Sandbox Reserved 322

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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)

Revision as of 02:03, 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.
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  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
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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


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)

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