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The NuGOwiki Metabolite Database is a joint initiative of NuGO and HMDB
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| Creatine Kinase MB | |
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| [[Image:{{{Image}}}|thumb|220px|2D structure for Creatine Kinase MB]] | |
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| Chemical Information | |
| Biochemical Taxonomy | |
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| Nutritional Taxonomy | |
| Metabolic Pathways | |
| Biofluid Location | |
| Tissue Location | |
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| Normal Tissue Concentrations | |
| Diseases / Conditions Related to Nutrition | |
| Other (Monogenic Disorders) | |
| Abnormal Biofluid Concentrations | |
| Abnormal Tissue Concentrations | |
| Physiological Processes | |
| Authors: | L. Pellis |
| Affiliations: | TNO, the Netherlands |
Contents |
Introduction
Multiple forms (isozymes) are known. Creatine kinase exists as a dimer: the muscle enzyme (MM) consists of 2 identical M subunits, and the brain enzyme (BB) consists of 2 identical B subunits (Dawson et al., 1968). Other tissues show a third, hybrid MB enzyme. Apparently, polymorphism of creatine kinase has not been identified. The dimeric creatine kinase isozymes are involved in maintaining intracellular ATP levels, particularly in tissues that have high energy demands. The creatine kinase MM isozyme is found exclusively in striated muscle; the BB isozyme is found in smooth muscle, brain, and nerve; CKMB is found in human heart.
Damaged cardiac tissue releases creatine kinase MB (CK-MB) 2-6 hours following infarction. CK-MB values peak at 12-24 hours after infarction and return to normal within 24-48 hours. Certain diseases of skeletal muscle result in an increased amount of CK-MB. The various causes of rhabdomyolysis, including the muscular dystrophies, commonly result in an abnormal increase in serum CK-MB activity.
Biological Function
Creatine kinase (EC 2.7.3.2) isoenzymes are crucial to energy metabolism, particularly in tissues with high energy requirements.