Comparative properties of arginases

Christopher P. Jenkinson, Wayne W. Grody, Stephen D. Cederbaum

Research output: Contribution to journalArticlepeer-review

471 Scopus citations

Abstract

Arginase is a primordial enzyme, widely distributed in the biosphere and represented in all primary kingdoms. It plays a critical role in the hepatic metabolism of most higher organisms as a cardinal component of the urea cycle. Additionally, it occurs in numerous organisms and tissues where there is no functioning urea cycle. Many extrahepatic tissues have been shown to contain a second form of arginase, closely related to the hepatic enzyme but encoded by a distinct gene or genes and involved in a host of physiological roles. A variety of functions has been proposed for the 'extrahepatic' arginases over the last three decades. In recent years, interest in arginase has been stimulated by a demonstrated involvement in the metabolism of the ubiquitous and multifaceted molecule nitric oxide. Molecular biology has begun to furnish new clues to the disparate functions of arginases in different environments and organisms. Comparative studies of arginase sequences are also beginning to elucidate the comparative evolution of arginases, their molecular structures and the nature of their catalytic mechanism. Further studies have sought to clarify the involvement of arginase in human disease. This review presents an outline of the current state of arginase research by giving a comparative overview of arginases and their associated properties.

Original languageEnglish (US)
Pages (from-to)107-132
Number of pages26
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume114
Issue number1
DOIs
StatePublished - 1996

Keywords

  • arginase
  • catalysis
  • comparative evolution
  • hepatic
  • hyperargininemia
  • isozymes
  • nitric oxide
  • urea cycle

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Comparative properties of arginases'. Together they form a unique fingerprint.

Cite this