Sandbox Reserved 489

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Renin
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Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1. Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site in a reduction-oxidation reaction with water to specifically cleave peptide substrates. Mature renin circulates in the blood and contains 406 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave [[Name of page|angiotensinogen]] to produce [[Name of page|angiotensin I]].

Revision as of 19:15, 13 April 2012

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Renin

Renin, also known as angiotensinogenase, is an aspartyl protease and belongs to the protein family peptidase A1. Aspartyl proteases are endopeptidases that typically use two aspartate residues in the active site in a reduction-oxidation reaction with water to specifically cleave peptide substrates. Mature renin circulates in the blood and contains 406 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave angiotensinogen to produce angiotensin I.

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