Pyridoxal Phosphatase Abstract: Difference between revisions
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Based on the provided PDB ID (2cfsA), evolutionary, structural and functional studies were carried out using the provided software with the aim of further characterizing 2cfsA. | Based on the provided PDB ID (2cfsA), evolutionary, structural and functional studies were carried out using the provided software with the aim of further characterizing 2cfsA. | ||
In the structural component of this paper, various databases such as DALI and PDBsum were utilized to identify potential structural homologies between | In the structural component of this paper, various databases such as DALI and PDBsum were utilized to identify potential structural homologies between 2cfsA and the generated protein hits. The practical aspect aside, theoretical research was conducted to provide a clearer insight on the structural properties of both the target and hit proteins. Based on the information provided, several inferences were made regarding the structure of 2cfsA. This information would undoubtedly be important in predicting the functions of the protein-of-interest. | ||
=====back to [[Pyridoxal Phosphatase]] main page====== | =====back to [[Pyridoxal Phosphatase]] main page====== | ||
Revision as of 05:09, 8 June 2008
Pyridoxal (pyridoxine, vitamin B6) Phosphatase, otherwise known as PLP (or PDXP, in certain cases), is defined as the metabolically active form of the water-soluble Vitamin B6. Its functions involve acting as a cofactor in many reactions of amino acid metabolism, gluconeogenesis and lipid metabolism.
Pyridoxal Phosphatase is an enzyme that catalyses the reaction:
Pyridoxal 5'-phosphate + H2O 
pyridoxal + phosphate
Based on the provided PDB ID (2cfsA), evolutionary, structural and functional studies were carried out using the provided software with the aim of further characterizing 2cfsA.
In the structural component of this paper, various databases such as DALI and PDBsum were utilized to identify potential structural homologies between 2cfsA and the generated protein hits. The practical aspect aside, theoretical research was conducted to provide a clearer insight on the structural properties of both the target and hit proteins. Based on the information provided, several inferences were made regarding the structure of 2cfsA. This information would undoubtedly be important in predicting the functions of the protein-of-interest.
