Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The development of the total rat brain creatine kinase was studied in brain homogenates. Until approx. 14-15 days after birth, the activity remains less than one-third that of the adult activity (207+/-6 units/g wet wt. s.d.; n=3). Over the next 10 days the activity increases markedly to the adult value and thereafter remains essentially constant. 2. In the adult brain, approx. 5% (11.9+/-2.2 units/g wet wt. s.d.; n=5) of the total creatine kinase is associated with the mitochondrial fraction. This creatine kinase could not be solubilized by sodium acetate solutions of up to 0.8m concentration, whereas 66% of the hexokinase associated with brain mitochondria was released under these conditions. 3. Rat brain mitochondria incubated in the presence of various concentrations of creatine (1, 5 and 10mm) and ADP (100mum) synthesized phosphocreatine at rates of approx. 4.5, 11 and 17.5nmol/min per mg of mitochondrial protein. Atractyloside (50mum) or oligomycin (1.5mug/mg of mitochondrial protein) completely inhibited the synthesis of phosphocreatine. 4. The apparent K(m) and V(max.) values of the mitochondrially bound rat brain creatine kinase were determined in both directions. The V(max.) in the direction of phosphocreatine synthesis is 237nmol/min per mg of mitochondrial protein, with an apparent K(m) for creatine of 1.67mm and for MgATP(2-) of 0.1mm, and in the reverse direction V(max.) is 489nmol/min per mg of mitochondrial protein, with an apparent K(m) for phosphocreatine of 0.4mm and for MgADP(-) of 27mum. 5. The results are discussed with reference to the role that the mitochondrially bound creatine kinase may play in the development of brain energy metabolism.
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PMID:Studies on the mitochondrially bound form of rat brain creatine kinase. 62 73

The B-CK isozyme of cytoplasmic creatine kinase is localized distinctly in the terminal web region of the intestinal epithelial cell brush border (Keller and Gordon: Cell Motil. Cytoskeleton 19:169-179, 1991). Experiments were performed to determine whether this CK is energetically coupled to the myosin II that is present in the circumferential ring and interrootlet structural domains of the brush border terminal web. In isolated brush borders, ATP-dependent circumferential ring contraction and interrootlet myosin solubilization were supported either by an exogenous PEP-pyruvate kinase-based ATP-regeneration system (PEP-PK) or by the addition of phosphocreatine to the endogenous B-CK-based ATP-regeneration system (PCr-B-CK). Addition of an exogenous hexokinase-glucose ATP-hydrolysis system (HK-G) effectively blocked both contraction and myosin solubilization in the PEP-PK assay. In contrast, HK-G had no significant effect on PCr-B-CK-supported brush border contraction, although it did inhibit interrootlet myosin solubilization. Thus, when high-energy phosphate is supplied as phosphocreatine, brush border B-CK imparts to the circumferential ring myosin a selective energetic advantage over other ATPases. These results suggest that myosin and B-CK are functionally coupled in the brush border circumferential ring, where they might comprise one end of an energy circuit that supplies energy for contraction, but that colocalization of CK with myosin in the brush border interrootlet domain is insufficient to establish functional coupling.
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PMID:Functional coupling to brush border creatine kinase imparts a selective energetic advantage to contractile ring myosin in intestinal epithelial cells. 153 84