Results 21 to 30 of about 150,694 (118)

NADP-Malate Dehydrogenase of Sweet Sorghum Improves Salt Tolerance of Arabidopsis thaliana

open access: yes, 2018
Sweet sorghum is a C4 crop that shows high salt tolerance and high yield. NADP-malate dehydrogenase (NADP-ME) is a crucial enzyme of the C4 pathway. The regulatory mechanism of NADP-ME remains unclear.
Hongxiang Zheng (795530)   +5 more
core   +1 more source

Hexose-6-phosphate dehydrogenase modulates the effect of inhibitors and alternative substrates of 11[beta]-hydroxysteroid dehydrogenase 1 [PDF]

open access: yes, 2008
Intracellular glucocorticoid reactivation is catalyzed by 11[beta]-hydroxysteroid dehydrogenase 1 (11[beta]-HSD1), which functions predominantly as a reductase in cells expressing hexose-6-phosphate dehydrogenase (H6PDH).
Alex Odermatt   +9 more
core  

The regulation of NADP-linked isocitrate dehydrogenase in Aspergillus nidulans

open access: yes, 1982
The regulation of NADP-linked isocitrate dehydrogenase (NADP-IDH) has been studied in wild-type and mutant strains of Aspergillus nidulans. In the wild-type strain studied, the levels of NADP-IDH vary in a similar way to those of acetamidase, acetyl-CoA ...
Hynes, M.J., Kelly, J.M.
core   +1 more source

CHARACTERIZATION OF THE MECHANISM OF 6-PHOSPHOGLUCONATE DEHYDROGENASE FROM TRYPANOSOMA BRUCEI AND ITS INTERACTION WITH INHIBITORS BY ISOTHERMAL TITRATION CALORIMETRY [PDF]

open access: yes, 2009
6-Phosphogluconate dehydrogenase (6PGDH) converts 6PG to ribulose 5-phosphate and concomitantly provides NADPH, inside the pentose phosphate pathway. Its presence has been shown essential for growth of bloodstream form Trypanosoma brucei, a parasite ...
Montin, Katy
core  

Escherichia coli Dihydropyrimidine Dehydrogenase Is a Novel NAD-Dependent Heterotetramer Essential for the Production of 5,6-Dihydrouracil

open access: yes, 2011
The reductive pyrimidine catabolic pathway is absent in Escherichia coli . However, the bacterium contains an enzyme homologous to mammalian dihydropyrimidine dehydrogenase. Here, we show that E.
Tatsuo Kurihara   +3 more
core   +1 more source

NADP-dependent 15-hydroxyprostaglandin dehydrogenase is homologous to NAD-dependent 15-hydroxyprostaglandin dehydrogenase and other short-chain alcohol dehydrogenases.

open access: yes, 1992
Human tissues contain two enzymes that catalyze the oxidation of the 15-hydroxy group of prostaglandins: NAD-dependent 15-hydroxyprostaglandin dehydrogenase which is fairly specific for prostaglandins and NADP-dependent 15-hydroxyprostaglandin ...
Wermuth B
core   +1 more source

Function of coenzyme F420-dependent NADP reductase in methanogenic archaea containing an NADP-dependent alcohol dehydrogenase

open access: yes, 1997
Methanogenic archaea growing on ethanol or isopropanol as the electron donor for CO2 reduction to CH4 contain either an NADP-dependent or a coenzyme F420-dependent alcohol dehydrogenase.
Thauer, R. ; https://orcid.org/   +1 more
core   +1 more source

A Semi-throughput Procedure for Assaying Plant NADP-malate Dehydrogenase Activity Using a Plate Reader

open access: yes, 2023
International audienceChloroplast NADP-dependent malate dehydrogenase (NADP-MDH) is a redox regulated enzyme playing an important role in plant redox homeostasis. Leaf NADP-MDH activation level is considered a proxy for the chloroplast redox status. NADP-
Kevin Baudry   +3 more
core   +1 more source

The Hydride Transfer Process in NADP-dependent Methylene-tetrahydromethanopterin Dehydrogenase

open access: yes, 2020
NADP-dependent methylene-tetrahydromethanopterin (methylene-H4MPT) dehydrogenase (MtdA) catalyzes the reversible dehydrogenation of methylene-H4MPT to form methenyl-H4MPT+ by using NADP+ as a hydride acceptor.
Huang, G.   +7 more
core   +1 more source

Dual-Targeting of NADP+-Isocitrate Dehydrogenase [PDF]

open access: yes, 2009
Many mitochondrial and chloroplast proteins are encoded in the nucleus and subsequently imported into the organelles via active protein transport systems. While usually highly specific, some proteins are dual-targeted to both organelles.
McKinnon, John David
core  

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