Identification of a non-purple tartrate-resistant acid phosphatase: An evolutionary link to Ser/Thr protein phosphatases?

Hadler, K.ieran S., Huber, Thomas, Cassady, A. Ian, Weber, Jane, Robinson, Jodie, Burrows, Allan, Kelly, Gregory, Guddat, Luke W., Hume, David A., Schenk, Gerhard and Flanagan, Jack U. (2008) Identification of a non-purple tartrate-resistant acid phosphatase: An evolutionary link to Ser/Thr protein phosphatases?. BMC Research Notes, 1 1-8. doi:10.1186/1756-0500-1-78


Author Hadler, K.ieran S.
Huber, Thomas
Cassady, A. Ian
Weber, Jane
Robinson, Jodie
Burrows, Allan
Kelly, Gregory
Guddat, Luke W.
Hume, David A.
Schenk, Gerhard
Flanagan, Jack U.
Title Identification of a non-purple tartrate-resistant acid phosphatase: An evolutionary link to Ser/Thr protein phosphatases?
Journal name BMC Research Notes   Check publisher's open access policy
ISSN 1756-0500
Publication date 2008-09-04
Year available 2008
Sub-type Article (original research)
DOI 10.1186/1756-0500-1-78
Open Access Status DOI
Volume 1
Start page 1
End page 8
Total pages 8
Place of publication London, U.K.
Publisher BioMed Central
Collection year 2009
Subject C1
060107 Enzymes
970106 Expanding Knowledge in the Biological Sciences
Formatted abstract
Background
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.

Findings
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.

Conclusion
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.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article number 78, pp. 1-8

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2009 Higher Education Research Data Collection
ERA 2012 Admin Only
School of Chemistry and Molecular Biosciences
 
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Created: Fri, 20 Feb 2009, 17:07:48 EST by Cody Mudgway on behalf of School of Chemistry & Molecular Biosciences