Human type II arginase, which is extrahepatic and mitochondrial in location, catalyzes the
hydrolysis of arginine to form ornithine and urea. While type I arginases function in the net …

There are two forms of arginase in humans, both catalyzing the hydrolysis of arginine to
ornithine and urea. Recent studies in animal models and in Type I arginase-deficient …

Two forms of arginase, both catalyzing the hydrolysis of arginine to ornithine and urea, are
found in animals ranging from amphibians to mammals. In humans, inherited deficiency of …

Mammals contain two genes encoding distinct isoforms of arginase (arginases I and II), both
of which catalyze the conversion of arginine to ornithine and urea. However, their …

Liver-type arginase (arginase I) is expressed almost exclusively in the liver and catalyzes
the last step of urea synthesis, whereas the nonhepatic type (arginase II) is expressed in …

Studies in experimental animals and humans demonstrate the existence of two arginase
isozymes. One, designated AI (or A1), has a high pI, is located in the cytosol, is most …

The two forms of arginase (AI and AII) in man, identical in enzymatic function, are encoded in
separate genes and are expressed differentially in various tissues. AI is expressed …

Of all arginine catabolic enzymes, the arginases and nitric oxide (NO) synthases are the
ones that are of greatest interest to many investigators. Mammalian arginases catalyze the …

Arginases catalyze the hydrolysis of l-arginine to yield l-ornithine and urea. Recent studies
indicate that arginases, both the type I and type II isozymes, participate in the regulation of …

A full-length cDNA encoding type II arginase was isolated from a human kidney cDNA library
and its sequence compared to those of vertebrate type I arginases as well as to arginases of …