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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 Mn<sup>2+</sup> cluster in the active site<ref name="a">PMID: 19456858 </ref>. Many organisms contain the enzyme arginase, for example Homo sapiens and Plasmodium falciparum, a parasite that causes cerebral malaria<ref name="b">PMID: 20527960 </ref>. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals<ref name="c">PMID: 15766238 </ref>.
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 Mn<sup>2+</sup> cluster in the active site<ref name="a">PMID: 19456858 </ref>. Many organisms contain the enzyme arginase, for example Homo sapiens and Plasmodium falciparum, a parasite that causes cerebral malaria<ref name="b">PMID: 20527960 </ref>. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals<ref name="c">PMID: 15766238 </ref>.
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The two types of arginases found in mammalian, are arginase I (hAI) and arginases II (hAII)3. Arginase I is found predominantly in the liver, where it catalyzes the final cytosolic step of the urea cycle3. 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 cavernosum3. 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 pathogenesis1. In addition the arginase fold is part of the ureohydrolase superfamily, which also includes agmatinase, histone de-acetylase and acetylpolyamine amidohydrolase1.
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The two types of arginases found in mammalian, are arginase I (hAI) and arginases II (hAII)<ref name="c"/>. Arginase I is found predominantly in the liver, where it catalyzes the final cytosolic step of the urea cycle3. 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 cavernosum3. 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 pathogenesis1. In addition the arginase fold is part of the ureohydrolase superfamily, which also includes agmatinase, histone de-acetylase and acetylpolyamine amidohydrolase1.
==='''Structure'''===
==='''Structure'''===
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Revision as of 04:40, 2 April 2011

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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 site[1]. Many organisms contain the enzyme arginase, for example Homo sapiens and Plasmodium falciparum, a parasite that causes cerebral malaria[2]. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals[3]. The two types of arginases found in mammalian, are arginase I (hAI) and arginases II (hAII)[3]. Arginase I is found predominantly in the liver, where it catalyzes the final cytosolic step of the urea cycle3. 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 cavernosum3. 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 pathogenesis1. In addition the arginase fold is part of the ureohydrolase superfamily, which also includes agmatinase, histone de-acetylase and acetylpolyamine amidohydrolase1.

Structure

Image:Arginine.jpg

Reference

[4] [5] [6] [7]

  1. ↑ Wells GA, Muller IB, Wrenger C, Louw AI. The activity of Plasmodium falciparum arginase is mediated by a novel inter-monomer salt-bridge between Glu295-Arg404. FEBS J. 2009 Jul;276(13):3517-30. Epub 2009 May 18. PMID:19456858 doi:10.1111/j.1742-4658.2009.07073.x
  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
  3. ↑ 3.0 3.1 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
  4. ↑ Wells GA, Muller IB, Wrenger C, Louw AI. The activity of Plasmodium falciparum arginase is mediated by a novel inter-monomer salt-bridge between Glu295-Arg404. FEBS J. 2009 Jul;276(13):3517-30. Epub 2009 May 18. PMID:19456858 doi:10.1111/j.1742-4658.2009.07073.x
  5. ↑ 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
  6. ↑ 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
  7. ↑ Kanyo ZF, Scolnick LR, Ash DE, Christianson DW. Structure of a unique binuclear manganese cluster in arginase. Nature. 1996 Oct 10;383(6600):554-7. PMID:8849731 doi:10.1038/383554a0
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