2.7.3.2	ADP + phosphocreatine	-	
2.7.3.2	ATP + creatine	-	
2.7.3.2	ATP + creatine	role in anaerobic metabolism	
2.7.3.2	ATP + creatine	regeneration of ATP as primary energy source	
2.7.3.2	ATP + creatine	mitochondrial model of CK in energy transport	
2.7.3.2	ATP + creatine	coupled to (Na+,K+)ATPase system	
2.7.3.2	ATP + creatine	physiological roles: 1. buffering of ADP/ATP ratio, 2. transport of high-energy phosphates from sites of ATP production to sites of ATP consumption	
2.7.3.2	ATP + creatine	overview on physiological roles	
2.7.3.2	ATP + creatine	evolution of enzyme, phylogenetics	
2.7.3.2	ATP + creatine	key enzyme in energy homeostasis	
2.7.3.2	ATP + creatine	key enzyme of energy homeostasis	
2.7.3.2	ATP + creatine	the enzyme is involved in energy homeostasis	
2.7.3.2	ATP + creatine	the mitochondrial isozyme MtCK catalyzes the almost complete transphosphorylation of mitochondrial ATP and cytosolic creatine into ADP and phophocreatine. ADP locally generated by MtCK is transferred into the matrix for rephosphorylation and phosphocreatine is released from mitochondria into the cytosol, direct channelling of ATP and ADP between mitochondrial matrix and MtCK via adenine nucleotide transporter	
2.7.3.2	additional information	enzyme inhibition, e.g. by branched chain alpha-amino acids, might contribute to the brain damage maple syrup urine disease MSUD	
2.7.3.2	additional information	probable enzyme evolution, overview	
2.7.3.2	additional information	ADP re-cycling accomplished by mitochondrial creatine kinase regulates reactive oxygen species generation, particularly in high glucose concentrations. Key role of enzyme as a preventive antioxidant against oxidative stress	
2.7.3.2	additional information	using a yeast two-hybrid screening to search for molecules that interact with NCX1 (sodium-calcium exchanger) it is shown that sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL. In addition to sMiCK, cytoplasmic muscle-type CK (CKM) is also able to interact with NCX1 in mammalian cells	
2.7.3.2	additional information	membrane proteins VAMP2/3 and JWA are putative BCK interaction partners. At the plasma membrane, BCK interacts with at least two members of the family of cation-coupled chloride transporters (solute carrier family 12): the K+/Cl- cotransporters 2 (KCC2 or SLC12A5) and 3 (KCC3 or SLC12A6), BCK may be required for maximal phosphorylation efficiency	
2.7.3.2	additional information	synaptical vesicle protein VAMP2/3 and membrane protein and JWA are BCK interaction partners, by Y2H assays. VAMP3 interacts with both, wild-type BCK and truncated DELTABCK mutant. The common and characteristic SNARE domain of VAMPs (amino acids 14-74 in VAMP3) is not sufficient for BCK interaction. JWA and VAMP both link BCK to energy-requiring intracellular vesicle transport