Sandbox Reserved 347: Difference between revisions
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==Biochemistry== | ==Biochemistry== | ||
[[Image:Man pic.png|thumb|left|Renin-Angiotensin-Aldosterone System]] | |||
Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref> | Renin is an aspartyl protease. <ref name= "Structure">PMID:2666611</ref> | ||
<Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' /> | <Structure load='2iko' size='500' frame='true' align='right' caption='Renin active site' scene='Sandbox_Reserved_347/Ligand/1' /> | ||
<scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene> | <scene name='Sandbox_Reserved_347/Ligand/1'>TextToBeDisplayed</scene> | ||
*Renin is found in the blood stream where it breaks down angiotensinogen, which is secreted from the liver, into angiotensin I. | |||
*Angiotensin I is then cleaved in the lungs by angiotensin converting enzymes (ACE) into angiotensin II. | |||
==Function== | ==Function== | ||
Revision as of 08:33, 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 a family called aspartic proteases which use an aspartate residue for the catalysis of their peptide substrate. X-ray diffraction experiments has shown there is a striking similarity among the structures of aspartyl proteases. [2] Renin consists of two homologous lobes each containing an aspartic acid. Between the lobes is the active site, which is catalyzed by the aspartic acid residues, a characteristic trait of all aspartate proteases. [1] Renin in its full mature form has a mass of 37 kDa and contains 340 amino acids.[3]
Biochemistry
Renin is an aspartyl protease. [4]
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- Renin is found in the blood stream where it breaks down angiotensinogen, which is secreted from the liver, into angiotensin I.
- Angiotensin I is then cleaved in the lungs by angiotensin converting enzymes (ACE) into angiotensin II.
Function
Renin plays a key role in the Renin-Angiotension sysmtem (RAS). It is essential in facilitating the conversion of angiotension to angiotension II, which is the active component of the system.[5] This system is responsible for the regulation of blood pressure, stimulation of the secretion of aldosterone which effects the salt and water balance.[5]
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References
- ↑ 1.0 1.1 Gradman AH, Kad R. Renin inhibition in hypertension. J Am Coll Cardiol. 2008 Feb 5;51(5):519-28. PMID:18237679 doi:10.1016/j.jacc.2007.10.027
- ↑ K Akahane, H Umeyama, S Nakagawa, I Moriguchi, S Hirose, K Iizuka, and K Murakami. "Three-dimensional structure of human renin". Hypertension. 1985;7:3-12
- ↑ Armstrong C. The vision of the pore. Science. 1998 Apr 3;280(5360):56-7. PMID:9556453
- ↑ Inagami T. Structure and function of renin. J Hypertens Suppl. 1989 Apr;7(2):S3-8. PMID:2666611
- ↑ 5.0 5.1 Reid IA, Morris BJ, Ganong WF. The renin-angiotensin system. Annu Rev Physiol. 1978;40:377-410. PMID:205167 doi:https://dx.doi.org/10.1146/annurev.ph.40.030178.002113
