User:Morgan Bertolino/Sandbox 1
From Proteopedia
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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' scene=''> | ||
| - | Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP)* is a hydrolase enzyme which is known to be expressed in the liver, kidney, and at moderate levels in the brain<ref>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>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 phospholysine*, 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>DOI: 10.1038/nature26140</ref>. | + | Phospholysine phosphohistidine inorganic pyrophosphate phosphatase **(LHPP)** is a hydrolase enzyme which is known to be expressed in the liver, kidney, and at moderate levels in the brain<ref>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>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 **phospholysine**, **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>DOI: 10.1038/nature26140</ref>. |
== The HAD Superfamily == | == The HAD Superfamily == | ||
| + | The haloacid dehalogenase superfamily contains over 79,000 unique sequences of enzymes and is largely made up of enzymes that catalyze phosphoryl transfer<ref>DOI: 10.1016/j.bbamcr.2018.07.007</ref>. **Phosphatases** (phosphate monoester hydrolases) make up the majority of these enzymes at ~79%, with many of the rest be **ATPases** (phosphoanhydride hydrolases)<ref>DOI: 10.1111/j.1742-4658.2012.08633.x</ref>. While many members of the enzyme family are found predominantly in prokaryotes, 183 human HAD enzymes have been identified, with at least 40 HAD-type phosphatases. This ancient group of enzymes has evolved over time to dephosphorylate a wide variety of substituents including carbohydrates, lipids, DNA, and various amino acid-phosphorylated proteins in humans, though many target small metabolites in intermediary metabolic reactions. These enzyme were originally thought to carry out simple regulatory tasks, but recent research has shown that some of these enzymes play roles in various genetic disorders<ref>DOI: 10.1016/j.bbamcr.2018.07.007</ref>. | ||
== HAD Phosphatases: Mechanism & Structure == | == HAD Phosphatases: Mechanism & Structure == | ||
Revision as of 03:38, 23 April 2020
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