Sechenov School
Home › Biochemistry › Creatine Kinase

Creatine Kinase

Creatine kinase

For medical students2 min readUpdated 2026-10-10

Creatine kinase (CK) is an enzyme that catalyzes the formation of the high-energy compound creatine phosphate. Determining the activity of various isoforms of this enzyme in blood plasma is a crucial tool in clinical biochemistry for diagnosing myocardial and skeletal muscle damage.

StructureThe enzyme is a dimer consisting of two subunits
Infarction markerBlood levels of the MB isoform increase specifically during myocardial injury
BB isoform propertyPractically undetectable in blood even during strokes due to the blood-brain barrier
Reaction chemistryTransfer of a phosphate group from ATP to the amine group of creatine

Function and Catalyzed Reaction

The primary function of creatine kinase in the body is to provide reversible phosphorylation of creatine. This process yields creatine phosphate, a vital high-energy compound that serves as a cellular energy reserve.

The chemical reaction involves the transfer of a phosphate group ($PO_3H_2$) from an ATP molecule directly to the amino group of a creatine molecule.

Reaction components:

Structure and Isoforms

Structurally, the creatine kinase molecule is a dimer, meaning a protein composed of exactly two subunits. Two basic types of subunits exist, named after the English terms reflecting their primary tissue localization:

  1. M (Muscle) — muscle subunit.
  2. B (Brain) — brain subunit.

Various paired combinations of these subunits form three creatine kinase isoenzymes (isoforms). They differ in electrophoretic mobility—the rate of directed movement from the origin (cathode, "minus") to the anode ("plus") in an electric field:

Tissue Localization

Each isoform has a strict tissue distribution, determining its role in the cellular metabolism of specific organs:

Clinical and Diagnostic Significance

Measuring the levels of various creatine kinase isoforms in blood plasma serves as a valuable diagnostic criterion in several acute conditions:

  1. Myocardial Infarction. When cardiomyocytes die, cell destruction occurs, and the MB isoform is actively released into blood plasma. Its elevation is considered one of the most important diagnostic markers for myocardial infarction.
  2. Skeletal Muscle Injury. Following physical trauma, crush syndrome, or other muscle damage, the amount of the muscle isoform MM increases in the blood accordingly.
  3. Central Nervous System Pathologies. Unlike the myocardium and skeletal muscles, the brain BB isoform is virtually undetectable in the blood during strokes and other CNS lesions. This is because the enzyme is physically unable to cross the blood-brain barrier. Consequently, measuring blood creatine kinase has no clinical diagnostic value for assessing brain pathologies.

Mnemonic

To easily remember the localization of the isoforms, rely on the English letters: M (Muscle) for muscles, B (Brain) for brain. The MM isoform works in skeletal muscles, BB in the brain, and their hybrid MB takes a bit from both and operates in the body's "motor"—the myocardium.

Frequently asked questions

How soon after a myocardial infarction does the CK-MB level reach its peak in the blood?

Creatine kinase levels reach their peak within 24 hours after the onset of a myocardial infarction.

Dynamics of enzyme activity in the blood:

  • Onset of elevation — expected 3–6 hours after the attack (acts as an early marker of injury).
  • Peak activity — reached by 24 hours (rises rapidly and peaks first).
  • Decline — after reaching the peak, activity decreases relatively rapidly.

Myocardial infarction involves the destruction of cardiomyocytes and an increase in plasma-specific MB creatine kinase isoform.

What is the essence of the reaction catalyzed by creatine kinase?

The enzyme catalyzes the reversible phosphorylation of creatine using ATP. A phosphate group is transferred to the amino group of creatine, producing the high-energy compound creatine phosphate and an ADP molecule.

Why does the creatine kinase level not rise during a stroke?

Brain tissue contains the BB isoform. When brain tissue is damaged, this enzyme cannot cross the blood-brain barrier to enter the systemic circulation, so it is not detected in blood plasma.

Which creatine kinase isoform has the highest electrophoretic mobility?

The brain isoform CK-1 (BB) possesses maximum mobility. During electrophoresis, it moves from the cathode to the anode faster than the others.

Go deeper

More topics in Biochemistry

Role of Glutathione in ErythrocytesIsoenzymesLactate DehydrogenaseGenetic PolymorphismLactate Metabolism and the Effects of Ethanol on Carbohydrate MetabolismFat BiosynthesisRecombinant DNA TechnologyRegulation of Glycolysis and Gluconeogenesis in the LiverObesityEnzymopathiesDNA Diagnostics and Gene TherapyFate of Amino Acid Carbon SkeletonsBiochemistry →