GO curators for mouse genes have assigned the following annotations to the gene product of Pfkm. (This text reflects annotations as of Wednesday, January 23, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of October 6, 2008. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.Summary from NCBI RefSeq
[Summary is not available for the mouse gene. This summary is for the human ortholog.] Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Tetramer composition varies depending on tissue type. This gene encodes the muscle-type isozyme. Mutations in this gene have been associated with glycogen storage disease type VII, also known as Tarui disease. Alternatively spliced transcript variants have been described.[provided by RefSeq, Nov 2009]Summary text based on GO annotations supported by experimental evidence in mouse
Researchers have inferred from direct assay, that the gene product of Pfkm
participates in the following biological processes:
Gekakis N et al. (1989) Phosphofructokinase isozyme expression during myoblast differentiation. J Biol Chem, 264:3658-61. (PubMed:2521854)
Nakamura N et al. (2010) Molecular complex of three testis-specific isozymes associated with the mouse sperm fibrous sheath: hexokinase 1, phosphofructokinase M, and glutathione S-transferase mu class 5. Biol Reprod, 82:504-15. (PubMed:19889946)
Richard AM et al. (2007) Tissue-dependent loss of phosphofructokinase-M in mice with interrupted activity of the distal promoter: impairment in insulin secretion. Am J Physiol Endocrinol Metab, 293:E794-801. (PubMed:17595219)
Schliselfeld LH et al. (2002) Inverse relationship of skeletal muscle glycogen from wild-type and genetically modified mice to their phosphorylase a activity. Biochem Biophys Res Commun, 290:874-7. (PubMed:11785984)