Aspartate aminotransferase Chemical Properties

Density 

1.17 g/mL at 20 °C

storage temp. 

2-8°C

form 

lyophilized powder

color 

Colorless to light yellow

EPA Substance Registry System

Aminotransferase, aspartate (9000-97-9)

Safety Information

Safety Statements 

22-24/25

WGK Germany 

3

TSCA 

Yes

MSDS

• Language:English Provider:SigmaAldrich

Aspartate aminotransferase Usage And Synthesis

Uses

Converts L-aspartate and alpha-ketoglutarate to oxaloacetate and L-glutamate

Definition

An enzyme that catalyzes reversibly the transfer of an amino group from glutamic acid to oxaloacetic acid, yielding α-ketoglutaric acid and aspartic acid. The codons for aspartate are GAC and GAU.

General Description

Glutamic-Oxalacetic Transaminase is found in all tissues and is predominant in the liver and skeletal muscle. It is a prototype of fold-type I pyridoxal 5′-phosphate (PLP)-enzymes. Glutamic-oxalacetic transaminase is a homodimer containing large and small domains in each subunit.

Biochem/physiol Actions

Glutamic-oxalacetic transaminase or aspartate aminotransferase (AAT) catalyzes the interconversion of L-aspartate and α-ketoglutarate with oxalacetate and L-glutamate. This reversible transaminase reaction is dependent on pyridoxal 5′-phosphate (PLP). Glutamic-oxalacetic transaminase maintains the nitrogen currency for metabolism by generating L-glutamate. Elevated serum levels of glutamic-oxalacetic transaminase are indicated in myocardial infarction, liver diseases, and some renal diseases.

Aspartate aminotransferase(9000-97-9)Related Product Information

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