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==='''Introduction'''===
==='''Introduction'''===
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Arginase is a 105 kD homotrimeric enzyme that requires manganese for the hydrolysis of L-arginine to form L-ornithine and urea. There are two genetically distinct isozymes which have evolved with differing tissue distributions and subcellular locations in mammals. The two types of arginase found in mammalian are arginase I and II. Arginase I is found predominantly in the liver, where it catalyzes the final cytosolic step of the urea cycle. Arginase II is a mitochondrial enzyme that does not appear to function in the urea cycle and is more widely distributed in numerous tissues, for example, kidney, brain, skeletal muscle, and liver. (Note: more will be updated soon)
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Arginase is a 105 kD homotrimeric metallo-protein that catalysis the hydrolysis of arginine to ornithine and urea by means of a binuclear spin-coupled Mn2+ cluster in the active site5. Many organisms contain the enzyme arginase, for example Homo sapiens and Plasmodium falciparum, a parasite that causes cerebral malaria1. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals2.
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The two types of arginases found in mammalian, are arginase I (hAI) and arginases II (hAII)2. Arginase I is found predominantly in the liver, where it catalyzes the final cytosolic step of the urea cycle2. Arginases II is a mitochondrial enzyme that does not appear to function in the urea cycle and is more widely disturbed in numerous tissues, for example kidney, brains, skeletal muscle, mammary gland and penile corpus cavernosum2. Recent studies show that Plasmodium falciparum arginase (PFA) plays a role in systemic depletion of arginine levels, which in turn has been associated with human cerebral malaria pathogenesis5. In addition the arginase fold is part of the ureohydrolase superfamily, which also includes agmatinase, histone de-acetylase and acetylpolyamine amidohydrolase5.
==='''Structure'''===
==='''Structure'''===
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Revision as of 03:53, 2 April 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
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PDB ID 3mmr

Drag the structure with the mouse to rotate
3mmr, resolution 2.14Å ()
Ligands: , ,
Gene: PFI0320w (Plasmodium falciparum 3D7)
Activity: Arginase, with EC number 3.5.3.1


Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

Arginase

Introduction

Arginase is a 105 kD homotrimeric metallo-protein that catalysis the hydrolysis of arginine to ornithine and urea by means of a binuclear spin-coupled Mn2+ cluster in the active site5. Many organisms contain the enzyme arginase, for example Homo sapiens and Plasmodium falciparum, a parasite that causes cerebral malaria1. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals2. The two types of arginases found in mammalian, are arginase I (hAI) and arginases II (hAII)2. Arginase I is found predominantly in the liver, where it catalyzes the final cytosolic step of the urea cycle2. Arginases II is a mitochondrial enzyme that does not appear to function in the urea cycle and is more widely disturbed in numerous tissues, for example kidney, brains, skeletal muscle, mammary gland and penile corpus cavernosum2. Recent studies show that Plasmodium falciparum arginase (PFA) plays a role in systemic depletion of arginine levels, which in turn has been associated with human cerebral malaria pathogenesis5. In addition the arginase fold is part of the ureohydrolase superfamily, which also includes agmatinase, histone de-acetylase and acetylpolyamine amidohydrolase5.

Structure

Image:Arginine.jpg

Reference

[1] [2]

  1. ↑ Christianson DW. Arginase: structure, mechanism, and physiological role in male and female sexual arousal. Acc Chem Res. 2005 Mar;38(3):191-201. PMID:15766238 doi:10.1021/ar040183k
  2. ↑ Dowling DP, Ilies M, Olszewski KL, Portugal S, Mota MM, Llinas M, Christianson DW. Crystal Structure of Arginase from Plasmodium falciparum and Implications for l-Arginine Depletion in Malarial Infection . Biochemistry. 2010 Jun 9. PMID:20527960 doi:10.1021/bi100390z
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