Results 101 to 110 of about 114,163 (257)

Novel mitochondrial substrates of omi indicate a new regulatory role in neurodegenerative disorders. [PDF]

open access: yesPLoS ONE, 2009
The mitochondrial protease OMI (also known as HtrA2) has been implicated in Parkinson's Disease (PD) and deletion or protease domain point mutations have shown profound neuropathologies in mice.
Felicity Johnson, Michael G Kaplitt
doaj   +1 more source

Inhibitors of Pyruvate Carboxylase [PDF]

open access: yes, 2010
This review aims to discuss the varied types of inhibitors of biotin-dependent carboxylases, with an emphasis on the inhibitors of pyruvate carboxylase.
Attwood, Paul V.   +2 more
core   +2 more sources

Malic enzyme facilitates D-lactate production through increased pyruvate supply during anoxic dark fermentation in Synechocystis sp. PCC 6803.

open access: yesACS Synthetic Biology, 2020
D-Lactate is one of the most valuable compounds for manufacturing bio-based polymers. Here, we have investigated the significance of endogenous malate dehydrogenase (decarboxylating) (Malic enzyme, ME), which catalyzes the oxidative decarboxylation of ...
Ryota Hidese   +4 more
semanticscholar   +1 more source

Diseases associated with the oxidative decarboxylation of pyruvate

open access: yes, 2021
Introducere. Decarboxilarea oxidativă a piruvatului reprezintă un proces biochimic complex. Produsul final Acetil-Co-A este utilizat ca substrat esențial în diverse căi metabolice de importanță vitală. Erorile în funcționarea acestui proces biochimic provoacă consecințe patometabolice periculoase. Scopul lucrării.
Colin, M., Timercan, T.V.
openaire   +1 more source

How Plants May Maintain Protein Homeostasis Under Rising Atmospheric CO2

open access: yesPlant, Cell &Environment, EarlyView.
ABSTRACT Vascular plants may employ several physiological mechanisms to stabilize their protein contents as atmospheric CO2 concentrations change over a day, year, decade, or century. One mechanism is that plants may rely more on soil ammonium as their nitrogen source when CO2 increases.
Arnold J. Bloom   +2 more
wiley   +1 more source

13C Tracers for Glucose Degrading Pathway Discrimination in Gluconobacter oxydans 621H

open access: yesMetabolites, 2015
Gluconobacter oxydans 621H is used as an industrial production organism due to its exceptional ability to incompletely oxidize a great variety of carbohydrates in the periplasm. With glucose as the carbon source, up to 90% of the initial concentration is
Steffen Ostermann   +5 more
doaj   +1 more source

Engineering pyruvate decarboxylase-mediated ethanol production in the thermophilic host Geobacillus thermoglucosidasius [PDF]

open access: yes, 2013
This study reports the expression, purification, and kinetic characterization of a pyruvate decarboxylase (PDC) from Gluconobacter oxydans . Kinetic analyses showed the enzyme to have high affinity for pyruvate (120 μM at pH 5), high catalytic efficiency
A Correa   +56 more
core   +1 more source

pdh modulate virulence through reducing stress tolerance and biofilm formation of Streptococcus suis serotype 2

open access: yesVirulence, 2019
Streptococcus suis serotype 2 (S. suis 2) is a zoonotic pathogen. It causes meningitis, arthritis, pneumonia and sepsis in pigs, leading to extremely high mortality, which seriously affects public health and the development of the pig industry.
Yang Wang   +7 more
doaj   +1 more source

Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae [PDF]

open access: yes, 2002
Leucine and valine are formed in a common pathway from pyruvate in which the first intermediate is 2-acetolactate. In some bacteria, this compound also has a catabolic fate as the starting point for the butanediol fermentation.
Duggleby, R.G.   +2 more
core   +2 more sources

Regulation of pyruvate dehydrogenase complex: Dancing to different drums in cancer

open access: yesInternational Journal of Cancer, Volume 158, Issue 6, Page 1464-1480, 15 March 2026.
Abstract Mechanisms governing the regulation of pyruvate dehydrogenase complex (PDC) are markedly modified in cancer cells compared to normal cells. PDC activity in normal cells is controlled by the reversible phosphorylation of three serine residues by dedicated kinases and phosphatases.
Mulchand S. Patel, Todd C. Rideout
wiley   +1 more source

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