Disease relevance of Fkbp6_predicted

• Suspensions of intact Ehrlich and Sarcoma 37 cells exhibited low PPiase activity, but this was only about 1 to 2% of the intracellular activity and was completely accounted for by activity present in the suspension medium [1].
• Systematic fractionation of subcellular components revealed that 92% of the total PPiase activity of rat liver and 97.5% of that of Hepatoma 3924A were in the cytosol [1].

High impact information on Fkbp6_predicted

• Only negligible PPiase activities were found in cell membranes isolated by sucrose gradient centrifugation [1].
• These results discount the occurrence of PPiase activity as an ectoenzyme or in the plasma membrane of these cells and point to the cytosol as the major and mitochondria as a minor locus of intracellular PPiase activity [1].
• CHL is without effect on the enzyme of fully disrupted microsomes or the system inorganic pyrophosphatase (PPiase) activity [2].
• Loss of Fkbp6 results in abnormal pairing and misalignments between homologous chromosomes, nonhomologous partner switches, and autosynapsis of X chromosome cores in meiotic spermatocytes [3].
• Fertility and meiosis are normal in Fkbp6 mutant females [3].

Biological context of Fkbp6_predicted

• Essential role of Fkbp6 in male fertility and homologous chromosome pairing in meiosis [3].
• Here we show that FK506 binding protein (Fkbp6) localizes to meiotic chromosome cores and regions of homologous chromosome synapsis [3].

Anatomical context of Fkbp6_predicted

• Targeted inactivation of Fkbp6 in mice results in aspermic males and the absence of normal pachytene spermatocytes [3].
• The data are consistent with the concept that GPase, PPiase and ATPase activities of cementum to a major part stem from one enzyme, namely nonspecific alkaline phosphatase [4].
• Some properties of inorganic pyrophosphatase (PPiase EC 3.6.1.1.) and para-nitrophenylphosphatase (p-NPPase EC 3.1.3.1) in the microsomal fraction of odontoblasts were investigated [5].
• The enzyme inorganic pyrophosphatase (PPiase, EC 3.6.1.1) from the odontoblastic layer of rat incisors has been studied by means of a radiochemical micromethod [6].
• The inorganic pyrophosphatase (PPiase) activity was determined by a colorimetric method in the odontoblasts and the parts of the enamel organ related to enamel matrix formation and enamel maturation [7].

Associations of Fkbp6_predicted with chemical compounds

• However, the inhibition of both PPiase and Glc-6-Pase by HNB becomes irreversible following incubation of HNB-exposed microsomes with 2.5 mm sodium borohydride, indicating that inhibition involves the formation of a Schiff base [2].
• Ca2+ alone inhibited the enzyme whereas, in the presence of EDTA, a Ca2+ stimulation of the PPiase was observed which was substrate-dependent and had an optimal activity at a Ca2+:PP4-i ratio of 1:1 [8].
• In hard tissues, several enzymes (adenosine triphosphatase (ATPase), alkaline phosphatase (APase), adenylate cyclase (AC) and perhaps pyrophosphatase (PPiase) are able to degrade adenosine triphosphate (ATP) [9].
• The influence of three diphosphonates, ethane-1-hydroxy 1.1. diphosphonate, methane-diphosphonate and dichloromethane diphosphonate, on inorganic pyrophosphatase (PPiase, E.C. 3.6.1.1.) was investigated [8].
• The characteristics of nonspecific alkaline phosphatase, (APase, EC 3.1.3.1.) measured as beta-glycerophosphatase (GPase, EC 3.1.3.1.), inorganic pyrophosphatase (PPiase, EC 3.6.1.1.) and adenosine triphosphatase (ATPase, EC 3.6.1.3.) were studied in detail of butanol extracts prepared from rat molar cementum [4].

References