The human arginases and arginase deficiency

R. Iyer, C. P. Jenkinson, J. G. Vockley, R. M. Kern, W. W. Grody, S. Cederbaum

Research output: Contribution to journalArticlepeer-review

118 Scopus citations

Abstract

Arginase is the final enzyme in the urea cycle. Its deficiency is the least frequently described disorder of this cycle. It results primarily in elevated blood arginine, and less frequently in either persistent or acute elevations in blood ammonia. This appears to be due to a second arginase locus, expressed primarily in the kidney, which can be recruited to compensate, in part, for the deficiency of liver arginase. The liver arginase gene structure permitted study of the molecular pathology of patients with the disorder and the results of these studies and the inferences about the protein structure are presented. The conserved regions among all arginases allowed the cloning of All, the second arginase isoform. It has been localized to the mitochondrion and is thought to be involved in ornithine biosynthesis. It shares the major conserved protein sequences, and structural features of liver arginase gene are also conserved. When AI and All from various species are compared, it appears that the two diverged some time prior to the evolution of amphibians. The evidence for the role of All in nitric oxide and polyamine metabolism is presented and this appears consonant with the data on the tissue distribution.

Original languageEnglish (US)
Pages (from-to)86-100
Number of pages15
JournalJournal of Inherited Metabolic Disease
Volume21
Issue numberSUPPL. 1
DOIs
StatePublished - 1998

ASJC Scopus subject areas

  • Genetics
  • Genetics(clinical)

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