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Sandbox Reserved 322

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<scene name='Sandbox_Reserved_322/Mn/4'>MN</scene>
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[[Image:Argine.jpg|thumb|alt=argine|
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==='''Reference'''===
==='''Reference'''===

Revision as of 03:00, 18 March 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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

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 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)

Structure


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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