Krebs Cycle ◽  
Tricarboxylic Acid ◽  
Malate Synthase ◽  
The Body ◽  
Mitochondrial Enzymes ◽  
Acid Cycle

The paper is the fundamental beginning of research series aimed at understanding the processes associated with high performance in higher animals. The research aim is to study correlation of dicarboxylic acid cycle with tricarboxylic acid cycle with establishment of activity and dislocation of enzymes, confirming the hypothesis of availability and active metabolic participation of peroxisome in highly productive animals. Research was conducted on the basis of the VNIIFBiP animal vivarium in 2019 with a group of piglets of the Irish Landrace breed (n = 10). After slaughter at the age of 210 days, the nuclear (with large tissue particles), mitochondrial and postmitochondrial fractions of the liver were studied with assessment of succinate dehydrogenase and activity of other dehydrogenes of the Krebs cycle. It was found that peroxisomes act as universal agents of communication and cooperation, and microtelets are able to generate various chemical signals that carry information, to control and arrange a number of mechanisms in the metabolic processes in the body. Despite the fact that the Krebs cycle dehydrogenases are considered mitochondrial enzymes, the experiment showed an increase in activity of priruvate dehydrogenase (P > 0.1), isocitrate dehydrogenase (0.1 > P > 0.05) and malate dehydrogenase (0.1 > P > 0.05), which, when comparing the mitochondrial and postmitochondrial fractions, indicates a higher activity of peroxisomal fractions. The peroxisome localization place is the postmitochondrial fraction, and the lower layer contains larger peroxisomes to a greater extent, while the upper layer contains smaller ones. It was found that indicator enzymes of glyoxylate cycle isocitratliase and malate synthase exhibit catalytic activity in the peroxisomal fraction of liver of highly productive pigs. The obtained data on functioning of key glyoxylate cycle enzymes and their intracellular compartmentalization in highly productive pigs allow learning more about the specifics of metabolism and its regulation processes. Application of this knowledge in practice opens up prospects for rationalizing the production of livestock products of increased quantity, improved quality with less feed, labor and financial resources spent.

scholarly journals The malate synthase ofParacoccidioides brasiliensis Pb01 is required in the glyoxylate cycle and in the allantoin degradation pathway

2009 ◽  
Vol 47 (7) ◽  
pp. 734-744 ◽  
Author(s):  
Patrícia Fernanda Zambuzzi-Carvalho ◽  
Aline Helena Da Silva Cruz ◽  
Ludier Kesser Santos-Silva ◽  
Alfredo Miranda Goes ◽  
Célia Maria De Almeida Soares ◽  
...  
Keyword(s):  
Glyoxylate Cycle ◽  
Degradation Pathway ◽  
Malate Synthase ◽  
The Glyoxylate Cycle

Re-Activation of the Expression of Glyoxysomal Genes in Green Plant Tissue

1990 ◽  
Vol 45 (1-2) ◽  
pp. 107-111 ◽  
Author(s):  
Ralf Birkhan ◽  
Helmut Kindl
Keyword(s):  
Gene Expression ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Green Plant ◽  
Malate Synthase ◽  
Dna Library ◽  
Glycollate Oxidase ◽  
Differential Gene ◽  
Cucumber Cotyledons ◽  
Leaf Peroxisome

Abstract Biochemie, Fachbereich Chemie, Universität Marburg, Hans-Meerwein-Straße, D-3550 Marburg, Bundesrepublik Deutschland Z. Naturforsch. 45c, Isocitrate Lyase c DNA, Malate Synthase c DNA, Glyoxysome, Leaf Peroxisome, Transition of Organelles Glyoxysomes are being replaced by leaf-type peroxisom es during the greening of dark-grown cucumber cotyledons. Light functions in this process as negative modulator of the gene expression of glyoxylate cycle enzymes but as positive regulator for the activation of glycollate oxidase formation. The differential gene expression was investigated at the level of m RNA amounts using c DNA probes hybridizing with malate synthase m RNA, isocitrate lyase m RNA, and glycollate oxidase m RNA. Hybrid ization probes were obtained from a c DNA library complementary to the germinationspecific m RNA s of cucumber cotyledons. The process of replacem ent of glyoxysomal proteins by leaf peroxisom al proteins was reversed to a certain extend when greened cotyledons were brought back in the dark. Hybridization on Northern b lots provided evidences that in greened cotyledons the amount of malate synthase m RNA and isocitratelyase m RNA starts to increase up on dark treatment.

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