(Redirected from Liver aminotransferases)
Jump to navigation Jump to search
Aspartate transaminase from E. coli with Pyridoxal 5' Phosphate cofactor


WikiDoc Resources for Transaminase


Most recent articles on Transaminase

Most cited articles on Transaminase

Review articles on Transaminase

Articles on Transaminase in N Eng J Med, Lancet, BMJ


Powerpoint slides on Transaminase

Images of Transaminase

Photos of Transaminase

Podcasts & MP3s on Transaminase

Videos on Transaminase

Evidence Based Medicine

Cochrane Collaboration on Transaminase

Bandolier on Transaminase

TRIP on Transaminase

Clinical Trials

Ongoing Trials on Transaminase at Clinical

Trial results on Transaminase

Clinical Trials on Transaminase at Google

Guidelines / Policies / Govt

US National Guidelines Clearinghouse on Transaminase

NICE Guidance on Transaminase


FDA on Transaminase

CDC on Transaminase


Books on Transaminase


Transaminase in the news

Be alerted to news on Transaminase

News trends on Transaminase


Blogs on Transaminase


Definitions of Transaminase

Patient Resources / Community

Patient resources on Transaminase

Discussion groups on Transaminase

Patient Handouts on Transaminase

Directions to Hospitals Treating Transaminase

Risk calculators and risk factors for Transaminase

Healthcare Provider Resources

Symptoms of Transaminase

Causes & Risk Factors for Transaminase

Diagnostic studies for Transaminase

Treatment of Transaminase

Continuing Medical Education (CME)

CME Programs on Transaminase


Transaminase en Espanol

Transaminase en Francais


Transaminase in the Marketplace

Patents on Transaminase

Experimental / Informatics

List of terms related to Transaminase

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]


In biochemistry, a transaminase or an aminotransferase is an enzyme that catalyzes a type of reaction between an amino acid and an α-keto acid. Specifically, this reaction (transamination) involves removing the amino group from the amino acid, leaving behind an α-keto acid, and transferring it to the reactant α-keto acid and converting it into an amino acid. The enzymes are important in the production of various amino acids, and measuring the concentrations of various transaminases in the blood is important in the diagnosing and tracking many diseases. Transaminases require the coenzyme pyridoxal-phosphate, which is converted into pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid. Enzyme-bound pyridoxamine in turn reacts with pyruvate, oxaloacetate, or alpha-ketoglutarate, giving alanine, aspartic acid, or glutamic acid, respectively.

The presence of elevated transaminases can be an indicator of liver damage.

Transaminases in amino acid metabolism in animals

Animals must metabolize proteins to amino acids, at the expense of muscle tissue, when blood sugar is low. The preference of liver transaminases for oxaloacetate or alpha-ketoglutarate plays a key role in funneling nitrogen from amino acid metabolism to Asp and Glu for conversion to urea for excretion of nitrogen. Similarly, in muscles the use of pyruvate for transamination gives Ala, which is carried by the bloodstream to the liver. Here other transaminases regenerate pyruvate, which provides a valuable precursor for gluconeogenesis. This alanine cycle is analogous to the Cori cycle which allows anaerobic metabolism by muscles.


  • Ghany, Marc & Hoofnagle, Jay H. (2005). Approach to the Patient With Liver Disease. In Dennis L. Kasper, Anthony S. Fauci, Dan L. Longo, Eugene Braunwald, Stephen L. Hauser, & J. Larry Jameson (Eds.), Harrison's Principles of Internal Medicine (16th Edition), pp. 1814–1815. New York: McGraw-Hill.
  • Nelson, David L. & Cox, Michael M. (2000). Lehninger Principles of Biochemistry (3rd ed.), pp. 628–631, 634, 828–830. New York: Worth Publishers.

See also

External links

de:Transaminase it:Transaminasi

Template:WikiDoc Sources