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Search results for: aminotransferase
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Characterization of two aminotransferases from Candida albicans
PublicationAminoadipate aminotransferase (AmAA) is an enzyme of α-aminoadipate pathway (AAP) for l-lysine biosynthesis. AmAA may also participated in biosynthesis or degradation of aromatic amino acids and in d-tryptophan based pigment production. The AAP is unique for fungal microorganisms. Enzymes involved in this pathway have specific structures and properties. These features can be used as potential molecular markers. Enzymes catalyzing...
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Versatility of putative aromatic aminotransferases from Candida albicans.
PublicationAmino acids constitute the key sources of nitrogen for growth of Candida albicans. In order to survive inside the host in different and rapidly changing environments, this fungus must be able to adapt via its expression of genes for amino acid metabolism. We analysed the ARO8, ARO9, YER152C, and BNA3 genes with regards to their role in the nutritional flexibility of C. albicans. CaAro8p is undoubtedly the most versatile enzyme...
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Crystal structures of aminotransferases Aro8 and Aro9 from Candida albicans and structural insights into their properties
PublicationAminotransferases catalyze reversibly the transamination reaction by a ping-pong bi-bi mechanism with pyridoxal 5′-phosphate (PLP) as a cofactor. Various aminotransferases acting on a range of substrates have been reported. Aromatic transaminases are able to catalyze the transamination reaction with both aromatic and acidic substrates. Two aminotransferases from C. albicans, Aro8p and Aro9p, have been identified recently, exhibiting...
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Construction of glucosamine-6-phosphate synthase with an internal hexahistydyl fragment
PublicationL-Glutamine: D-fructose-6-phosphate aminotransferase (EC 2.6.1.16), known also as glucosamine-6-phosphate (GlcN-6-P) syntase, catalyzes the first committed step in the amino sugar biosynthetic pathway in prokaryotic and eukaryotic organisms. The enzyme carries out a complex reaction involving ammonia transfer and sugar phosphate isomerization. GlcN-6-P syntase is an important point of metabolic control of amino sugar biosynthesis...
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Importance of Bile Composition for Diagnosis of Biliary Obstructions
PublicationDetermination of the cause of a biliary obstruction is often inconclusive from serum analysis alone without further clinical tests. To this end, serum markers as well as the composition of bile of 74 patients with biliary obstructions were determined to improve the diagnoses. The samples were collected from the patients during an endoscopic retrograde cholangiopancreatography (ERCP). The concentration of eight bile salts, specifically...
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Enzymes of the lysine biosynthetic pathway as targets for antifungals ?
PublicationSystemic infections caused by human pathogenic fungi in immunocompromized patients continue to be one of the important clinical problems. Limited availability of safe and efficacious antifungal chemotherapeutics and emerging resistance to existing drugs stimulates search for novel molecular targets for antifungals. The α-aminoadipate pathway (AAP) of L-lysine biosynthesis is unique in fungi and thus has been so far considered...
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Glucosamine-6-phosphate synthase with an oligoHis insert
PublicationGlucosamine-6-phosphate (GlcN-6-P) synthase known also as L-Glutamine: D-fructose-6-phosphate aminotransferase (EC 2.6.1.16), catalyzes the first committed step in the amino sugar biosynthetic pathway in prokaryotic and eukaryotic organisms. The final product of this pathway is an activated precursor of numerous macromolecules containing amino sugars, including chitin and mannproteins in fungi, peptydoglican and lipopolysaccharides...
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Iwona Gabriel dr hab. inż.
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