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Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production
- A. Michelucci, Thekla Cordes, K. Hiller
- BiologyProceedings of the National Academy of Sciences
- 22 April 2013
It is shown that itaconic acid inhibits the growth of bacteria expressing isocitrate lyase, such as Salmonella enterica and Mycobacterium tuberculosis, and Irg1 gene silencing in macrophages resulted in significantly decreased intracellular itaconi acid levels as well as significantly reduced antimicrobial activity during bacterial infections.
Arabidopsis VTC2 Encodes a GDP-l-Galactose Phosphorylase, the Last Unknown Enzyme in the Smirnoff-Wheeler Pathway to Ascorbic Acid in Plants*♦
In characterizing recombinant VTC2 from A. thaliana as a specific GDP-l-galactose/GDP-d-glucose phosphorylase, it is concluded that enzymes catalyzing each of the ten steps of the Smirnoff-Wheeler pathway from glucose to ascorbate have been identified.
L-Ascorbate biosynthesis in higher plants: the role of VTC2.
Extremely Conserved ATP- or ADP-dependent Enzymatic System for Nicotinamide Nucleotide Repair*
- Alexandre Y Marbaix, G. Noël, Aline M Detroux, D. Vertommen, E. Van Schaftingen, Carole L. Linster
- BiologyJournal of Biological Chemistry
- 12 October 2011
This work identified an enzymatic repair system for hydrated NAD(P)H consisting of an ATP- or ADP-dependent dehydratase and an epimerase and indicates that searches for other enzymes involved in metabolite and coenzyme repair might be fruitful.
Metabolite damage and its repair or pre-emption.
Chemical biology is demonstrating that diverse metabolites are damaged by side reactions of 'promiscuous' enzymes or by spontaneous chemical reactions, that the products are useless or toxic and that the unchecked buildup of these products can be devastating.
Impact of Oxidative Stress on Ascorbate Biosynthesis in Chlamydomonas via Regulation of the VTC2 Gene Encoding a GDP-l-galactose Phosphorylase*
The results indicate that C. reinhardtii VTC2, like its plant homologs, is a highly regulated enzyme in ascorbate biosynthesis in green algae and that, together with the asCorbate recycling system, the l-galactose pathway represents the major route for providing protective levels of ascorBate in oxidatively stressed algal cells.
Biosynthesis, recycling and degradation in mammals
A conserved phosphatase destroys toxic glycolytic side products in mammals and yeast.
It is discovered that a single, widely conserved enzyme, known as phosphoglycolate phosphatase (PGP) in mammals, dephosphorylates both 4-Phosphoerythronate and 2-phospho-L-lactate, thereby preventing a block in the pentose phosphate pathway and glycolysis.
Saccharomyces cerevisiae Forms d-2-Hydroxyglutarate and Couples Its Degradation to d-Lactate Formation via a Cytosolic Transhydrogenase*♦
- Julia Becker-Kettern, Nicole Paczia, Carole L. Linster
- BiologyThe Journal of Biological Chemistry
- 16 January 2016
It is proposed that 2HG is mainly formed and degraded in the cytosol of S. cerevisiae cells in a process that couples d-2HG metabolism to the shuttling of reducing equivalents from cytosolic NADH to the mitochondrial respiratory chain via the d-lactate dehydrogenase Dld1.
Millifluidic culture improves human midbrain organoid vitality and differentiation.
A computational model of oxygen transport and consumption in hMOs predicted higher oxygen levels in the hMO core region under millifluidic conditions, and a significantly smaller "dead core" was observed in h MOs cultured in a bioreactor system compared to those ones kept under conventional shaking conditions.