Sandbox Reserved 347: Difference between revisions
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{{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }} | {{STRUCTURE_2iko | PDB=2iko | SCENE=Sandbox_Reserved_347/Close_up/1 }} | ||
=Introduction= | =Introduction= | ||
<scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (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. <ref name= | <scene name='Sandbox_Reserved_347/Close_up/1'>Renin</scene> (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. <ref name="hypertension">doi:10.1016/j.jacc.2007.10.027 | ||
</ref> | </ref> | ||
==Structure== | ==Structure== | ||
Renin belongs in the family called aspartic proteases because they use an aspartate residue for catalysis of their peptide substrate.<ref name= | 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== | ||
