Results 111 to 120 of about 268,882 (295)

The structure of mitochondrial NADH dehydrogenase

open access: yes, 1981
Antisera to Complex I (NADH-ubiquinone oxidoreductase, EC 1.6.99.3.) purified from bovine heart mitochondria, and to fractions from this enzyme have been used to study the structure of mitochondrial NADH dehydrogenase. Analysis by one and two dimensional
Smith, Stuart Kevin
core  

Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase

open access: yes, 2001
Background: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD+ to NADH.
Baker PJ   +26 more
core   +1 more source

Polyphosphate Copper Nanospheres Drive Mitochondrial Metabolic Reprogramming via Calcium Phase Separation for Self‐Sensitizing Cuproptosis

open access: yesAdvanced Science, EarlyView.
This study developed polyphosphate (polyP)‐based nanostructures that enable calcium‐mediated metabolic reprogramming via liquid–liquid phase separation (LLPS). Released polyP undergoes LLPS with Ca2+, suppressing glycolytic flux and enhancing mitochondrial metabolism effectively.
Jing Wang   +10 more
wiley   +1 more source

Macrophage GLUD1 is Essential for Redox Balance and Immune Homeostasis in Cardiac Injury

open access: yesAdvanced Science, EarlyView.
Excessive free radical production and dysregulated immune responses are key contributors to myocardial ischemia‐reperfusion (IR) injury. Macrophage GLUD1 activity safeguards against HIF‐1α accumulation and maladaptive responses to IR‐induced ROS production.
Tingting Jin   +16 more
wiley   +1 more source

Functional characterization of SlscADH1, a fruit-ripening associated short-chain alcohol dehydrogenase of tomato [PDF]

open access: yes, 2012
A tomato short-chain dehydrogenase-reductase (SlscADH1) is preferentially expressed in fruit with a maximum expression at the breaker stage while expression in roots, stems, leaves and flowers is very weak.
Moummou, Hanane   +8 more
core   +1 more source

PHGDH‐Mediated Serine Metabolism in Nucleus Pulposus Cells Is a Potential Therapeutic Target for Intervertebral Disc Degeneration

open access: yesAdvanced Science, EarlyView.
When nucleus pulposus cells senesce, PHGDH decreases, reducing serine synthesis and glutathione, impairing antioxidant capacity. The intermediate α‐KG also drops, lowering JMJD3 demethylase activity, increasing H3K27me3 at the Rap1b promoter, and reducing Rap1b expression, whose down‐regulation in turn activates mTORC1 and suppresses autophagy ...
Hao‐Wei Xu   +5 more
wiley   +1 more source

Bifunktionale Cosubstrate ermöglichen Threonin‐Dehydrogenase katalysierte chemoenzymatische Pyrrolsynthese

open access: yesAngewandte Chemie, EarlyView.
Klassische Knorr‐Chemie trifft auf moderne Biokatalyse. Die Threonindehydrogenase erzeugt aus l‐Threonin Aminoaceton, welches direkt in einer chemoenzymatischen Knorr‐Pyrrolsynthese abgefangen wird. Ein bifunktionales β‐Dicarbonylsubstrat dient sowohl als Pyrrolbaustein als auch als Hydridakzeptor für integrierte NAD+‐Recyclierung und ermöglicht die ...
Valentina Jurkaš   +8 more
wiley   +1 more source

An analysis of the reaction between immobilized LD and NADH [PDF]

open access: yes, 2001
We tried to analyse the reaction between LD and NADH using a FIA (flow injection analysis) system involving an immobilized enzyme column and chemiluminescence.
田附, 康彦, 田畑, 勝好
core  

Altering the sensitivity of Escherichia coli pyruvate dehydrogenase complex to NADH inhibition by structure-guided design

open access: yes, 2018
A sufficient supply of reducing equivalents is essential for obtaining the maximum yield of target products in anaerobic fermentation. The pyruvate dehydrogenase (PDH) complex controls the critical step in pyruvate conversion to acetyl-CoA and NADH ...
Wang, Xiuwen   +4 more
core   +1 more source

Dual‐Function Cosubstrates Enable Threonine Dehydrogenase‐Driven Chemoenzymatic Pyrrole Synthesis

open access: yesAngewandte Chemie International Edition, EarlyView.
Classical Knorr chemistry meets contemporary biocatalysis. Threonine dehydrogenase generates aminoacetone from l‐threonine, which is directly intercepted in a chemoenzymatic Knorr pyrrole synthesis. A dual‐function β‐dicarbonyl substrate serves as both pyrrole precursor and hydride acceptor for integrated NAD+ recycling, affording substituted pyrroles ...
Valentina Jurkaš   +8 more
wiley   +1 more source

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