Sandbox Reserved 1094: Difference between revisions
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The most common mutations in the amino acids sequence found that induce a loss of catalytic activity are a substitution of the bold amino acids by another one<ref>PMID: 11106479</ref>: | The most common mutations in the amino acids sequence found that induce a loss of catalytic activity are a substitution of the bold amino acids by another one<ref>PMID: 11106479</ref>: | ||
MVSEIKTLVT FFGG <font color='turquoise'>'''T'''</font> GDLAK R <font color='turquoise'>'''TK'''</font> LYPSVFNL YKKGYLQKHF AIVGTA <font color='turquoise'>'''RQ'''</font> AL NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEK <font color=' | MVSEIKTLVT FFGG <font color='turquoise'>'''T'''</font> GDLAK R <font color='turquoise'>'''TK'''</font> LYPSVFNL YKKGYLQKHF AIVGTA <font color='turquoise'>'''RQ'''</font> AL NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEK <font color='turquoise'>'''P'''</font> FGTSYDTAAE LQNDLENAFD DNQLFRI <font color='turquoise'>'''DHY'''</font> LG <font color='turquoise'>'''K'''</font> EMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN <font color='turquoise'>'''H''' </font> TMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAA <font color='turquoise'> '''K''' </font> QTRVDI VFKAGTFNFG SEQEAQEAVL SIII <font color='turquoise'> '''D''' </font> PKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEP <font color='turquoise'> '''Y''' </font> ERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG. | ||
This sequence being the normal protein sequence found in L. ''mesenteroides''. | This sequence being the normal protein sequence found in L. ''mesenteroides''. | ||
== Structural highlights == | == Structural highlights == | ||
Glucose-6-Phosphate Dehydrogenase is formed of a homodimer, so a dimer of two identical [https://en.wikipedia.org/wiki/Protein_subunit subunit]. Each <scene name='82/829347/Monomerg6pd/1'>monomer</scene> is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/5'>1 red and 1 green</scene>. | '''Glucose-6-Phosphate Dehydrogenase''' is formed of a homodimer, so a dimer of two identical [https://en.wikipedia.org/wiki/Protein_subunit subunit]. Each <scene name='82/829347/Monomerg6pd/1'>monomer</scene> is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/5'>1 red and 1 green</scene>. | ||
Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to | Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to '''G6PD''', and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.<ref name="struc">PMID: 7881907</ref> | ||
