Results 41 to 50 of about 11,248,301 (236)
NADP-Malate Dehydrogenase of Sweet Sorghum Improves Salt Tolerance of Arabidopsis thaliana
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
Properties of the apo-form of the NADP(H)-binding domain III of proton-pumping Escherichia coli transhydrogenase: implications for the reaction mechanism of the intact enzyme [PDF]
Proton-translocating nicotinamide nucleotide transhydrogenases contain an NAD(H)-binding domain (dI), an NADP(H)-binding domain (dIII) and a membrane domain (dII) with the proton channel. Separately expressed and isolated dIII contains tightly bound NADP(
Jenny Karlsson +11 more
core +1 more source
Self‐Assembled Hybrid Cell‐Enzyme Materials for Gas‐Powered Biocatalysis
Integrating living cells with programmable enzyme networks enables hybrid materials that convert gaseous feedstocks into chemical reducing power. These gas‐powered catalytic beads operate as modular, recyclable platforms for adaptive biocatalysis and sustainable synthesis.
Marius Stoeckle +2 more
wiley +1 more source
Glucose-6-phosphate dehydrogenase (Zwf) is an important enzyme in glucose metabolism via the Entner-Doudoroff pathway and the first enzyme in the oxidative pentose-phosphate pathway. It generates NAD(P)H during the conversion of glucose-6-phosphate (G6P)
Bhavik A. Shah +2 more
doaj +1 more source
Programmable Carrier‐Free All‐Enzyme Beads for Modular Continuous‐Flow Biocatalysis
Genetically encoded enzyme building blocks self‐assemble into monodisperse, carrier‐free protein beads via a droplet‐based formulation strategy. These programmable catalytic particles enable modular continuous‐flow biocatalysis, from single‐enzyme reactions to multi‐enzyme cascades and bead–bead coupled reactor systems.
Jennifer Kühne +12 more
wiley +1 more source
A soluble monoterpene primary alcohol:NADP+ oxidoreductase has been purified to apparent homogeneity from leaves of the catmint, Nepeta racemosa. The purified enzyme consisted of two polypeptides, with molecular masses of 42,000 and 40,000 Da, and ...
Pickett, J. A. +13 more
core +1 more source
Structure-guided engineering of the coenzyme specificity of Pseudomonas fluorescens mannitol 2-dehydrogenase to enable efficient utilization of NAD(H) and NADP(H) [PDF]
The structure of Pseudomonas fluorescens mannitol 2-dehydrogenase with bound NAD+ leads to the suggestion that the carboxylate group of Asp69 forms a bifurcated hydrogen bond with the 2′ and 3′ hydroxyl groups of the adenosine of NAD+ and contributes to ...
Mario Klimacek +5 more
core +1 more source
A multi‐omics framework combining multitissue genome‐wide association studies, metabolomics, transcriptomics, proteomics, and functional validation uncovers the genetic basis of specialized metabolism in quinoa. The study identifies hundreds of metabolite‐associated loci, prioritizes candidate genes for saponin, betalain, and flavonoid biosynthesis ...
Julia von Steimker +11 more
wiley +1 more source
Structural Basis for Broad Substrate Selectivity of Alcohol Dehydrogenase YjgB from Escherichia coli
In metabolic engineering and synthetic biology fields, there have been efforts to produce variable bioalcohol fuels, such as isobutanol and 2-phenylethanol, in order to meet industrial demands. YjgB is an aldehyde dehydrogenase from Escherichia coli that
Giang Thu Nguyen +3 more
doaj +1 more source
The NADP-binding site of Plasmodium falciparum ferredoxin-NADP+ reductase contains two basic residues, His286 and Lys249, conserved within the Plasmodium genus, but not in other plant-type homologues.
M. Bolognesi +7 more
core +1 more source

