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Sandbox GGC7
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== Structure and Function == | == Structure and Function == | ||
| - | + | <scene name='75/752270/Homotetramer_without_substrate/5'>Triphosphate isomerase</scene> of some thermophilic sepecies exist as a homotetramer due to the hard physiological environment, however, it exists as a dimer in solution. Each subunits of homotetramer forms TIM barrel in which 8α helices alternate with 8β sheets to form backbone of the protein. Hydrophobic chain form the core enzyme whereas hydrophilic found near the ends of the barrel where exposed to solvent. Each subunit has it own active site and only active as a dimer <scene name='75/752270/Dimer_with_substrates/1'>Dimer with substrate on each subunit</scene>. The <scene name='75/752270/Active_site_on_chain_a/1'>active site</scene> on chain A includes Gly 70, His 71, Asp 61, Leu 94, Arg 92, and His 59 | |
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== Disease == | == Disease == | ||
Revision as of 21:09, 30 April 2017
Triose phosphate isomerase
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References
- ↑ Park SH, Kim HS, Park MS, Moon S, Song MK, Park HS, Hahn H, Kim SJ, Bae E, Kim HJ, Han BW. Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum. PLoS One. 2015 Dec 28;10(12):e0145331. doi: 10.1371/journal.pone.0145331., eCollection 2015. PMID:26709515 doi:http://dx.doi.org/10.1371/journal.pone.0145331
