Renin: Difference between revisions
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<StructureSection load='2ren' size='450' side='right' scene='' caption=' | <StructureSection load='2ren' size='450' side='right' scene='' caption='Glycosylated human renin (PDB code [[2ren]])'> | ||
{{Clear}} | {{Clear}} | ||
'''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. | ||