CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activity. [PDF]
Hum 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
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The product complex of M. tuberculosis malate synthase revisited [PDF]
Protein 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
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Medical and Health Science Journal, 2023 Introduction: Dermatophytes are pathogenic fungi that cause cutaneousinfection of human and animal and grow exclusively on the stratumcorneum, nail and hair. Methods: The present study was conducted on 160 samples from clinicallydiagnosed onycomycosis
Shyama Datt +3 more
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Exploring Metabolic Disruption and Redox Modulation by Senna Leaf Extracts Induces Mortality in the Zoonotic Parasite Hymenolepis diminuta [PDF]
Journal of Parasitology ResearchSenna leaf extracts exhibit strong anthelmintic effects against the zoonotic cestode Hymenolepis diminuta, inducing profound morphological and biochemical alteration.
Saptarshi Roy, Larisha M. Lyndem
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Menstrual cycle influence on skeletal muscle mitochondrial respiration in humans [PDF]
Physiological ReportsThe menstrual cycle influences function in various tissues in the body. We sought to determine if menstrual cycle phase could influence mitochondrial function in skeletal muscle in females.
W. Bradley Nelson +10 more
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Cottonseed Malate Synthase [PDF]
Plant Physiology, 1987 Malate synthase (EC 4.1.3.2), an enzyme unique to the glyoxylate cycle, was purified to homogeneity from cotyledons of 72-hours, darkgrown cotton (Gossypium hirsutum L.) seedlings. Homogeneity of the enzyme was assessed by silver staining SDS-PAGE gels.
Richard N. Trelease +3 more
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Biochemical characterization of malate synthase G of P. aeruginosa [PDF]
BMC Biochemistry, 2009 BackgroundMalate 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
B. Roucourt +5 more
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Modeling, molecular docking, probing catalytic binding mode of acetyl-CoA malate synthase G in Brucella melitensis 16M. [PDF]
Biochem Biophys Rep, 2016 Adi PJ, Yellapu NK, Matcha B.
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Alkaloids as Inhibitors of Malate Synthase from Paracoccidioides spp.: Receptor-Ligand Interaction-Based Virtual Screening and Molecular Docking Studies, Antifungal Activity, and the Adhesion Process [PDF]
Antimicrobial Agents and Chemotherapy, 2015 Fausto Guimarães Costa +10 more
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Noninvolvement of Acyl Carrier Protein with Citrate Synthase and Malate Synthase [PDF]
Journal of Bacteriology, 1968 Acyl carrier protein (ACP coli) was isolated from commercially grown Escherichia coli B and was acetylated by chemical methods. Biological activity of the synthesized acetyl-ACP coli was checked in an in vitro fatty acid-synthesizing system isolated from E. coli B.
Stuart L. Marcus +2 more
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