Results 1 to 10 of about 321,356 (325)

Malate synthase contributes to the survival of Salmonella Typhimurium against nutrient and oxidative stress conditions [PDF]

open access: yesScientific Reports, 2022
To survive and replicate in the host, S. Typhimurium have evolved several metabolic pathways. The glyoxylate shunt is one such pathway that can utilize acetate for the synthesis of glucose and other biomolecules. This pathway is a bypass of the TCA cycle
Ratanti Sarkhel   +5 more
doaj   +3 more sources

Theranostic Application of a Novel G-Quadruplex-Forming DNA Aptamer Targeting Malate Synthase of Mycobacterium tuberculosis [PDF]

open access: yesMolecular Therapy: Nucleic Acids, 2019
The successful management of tuberculosis (TB) requires efficient diagnosis and treatment. Further, the increasing prevalence of drug-resistant TB highlights the urgent need to develop novel inhibitors against both drug-susceptible and drug-resistant ...
Abhijeet Dhiman   +13 more
doaj   +3 more sources

Intermolecular interactions of the malate synthase of Paracoccidioides spp. [PDF]

open access: yesBMC Microbiol, 2013
Abstract Background The fungus Paracoccidioides spp is the agent of paracoccidioidomycosis (PCM), a pulmonary mycosis acquired by the inhalation of fungal propagules. Paracoccidioides malate synthase (PbMLS) is important in the infectious process of Paracoccidioides spp because the transcript is up-regulated during ...
de Oliveira KM   +8 more
europepmc   +8 more sources

CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activity. [PDF]

open access: yesHum Mol Genet, 2014
CLYBL is a human mitochondrial enzyme of unknown function that is found in multiple eukaryotic taxa and conserved to bacteria. The protein is expressed in the mitochondria of all mammalian organs, with highest expression in brown fat and kidney. Approximately 5% of all humans harbor a premature stop polymorphism in CLYBL that has been associated with ...
Strittmatter L   +5 more
europepmc   +6 more sources

Evidence That Glyoxysomal Malate Synthase Is Segregated by the Endoplasmic Reticulum [PDF]

open access: greenPlant Physiology, 1978
At the onset of castor bean (Ricinus communis) germination, 76% of the cellular malate synthase activity of the endosperm tissue was located in the microsomal fraction, with the remainder in the glyoxysomal fraction. During later developmental stages, when rapid malate synthase synthesis was occurring, an increasing proportion of the enzyme was ...
Janet M. Lord, Linda Bowden
semanticscholar   +6 more sources

Biochemical characterization of malate synthase G of P. aeruginosa [PDF]

open access: hybridBMC Biochemistry, 2009
Abstract Background Malate synthase catalyzes the second step of the glyoxylate bypass, the condensation of acetyl coenzyme A and glyoxylate to form malate and coenzyme A (CoA). In several microorganisms, the glyoxylate bypass is of general importance to microbial pathogenesis.
Bart Roucourt   +5 more
semanticscholar   +6 more sources

Expression regulation of MALATE SYNTHASE involved in glyoxylate cycle during protocorm development in Phalaenopsis aphrodite (Orchidaceae). [PDF]

open access: yesSci Rep, 2020
Orchid (Orchidaceae) is one of the largest families in angiosperms and presents exceptional diversity in lifestyle. Their unique reproductive characteristics of orchid are attracted by scientist for centuries.
Wu WL   +9 more
europepmc   +2 more sources

The product complex of M. tuberculosis malate synthase revisited [PDF]

open access: greenProtein Science, 2006
AbstractEnzymes of the glyoxylate shunt have been implicated as virulence factors in several pathogenic organisms, notably Mycobacterium tuberculosis and Candida albicans. Malate synthase has thus emerged as a promising target for design of anti‐microbial agents. For this effort, it is essential to have reliable models for enzyme:substrate complexes. A
David M. Anstrom, S. James Remington
semanticscholar   +5 more sources

Spontaneous refolding of the large multidomain protein malate synthase G proceeds through misfolding traps. [PDF]

open access: yesJ Biol Chem, 2018
Most protein folding studies until now focus on single domain or truncated proteins. Although great insights in the folding of such systems has been accumulated, very little is known regarding the proteins containing multiple domains.
Kumar V, Chaudhuri TK.
europepmc   +2 more sources

Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange. [PDF]

open access: yesJ Biol Chem, 2016
Fragment screening and high throughput screening are complementary approaches that combine with structural biology to explore the binding capabilities of an active site.
Huang HL   +4 more
europepmc   +2 more sources

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