METAP2

Methionine aminopeptidase 2 is an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> that in humans is encoded by the METAP2 <a href="/facts/Gene/e1swwPY6">gene</a>.
Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a <a href="/facts/Cytosolic/VyXgygWm">cytosolic</a> metalloenzyme that catalyzes the hydrolytic removal of N-terminal <a href="/facts/Methionine/7neydPKo">methionine</a> residues from nascent <a href="/facts/Proteins/Jxmagu3E">proteins</a>.

<ul><li>peptide-methionine 
 
 
 
 ⇌
 
 
 {\displaystyle \rightleftharpoons }
 
 peptide + methionine</li></ul>
MetAP2 is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. Furthermore, MetAP2 is of particular interest because the enzyme plays a key role in <a href="/facts/Angiogenesis/h0HF9IUd">angiogenesis</a>, the growth of new blood vessels, which is necessary for the progression of diseases including solid tumor <a href="/facts/Cancers/PVW6n1D0">cancers</a> and <a href="/facts/Rheumatoid_arthritis/qFK4Xwv7">rheumatoid arthritis</a>. MetAP2 is also the target of two groups of anti-angiogenic natural products, ovalicin and <a href="/facts/Fumagillin/2Xf9EwDb">fumagillin</a>, and their analogs such as <a href="/facts/Beloranib/fhbcbpw5">beloranib</a>.

METAP2 open-in-new

METAP2