Production of a novel opine dehydrogenase
Апстракт
Opine dehydrogenases are a family of NAD(P)H dependent oxidoreductases, which
catalyze the reductive condensation of an α amino group from an amino acid with an αketo acid during anaerobic glycolysis by regenerating NAD. They are widespread in
cephalopods and mollusks. Opines are associated with crown gall tumor pathogenesis
caused by A. tumefaciens providing nutrients to the pathogen, and novel opine compounds
acting as metallophores have been identified. Besides, opine-type secondary amine
dicarboxylic acids are chiral intermediates of angiotensin-converting enzyme inhibitors. A
novel enzyme originating from an extremophile bacterium, with assumed opine
dehydrogenase function was successfully expressed in Escherichia coli STAR cells and
purified by affinity chromatography. Molecular mass determined by SDS-PAGE was
approximately 40 kDa. The activity was measured by using pyruvate and alanine as
substrates, by which proved that it has opine dehydrogenase activity.
Кључне речи:
Opine dehydrogenasesИзвор:
Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry", 2022, 79-Издавач:
- Faculty of Chemistry, Serbian Biochemical Society
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200053 (Универзитет у Београду, Институт за мултидисциплинарна истраживања) (RS-MESTD-inst-2020-200053)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200026 (Универзитет у Београду, Институт за хемију, технологију и металургију - ИХТМ) (RS-MESTD-inst-2020-200026)
Институција/група
Institut za multidisciplinarna istraživanjaTY - CONF AU - Kalicanin, Nevena AU - Balaz, Ana Marija AU - Prodanović, Olivera AU - Prodanović, Radivoje PY - 2022 UR - http://rimsi.imsi.bg.ac.rs/handle/123456789/3048 AB - Opine dehydrogenases are a family of NAD(P)H dependent oxidoreductases, which catalyze the reductive condensation of an α amino group from an amino acid with an αketo acid during anaerobic glycolysis by regenerating NAD. They are widespread in cephalopods and mollusks. Opines are associated with crown gall tumor pathogenesis caused by A. tumefaciens providing nutrients to the pathogen, and novel opine compounds acting as metallophores have been identified. Besides, opine-type secondary amine dicarboxylic acids are chiral intermediates of angiotensin-converting enzyme inhibitors. A novel enzyme originating from an extremophile bacterium, with assumed opine dehydrogenase function was successfully expressed in Escherichia coli STAR cells and purified by affinity chromatography. Molecular mass determined by SDS-PAGE was approximately 40 kDa. The activity was measured by using pyruvate and alanine as substrates, by which proved that it has opine dehydrogenase activity. PB - Faculty of Chemistry, Serbian Biochemical Society C3 - Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry" T1 - Production of a novel opine dehydrogenase SP - 79 UR - https://hdl.handle.net/21.15107/rcub_rimsi_3048 ER -
@conference{ author = "Kalicanin, Nevena and Balaz, Ana Marija and Prodanović, Olivera and Prodanović, Radivoje", year = "2022", abstract = "Opine dehydrogenases are a family of NAD(P)H dependent oxidoreductases, which catalyze the reductive condensation of an α amino group from an amino acid with an αketo acid during anaerobic glycolysis by regenerating NAD. They are widespread in cephalopods and mollusks. Opines are associated with crown gall tumor pathogenesis caused by A. tumefaciens providing nutrients to the pathogen, and novel opine compounds acting as metallophores have been identified. Besides, opine-type secondary amine dicarboxylic acids are chiral intermediates of angiotensin-converting enzyme inhibitors. A novel enzyme originating from an extremophile bacterium, with assumed opine dehydrogenase function was successfully expressed in Escherichia coli STAR cells and purified by affinity chromatography. Molecular mass determined by SDS-PAGE was approximately 40 kDa. The activity was measured by using pyruvate and alanine as substrates, by which proved that it has opine dehydrogenase activity.", publisher = "Faculty of Chemistry, Serbian Biochemical Society", journal = "Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry"", title = "Production of a novel opine dehydrogenase", pages = "79", url = "https://hdl.handle.net/21.15107/rcub_rimsi_3048" }
Kalicanin, N., Balaz, A. M., Prodanović, O.,& Prodanović, R.. (2022). Production of a novel opine dehydrogenase. in Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry" Faculty of Chemistry, Serbian Biochemical Society., 79. https://hdl.handle.net/21.15107/rcub_rimsi_3048
Kalicanin N, Balaz AM, Prodanović O, Prodanović R. Production of a novel opine dehydrogenase. in Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry". 2022;:79. https://hdl.handle.net/21.15107/rcub_rimsi_3048 .
Kalicanin, Nevena, Balaz, Ana Marija, Prodanović, Olivera, Prodanović, Radivoje, "Production of a novel opine dehydrogenase" in Proceedings Eleventh Conference, Scientific meeting of an international character "Amazing Biochemistry" (2022):79, https://hdl.handle.net/21.15107/rcub_rimsi_3048 .