Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP): Difference between revisions
New page: == Background == <StructureSection load='2x4d' size='340' side='right' caption='Crystal structure of human phospholysine phosphohistidine inorganic pyrophosphate phosphatase' scene=''> Pho... |
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== Background == | == Background == | ||
<StructureSection load='2x4d' size='340' side='right' caption='Crystal structure of human phospholysine phosphohistidine inorganic pyrophosphate phosphatase' scene=''> | <StructureSection load='2x4d' size='340' side='right' caption='Crystal structure of human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (PDB id [[2x4d]])' scene=''> | ||
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase <scene name='84/842888/Lhpp/1'>(LHPP)</scene> is a hydrolase enzyme which is known to be expressed in the liver, kidney, and at moderate levels in the brain<ref name=Gohla>DOI: 10.1016/j.bbamcr.2018.07.007</ref>. It belongs to the haloacid dehalogenase (HAD) superfamily of hydrolases with hydrolyze a wide variety of substrates<ref name=Seifried>DOI: 10.1111/j.1742-4658.2012.08633.x</ref>. LHPP, specifically, hydrolyzes both oxygen-phosphorous bonds in inorganic phosphate and nitrogen-phosphorous bonds in 6-phospholysine, 3-phosphohistidine, and imidodiphosphate. LHPP has been of particular interest to researchers in recent years due to its hypothesized function as a tumor suppressor and thus its role in various cancers<ref name=Hindupur>DOI: 10.1038/nature26140</ref>. | '''Phospholysine phosphohistidine inorganic pyrophosphate phosphatase''' <scene name='84/842888/Lhpp/1'>(LHPP)</scene> is a hydrolase enzyme which is known to be expressed in the liver, kidney, and at moderate levels in the brain<ref name=Gohla>DOI: 10.1016/j.bbamcr.2018.07.007</ref>. It belongs to the haloacid dehalogenase (HAD) superfamily of hydrolases with hydrolyze a wide variety of substrates<ref name=Seifried>DOI: 10.1111/j.1742-4658.2012.08633.x</ref>. LHPP, specifically, hydrolyzes both oxygen-phosphorous bonds in inorganic phosphate and nitrogen-phosphorous bonds in 6-phospholysine, 3-phosphohistidine, and imidodiphosphate. LHPP has been of particular interest to researchers in recent years due to its hypothesized function as a tumor suppressor and thus its role in various cancers<ref name=Hindupur>DOI: 10.1038/nature26140</ref>. | ||
== The HAD Superfamily == | == The HAD Superfamily == | ||