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It is a rare disease in dogs, with cats seven to ten times more likely to be infected. The disease in dogs can affect the lungs and skin, but more commonly the eye and central nervous system. [20] Ringworm is a fungal skin disease that in dogs is caused by Microsporum canis (70%), Microsporum gypseum (20%), and Trichophyton mentagrophytes (10% ...
This article provides a list of autoimmune diseases. These conditions, where the body's immune system mistakenly attacks its own cells, affect a range of organs and systems within the body. Each disorder is listed with the primary organ or body part that it affects and the associated autoantibodies that are typically found in people diagnosed ...
Late-onset PFK deficiency, as the name suggests, is a form of the disease that presents later in life. Common symptoms associated with late-onset phosphofructokinase deficiency are myopathy, weakness and fatigue. Many of the more severe symptoms found in the classic type of this disease are absent in the late-onset form. [citation needed]
[2] [3] It is allosterically inhibited by ATP and allosterically activated by AMP, thus indicating the cell's energetic needs when it undergoes the glycolytic pathway. [4] PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta ...
List of aquarium diseases; List of dog diseases; List of feline diseases; List of diseases of the honey bee; List of diseases spread by invertebrates; Poultry disease; Lists of zoonotic diseases, infectious diseases that have jumped from an animal to a human
This may be due to redirecting glucose flux towards the pentose phosphate pathway to generate NADPH to detoxify reactive oxygen species. [19] Herpes simplex type 1 and phosphofructokinase: Some viruses, including HIV, HCMV and Mayaro affect cellular metabolic pathways such as glycolysis by a MOI-dependent increase in the activity of PFK.
PFK-2 is known as the "bifunctional enzyme" because of its notable structure: though both are located on one protein homodimer, its two domains act as independently functioning enzymes. [5] One terminus serves as a kinase domain (for PFK-2) while the other terminus acts as a phosphatase domain (FBPase-2). [6]
This 85-kDa protein is one of two subunit types that comprise the seven tetrameric PFK isozymes. [6] [7] The muscle isozyme is composed solely of PFKM.[6] [8] [9] The liver PFK (PFK-5) contains solely the second subunit type, PFKL, while the erythrocyte PFK includes five isozymes composed of different combinations of PFKM and PFKL.