aminotransferase

The systematic name of this enzyme class is D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase.

Five patients' aminotransferase activities more than doubled during treatment.

Of the total aromatic aminotransferase activity, 10-20% was found in the periplasm.

The enzyme involved in this reaction is an aminotransferase.

A reverse of the alanine aminotransferase reaction takes place in liver.

Other names in common use include 3,5-dinitrotyrosine transaminase, and thyroid hormone aminotransferase.

The disease results from a deficiency in hepatic tyrosine aminotransferase.

Tyrosinemia is the most common metabolic disease associated with tyrosine aminotransferase.

Ornithine aminotransferase forms the initial intermediate in this process.

Tyrosine Aminotransferase as a dimer has two identical active sights.

The branched chain aminotransferase found in this image was isolated from mycobacteria.

This enzyme is also called 4-hydroxyglutamate aminotransferase.

The possible periplasmic location of an aromatic aminotransferase has been anticipated, but not directly examined until now.

Serum aminotransferase activities and bilirubin concentrations were measured by autoanalyser.

The enzyme contains two major domains, responsible for the aminotransferase and synthase activity, respectively.

In addition, both interferon courses induced transient rises in aminotransferase levels.

Enzymes involved are branched chain aminotransferase and 3-methyl-2-oxobutanoate dehydrogenase.

This reaction is catalyzed by the enzyme succinyl diaminopimelate aminotransferase.

Side effects during the study included alanine aminotransferase, proteinuria, and hypertension (elevated blood pressure) among others.

Two peaks with aromatic aminotransferase activity eluted from the hydroxylapatite column mentioned above.

In most patients, asymptomatic aminotransferase elevations resolve spontaneously.

It inhibits ornithine aminotransferase at concentrations as low as 10 nM.

Glutamate acts as the amine donor for ornithine aminotransferase, forming α-ketoglutarate.

The major peak of aromatic aminotransferase was pooled and subjected to Superdex gel filtration as described above.

The fractions showing high aromatic aminotransferase activity were pooled and concentrated by centrifugal filtration.