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 …

Mammals express two isoforms of arginase, designated types I and II. Arginase I is a
component of the urea cycle, and inherited defects in arginase I have deleterious …

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 …

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 …

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 …

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 …

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 …

A human liver cDNA library was screened by colony hybridization with a rat liver arginase
cDNA. The number of positive clones detected was in agreement with the estimated …

Arginases and related enzymes metabolize arginine or similar nitrogen-containing
compounds to urea or formamide. In the present report a sequence alignment of 31 …

Arginase (EC 3.5. 3.1) catalyzes the last step of the urea cycle in the liver of ureotelic
animals. Inherited deficiency of the enzyme results in argininemia, an autosomal recessive …