PFKL (P17858) - Overview - Molecular Target Synopsis
PFKL, ATP-dependent 6-phosphofructokinase, liver type
Enzyme Classification 184.108.40.206
Also Known as PFKAL_HUMAN, PFKL
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:22923583). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway. Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (where M stands for Muscle), PFKL (Liver) and PFKP (Platelet). The composition of the PFK tetramer differs according to the tissue type it is present in. In muscles, it is composed of 4 PFKM subunits (also called M4). In the liver, the predominant form is a tetramer of PFKL subunits (L4). In erythrocytes, both PFKM and PFKL subunits randomly tetramerize to form M4, L4 and other combinations (ML3, M2L2, M3L). The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues.
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UniProt: PFKL is active in the following subcellular-locations: cytoplasm.
GO terms: PFKL is active in the following subcellular-locations: 6-phosphofructokinase complex, cytosol, extracellular exosome, extracellular region, ficolin-1-rich granule lumen, membrane, secretory granule lumen.