Počet záznamů: 1
The regulation and catalytic mechanism of the NADP-malic enzyme from tobacco leaves
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SYSNO ASEP 0337488 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The regulation and catalytic mechanism of the NADP-malic enzyme from tobacco leaves Překlad názvu Regulace a mechanismus katalýzy NADP dependentní malátdehydrogenasy (dekarboxylační) z listů tabáku Tvůrce(i) Doubnerová, V. (CZ)
Potůčková, L. (CZ)
Müller, Karel (UEB-Q) RID, ORCID
Ryšlavá, H. (CZ)Zdroj.dok. Journal of the Serbian Chemical Society - ISSN 0352-5139
Roč. 14, 8-9 (2009), s. 893-906Poč.str. 14 s. Jazyk dok. eng - angličtina Země vyd. CS - CS Klíč. slova NADP-malic enzyme ; macroergic compounds ; Nicotiana tabacum L. Vědní obor RIV ED - Fyziologie CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000270267200005 DOI 10.2298/JSC0909893D Anotace The non-photosynthetic NADP-malic enzyme EC 1.1.1.40 (NADP-ME), which catalyzes the oxidative decarboxylation of L-malate and NADP(+) to produce pyruvate and NADPH, respectively, and which could be involved in plant defense responses, was isolated from Nicotiana tabacum L. leaves. The mechanism of the enzyme reaction was studied by the initial rate method and was found to be an ordered sequential one. Regulation possibilities of purified cytosolic NADP-ME by cell metabolites were tested. Intermediates of the citric acid cycle (a-ketoglutarate, succinate, fumarate), metabolites of glycolysis (pyruvate, phosphoenolpyruvate, glucose-6-phosphate), compounds connected with lipogenesis (coenzyme A, acetyl-CoA, palmitoyl-CoA) and some amino acids (glutamate, glutamine, aspartate) did not significantly affect the NADP-ME activity from tobacco leaves. In contrast, macroergic compounds (GTP, ATP and ADP) were strong inhibitors of NADP-ME. Pracoviště Ústav experimentální botaniky Kontakt David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Rok sběru 2010
Počet záznamů: 1