Creatine Kinase MB

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Creatine Kinase MB
[[Image:{{{Image}}}|thumb|220px|2D structure for Creatine Kinase MB]]
Chemical Name
Chemical Formula
CAS Number
Chemical Information
Biochemical Taxonomy
Functional Taxonomy
Nutritional Taxonomy
Metabolic Pathways
Biofluid Location
Tissue Location
Normal Biofluid Concentrations
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

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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

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Creatine kinase (EC 2.7.3.2) isoenzymes are crucial to energy metabolism, particularly in tissues with high energy requirements.

Catabolism

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Diseases / Conditions Related to Nutrition

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Other (Monogenic) Disorders

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Nutritional Information

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Other resources

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Links

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CK M OMIM UniProtKB

CK B OMIM UniProtKB