Sandbox Reserved 347: Difference between revisions
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==Structure== | ==Structure== | ||
Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate. <ref name= ”hypertension” | Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate.<ref name=”hypertension”/> | ||
==Biochemistry== | ==Biochemistry== | ||
Revision as of 04:00, 4 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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| 2iko, resolution 1.90Å (default scene) | |||||||||||||
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| Ligands: | 7IG | ||||||||||||
| Gene: | REN (Homo sapiens) | ||||||||||||
| Activity: | Renin, with EC number 3.4.23.15 | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Introduction
Renin (pronounced /ˈriːnɨn/ REE-nin) is also known as angiotensinogenase, a monospecific enzyme that participates in the body's renin-angiotensin system (RAS). Renin is responsible for catalyzing the rate-limiting step in the synthesis of angiotensin II. Once renin and pro-renin bind to the pro-renin receptor, there is an increased enzymatic activity and additional physiological effects. [1]
Structure
Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate.[1]
Biochemistry
Renin is an aspartyl protease. [2]
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Function
Renin plays a key role in the Renin-Angiotension sysmtem (RAS). This system is responsible for the control of blood pressure and salt balances in mammals.
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