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EC 2.7.1.171

<html><head><title>EC 2.7.1.171</title><script type="text/javascript" src="/ruxitagentjs_ICA7NVfqrux_10303241106123517.js" data-dtconfig="rid=RID_1900294914|rpid=1260272980|domain=qmul.ac.uk|reportUrl=/rb_bf91175sbx|app=79d1ebe45b56f889|cuc=wwsfiovv|mel=100000|expw=1|featureHash=ICA7NVfqrux|dpvc=1|lastModification=1732098934976|tp=500,50,0|rdnt=1|uxrgce=1|agentUri=/ruxitagentjs_ICA7NVfqrux_10303241106123517.js"></script></head> <base href="https://iubmb.qmul.ac.uk/enzyme/EC2/7/1/171.html"> <body> <center><b>IUBMB Enzyme Nomenclature</b><p> <h1><b>EC 2.7.1.171</b></h1></center> <b>Accepted name:</b> protein-fructosamine 3-kinase<p> <b>Reaction:</b> ATP + [protein]-<i>N</i><small><sup>6</sup></small>-<small>D</small>-fructosyl-<small>L</small>-lysine = ADP + [protein]-<i>N</i><small><sup>6</sup></small>-(3-<i>O-</i>phospho-<small>D</small>-fructosyl)-<small>L</small>-lysine<p> <b>Other name(s):</b> FN3K; fructosamine 3-kinase<p> <b>Systematic name:</b> ATP:[protein]-<i>N</i><small><sup>6</sup></small>-<small>D</small>-fructosyl-<small>L</small>-lysine 3-phosphotransferase<p> <b>Comments:</b> Nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as [protein]-<i>N</i><small><sup>6</sup></small>-<small>D</small>-fructosyl-<small>L</small>-lysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins. The phosphorylation destablilizes the [protein]-<i>N</i><small><sup>6</sup></small>-<small>D</small>-fructosyl-<small>L</small>-lysine adduct and leads to its spontaneous decomposition. <i>cf.</i> <a href="172.html">EC 2.7.1.172</a>, protein-ribulosamine 3-kinase.<p> <b>Links to other databases:</b> <a href="http://www.brenda-enzymes.org/enzyme.php?ecno=2.7.1.171" target="new">BRENDA</a>, <a href="http://enzyme.expasy.org/EC/2.7.1.171" target="new">EXPASY</a>, <a href="http://www.genome.ad.jp/dbget-bin/www_bget?ec:2.7.1.171" target="new">KEGG</a>, <a target="new" href="http://www.metacyc.org/META/NEW-IMAGE?type=EC-NUMBER&object=EC-2.7.1.171">Metacyc</a>, CAS registry number: <p> <b>References:</b><p> 1. Szwergold, B.S., Howell, S. and Beisswenger, P.J. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity <i>in vivo. Diabetes</i> 50 (2001) 2139-2147. [PMID: <a href="http://www.ncbi.nlm.nih.gov/pubmed/11522682?dopt=Abstract" target="new">11522682</a>]<p> 2. Delpierre, G., Rider, M.H., Collard, F., Stroobant, V., Vanstapel, F., Santos, H. and Van Schaftingen, E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. <i>Diabetes</i> 49 (2000) 1627-1634. [PMID: <a href="http://www.ncbi.nlm.nih.gov/pubmed/11016445?dopt=Abstract" target="new">11016445</a>]<p> <center><small>[EC 2.7.1.171 created 2011]</small></center><p> <hr> Return to <a href="../1/">EC 2.7.1 home page</a><br> Return to <a href="../">EC 2.7 home page</a><br> Return to <a href="../../">EC 2 home page</a><br> Return to <a href="../../../">Enzymes home page</a><br> Return to <a href="../../../../">IUBMB Biochemical Nomenclature home page</a><p> </body></html>

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