Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?
<p>Abstract</p> <p>Background</p> <p>Tartrate-resistant acid phosphatases (TRAcPs), also known as purple acid phosphatases (PAPs), are a family of binuclear metallohydrolases that have been identified in plants, animals and fungi. The human enzyme is a major histochemic...
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| Format: | Article |
| Language: | English |
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BMC
2008-09-01
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| Series: | BMC Research Notes |
| Online Access: | http://www.biomedcentral.com/1756-0500/1/2 |
| _version_ | 1818021736258469888 |
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| author | Hume David A Guddat Luke W Kelly Gregory Burrows Allan Robinson Jodie Weber Jane Cassady A Ian Huber Thomas Hadler Kieran S Schenk Gerhard Flanagan Jack U |
| author_facet | Hume David A Guddat Luke W Kelly Gregory Burrows Allan Robinson Jodie Weber Jane Cassady A Ian Huber Thomas Hadler Kieran S Schenk Gerhard Flanagan Jack U |
| author_sort | Hume David A |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Tartrate-resistant acid phosphatases (TRAcPs), also known as purple acid phosphatases (PAPs), are a family of binuclear metallohydrolases that have been identified in plants, animals and fungi. The human enzyme is a major histochemical marker for the diagnosis of bone-related diseases. TRAcPs can occur as a small form possessing only the ~35 kDa catalytic domain, or a larger ~55 kDa form possessing both a catalytic domain and an additional N-terminal domain of unknown function. Due to its role in bone resorption the 35 kDa TRAcP has become a promising target for the development of anti-osteoporotic chemotherapeutics.</p> <p>Findings</p> <p>A new human gene product encoding a metallohydrolase distantly related to the ~55 kDa plant TRAcP was identified and characterised. The gene product is found in a number of animal species, and is present in all tissues sampled by the RIKEN mouse transcriptome project. Construction of a homology model illustrated that six of the seven metal-coordinating ligands in the active site are identical to that observed in the TRAcP family. However, the tyrosine ligand associated with the charge transfer transition and purple color of TRAcPs is replaced by a histidine.</p> <p>Conlusion</p> <p>The gene product identified here may represent an evolutionary link between TRAcPs and Ser/Thr protein phosphatases. Its biological function is currently unknown but is unlikely to be associated with bone metabolism.</p> |
| first_indexed | 2024-04-14T08:22:59Z |
| format | Article |
| id | doaj.art-3596ca8544914cc2b1088790b1c273c6 |
| institution | Directory Open Access Journal |
| issn | 1756-0500 |
| language | English |
| last_indexed | 2024-04-14T08:22:59Z |
| publishDate | 2008-09-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Research Notes |
| spelling | doaj.art-3596ca8544914cc2b1088790b1c273c62022-12-22T02:04:10ZengBMCBMC Research Notes1756-05002008-09-01117810.1186/1756-0500-1-78Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?Hume David AGuddat Luke WKelly GregoryBurrows AllanRobinson JodieWeber JaneCassady A IanHuber ThomasHadler Kieran SSchenk GerhardFlanagan Jack U<p>Abstract</p> <p>Background</p> <p>Tartrate-resistant acid phosphatases (TRAcPs), also known as purple acid phosphatases (PAPs), are a family of binuclear metallohydrolases that have been identified in plants, animals and fungi. The human enzyme is a major histochemical marker for the diagnosis of bone-related diseases. TRAcPs can occur as a small form possessing only the ~35 kDa catalytic domain, or a larger ~55 kDa form possessing both a catalytic domain and an additional N-terminal domain of unknown function. Due to its role in bone resorption the 35 kDa TRAcP has become a promising target for the development of anti-osteoporotic chemotherapeutics.</p> <p>Findings</p> <p>A new human gene product encoding a metallohydrolase distantly related to the ~55 kDa plant TRAcP was identified and characterised. The gene product is found in a number of animal species, and is present in all tissues sampled by the RIKEN mouse transcriptome project. Construction of a homology model illustrated that six of the seven metal-coordinating ligands in the active site are identical to that observed in the TRAcP family. However, the tyrosine ligand associated with the charge transfer transition and purple color of TRAcPs is replaced by a histidine.</p> <p>Conlusion</p> <p>The gene product identified here may represent an evolutionary link between TRAcPs and Ser/Thr protein phosphatases. Its biological function is currently unknown but is unlikely to be associated with bone metabolism.</p>http://www.biomedcentral.com/1756-0500/1/2 |
| spellingShingle | Hume David A Guddat Luke W Kelly Gregory Burrows Allan Robinson Jodie Weber Jane Cassady A Ian Huber Thomas Hadler Kieran S Schenk Gerhard Flanagan Jack U Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases? BMC Research Notes |
| title | Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases? |
| title_full | Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases? |
| title_fullStr | Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases? |
| title_full_unstemmed | Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases? |
| title_short | Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases? |
| title_sort | identification of a non purple tartrate resistant acid phosphatase an evolutionary link to ser thr protein phosphatases |
| url | http://www.biomedcentral.com/1756-0500/1/2 |
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