ATP Phosphoribosyl Transferase: Difference between revisions
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<applet load='1z7n' size='350' frame='true' align='right' caption='ATP phosphoribosyltransferase regulatory subunit tetramer (grey, green, pink, yellow) with ATP phosphoribosyltransferase (magenta, cyan, red, gold) complex with substrate α-phosphoribosylpyrophosphoric acid (PRPP) and phosphate, [[1z7n]]' /> | |||
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=='''HisG – ATP Phosphoribosyl Transferase'''== | =='''HisG – ATP Phosphoribosyl Transferase'''== | ||
ATP Phosphoribosyl transferase (ATP-PRTase) (EC 2.4.2.17), also called HisG, belongs to the enzyme super family, phosphoribosyl transferases (PRTases) and the glycosyltransferases family. It catalyzes the reversible condensation of 5-phosphoribosyl-α-1-pyrophosphate (PRPP) with ATP, yielding N’-5’-phosphoribosyl-ATP (PR-ATP) and inorganic pyrophosphate (PPi). | '''ATP Phosphoribosyl transferase''' (ATP-PRTase) (EC 2.4.2.17), also called '''HisG''', belongs to the enzyme super family, phosphoribosyl transferases (PRTases) and the glycosyltransferases family. It catalyzes the reversible condensation of 5-phosphoribosyl-α-1-pyrophosphate (PRPP) with ATP, yielding N’-5’-phosphoribosyl-ATP (PR-ATP) and inorganic pyrophosphate (PPi). | ||
5-phosphoribosyl-α-1-pyrophosphate + ATP = N’-5’-phosphoribosyl-ATP + pyrophosphate. | 5-phosphoribosyl-α-1-pyrophosphate + ATP = N’-5’-phosphoribosyl-ATP + pyrophosphate. | ||
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and ATP-PRTase belongs to the type IV class, a unique fold from all others’;. The presence of four different classes of PRTases points to the fact that these enzyme evolved from different ancestors to perform similar functions, a case of convergent evolution. PRTases possess a conserved P-loop for binding the ribose-5’-phosphate group of PRPP <ref> 4. Sangita C Sinha and Janet L Smith, (2001), The PRT protein family, Current Opinion in Structural Biology ,'''11''' ,733-739 </ref>. | and ATP-PRTase belongs to the type IV class, a unique fold from all others’;. The presence of four different classes of PRTases points to the fact that these enzyme evolved from different ancestors to perform similar functions, a case of convergent evolution. PRTases possess a conserved P-loop for binding the ribose-5’-phosphate group of PRPP <ref> 4. Sangita C Sinha and Janet L Smith, (2001), The PRT protein family, Current Opinion in Structural Biology ,'''11''' ,733-739 </ref>. | ||
<scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_i/1'>TYPE I FOLD</scene> | <scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_i/1'>TYPE I FOLD</scene>, | ||
<scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_ii/1'>TYPE II FOLD</scene> | <scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_ii/1'>TYPE II FOLD</scene>, | ||
<scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_iii/1'>TYPE III FOLD</scene> | <scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_iii/1'>TYPE III FOLD</scene>, | ||
<scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_iv/1'>TYPE IV FOLD</scene> | <scene name='User:Lawrence_Sheringham_Borketey/Sandbox_1/Type_iv/1'>TYPE IV FOLD</scene> | ||
'''Role of HisG in Histidine biosynthetic Pathway''' | =='''Role of HisG in Histidine biosynthetic Pathway'''== | ||
The reaction catalyzed by ATP-PRTase is the first reaction in the histidine biosynthetic pathway. The reaction also leads to the formation of intermediates involved in purine, pyrimidine and tryptophan biosynthesis. ATP and PRPP are also involved in energy metabolism. Because of the key role of ATP-PRTase in the histidine biosynthetic pathway, a unique pathway for bacteria, plants and fungi but not humans, it is a potential drug target for antimicrobials <ref> . Yoonsang Cho, Thomas R. Ioerger and James C. Sacchettini; (2008), Discovery of Novel Nitrobenzothiazole Inhibitors for ''Mycobacterium tuberculosis'' ATP Phosphoribosyl Transferase (HisG) through Virtual Screening, J. Med. Chem. '''51''', 5984–5992. </ref> | The reaction catalyzed by ATP-PRTase is the first reaction in the histidine biosynthetic pathway. The reaction also leads to the formation of intermediates involved in purine, pyrimidine and tryptophan biosynthesis. ATP and PRPP are also involved in energy metabolism. Because of the key role of ATP-PRTase in the histidine biosynthetic pathway, a unique pathway for bacteria, plants and fungi but not humans, it is a potential drug target for antimicrobials <ref> . Yoonsang Cho, Thomas R. Ioerger and James C. Sacchettini; (2008), Discovery of Novel Nitrobenzothiazole Inhibitors for ''Mycobacterium tuberculosis'' ATP Phosphoribosyl Transferase (HisG) through Virtual Screening, J. Med. Chem. '''51''', 5984–5992. </ref> | ||
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'''Types of ATP-PRTases''' | =='''Types of ATP-PRTases'''== | ||
Two forms of ATP-PRTase have been identified: | Two forms of ATP-PRTase have been identified: | ||
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==3D structures of ATP phosphoribosyl transferase== | |||
[[ATP phosphoribosyl transferase 3D structures]] | |||
==Additional Resources== | |||
For additional information, see: [[Amino Acid Synthesis & Metabolism]] | |||
For additional information, see: [[ | |||
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<references /> | <references /> | ||
[[Category:Topic Page]] | |||