Sandbox Reserved 489: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
<span style="font-size:200%">Renin</span> | <span style="font-size:200%">Renin</span> | ||
---- | ---- | ||
[[Image: | [[Image:ColoredRenin.png|thumb|530px|alt=text|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 to specifically cleave peptide substrates using an acid-base hydrolysis mechanism. Mature renin circulates in the blood stream and contains 340 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave angiotensinogen to produce angiotensin I. | 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 to specifically cleave peptide substrates using an acid-base hydrolysis mechanism. Mature renin circulates in the blood stream and contains 340 amino acid residues and has a mass of approximately 37 kDa. The function of renin is to cleave angiotensinogen to produce angiotensin I. | ||
