Results 11 to 20 of about 11,666 (204)

The Catalytic Decarboxylation of Pyruvate by Thiamine

open access: hybridJournal of Biological Chemistry, 1959
Emeteria Yatco-Manzo   +3 more
openalex   +3 more sources

Decarboxylation of Pyruvate by Thiamine Analogues

open access: hybridJournal of Biological Chemistry, 1959
Sources of Compounds Tested-Thiamine hydrochloride (Merck, U.S.P. grade), 0-acetylthiamine hydrochloride and oxythiamine dihydrochloride (California Foundation for Biochemical Research), pyrithiamine hydrobromide and 4-amino-5 aminomethyl-a-methyl pyrimidine dihydrochloride (Nutritional Biochemicals Corporation) were all used without further ...
Ralph G. Yount, David E. Metzler
openalex   +3 more sources

Pig liver pyruvate carboxylase. The reaction pathway for the decarboxylation of oxaloacetate [PDF]

open access: bronzeBiochemical Journal, 1974
1. The reaction pathway for the decarboxylation of oxaloacetate, catalysed by pig liver pyruvate carboxylase, was studied in the presence of saturating concentrations of K+ and acetyl-CoA. 2. Free Mg2+ binds to the enzyme in an equilibrium fashion and remains bound during all further catalytic cycles.
Graham Warren, Keith F. Tipton
openalex   +4 more sources

Decarboxylation of oxalacetate to pyruvate by purified avian liver phosphoenolpyruvate carboxykinase

open access: hybridJournal of Biological Chemistry, 1975
Phosphoenolpyruvate carboxykinase, which has been isolated from chicken liver mitochondria in essentially homogenous form, carries out the irreversible decarboxylation of oxalacetate to pyruvate in the presence of catalytic amounts of GDP or IDP, as well as the reversible decarboxylation of oxalacetate to phosphoenolpyruvate in the presence of ...
PS Noce, M.F. Utter
openalex   +3 more sources

Evidence for separate enzymes of pyruvate decarboxylation and pyruvate synthesis in soluble extracts of Clostridium pasteurianum.

open access: hybridJournal of Biological Chemistry, 1977
Additional evidence to that already presented (Sauer, F. D., Bush, R. S., and Stevenson, I. L. (1976) Biochim. Biophys. Acta 445, 518-520) suggests that pyruvate-ferredoxin oxidoreductase isolated from Clostridium pasteurianum consists of two separate enzymes: (a) pyruvate lyase, which catalyzes the CoA and electron acceptor-dependent decarboxylation ...
R. S. Bush, Frank Sauer
openalex   +3 more sources

Shortcutting photorespiration: avenues and challenges toward realizing higher-yielding photorespiratory bypass crops. [PDF]

open access: yesNew Phytol
Summary Photorespiration is a major source of photosynthetic inefficiency in C3 crops. In photorespiration, the oxygenation rather than carboxylation of RuBP by Rubisco triggers an energy‐expensive pathway to recycle inhibitory byproducts and recapture lost carbon, ultimately reducing yields.
Meacham-Hensold K   +3 more
europepmc   +2 more sources

Metabolic Response of the Immature Right Ventricle to Acute Pressure Overloading

open access: yesJournal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2018
BackgroundSurgical palliation or repair of complex congenital heart disease in early infancy can produce right ventricular (RV) pressure overload, often leading to acute hemodynamic decompensation.
Masaki Kajimoto   +5 more
doaj   +1 more source

Pyruvate:ferredoxin oxidoreductase and low abundant ferredoxins support aerobic photomixotrophic growth in cyanobacteria

open access: yeseLife, 2022
The decarboxylation of pyruvate is a central reaction in the carbon metabolism of all organisms. It is catalyzed by the pyruvate:ferredoxin oxidoreductase (PFOR) and the pyruvate dehydrogenase (PDH) complex.
Yingying Wang   +10 more
doaj   +1 more source

Pathogenic mechanisms underlying X-linked Charcot-Marie-Tooth neuropathy (CMTX6) in patients with a pyruvate dehydrogenase kinase 3 mutation

open access: yesNeurobiology of Disease, 2016
Charcot-Marie-Tooth disease (CMT) is the most common inherited peripheral neuropathy. An X-linked form of CMT (CMTX6) is caused by a missense mutation (R158H) in the pyruvate dehydrogenase kinase isoenzyme 3 (PDK3) gene.
Gonzalo Perez-Siles   +9 more
doaj   +1 more source

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