Comparative properties of arginases

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 i...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 1996-05, Vol.114 (1), p.107-132
Main Authors: Jenkinson, Christopher P., Grody, Wayne W., Cederbaum, Stephen D.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Arginase
Arginase - chemistry
Arginase - physiology
Arginine - metabolism
Biological Evolution
catalysis
comparative evolution
hepatic
Humans
hyperargininemia
Invertebrates
isozymes
Liver - enzymology
Molecular Sequence Data
nitric oxide
Plants - enzymology
Space life sciences
Urea - metabolism
urea cycle
Vertebrates
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Summary: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.
ISSN:1096-4959
1879-1107
DOI:10.1016/0305-0491(95)02138-8