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| | ==Human triosephosphate isomerase mutant V231M== | | ==Human triosephosphate isomerase mutant V231M== |
| - | <StructureSection load='6c2g' size='340' side='right' caption='[[6c2g]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='6c2g' size='340' side='right'caption='[[6c2g]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c2g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C2G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c2g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C2G FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPI1, TPI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6c2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c2g OCA], [https://pdbe.org/6c2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c2g RCSB], [https://www.ebi.ac.uk/pdbsum/6c2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c2g ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6c2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c2g OCA], [http://pdbe.org/6c2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c2g RCSB], [http://www.ebi.ac.uk/pdbsum/6c2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c2g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN]] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[http://omim.org/entry/190450 190450]]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection. | + | [https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN] Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:[https://omim.org/entry/190450 190450]. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection. |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6c2g" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6c2g" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Triose-phosphate isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Enriquez, F S]] | + | [[Category: Enriquez FS]] |
| - | [[Category: Torres, L A]] | + | [[Category: Torres LA]] |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Disease
TPIS_HUMAN Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:190450. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.
Function
TPIS_HUMAN
Publication Abstract from PubMed
Human triosephosphate isomerase (TIM) deficiency is a very rare disease, but there are several mutations reported to be causing the illness. In this work, we produced nine recombinant human triosephosphate isomerases which have the mutations reported to produce TIM deficiency. These enzymes were characterized biophysically and biochemically to determine their kinetic and stability parameters, and also to substitute TIM activity in supporting the growth of an Escherichia coli strain lacking the tim gene. Our results allowed us to rate the deleteriousness of the human TIM mutants based on the type and severity of the alterations observed, to classify four "unknown severity mutants" with altered residues in positions 62, 72, 122 and 154 and to explain in structural terms the mutation V231M, the most affected mutant from the kinetic point of view and the only homozygous mutation reported besides E104D.
Differential effects on enzyme stability and kinetic parameters of mutants related to human triosephosphate isomerase deficiency.,Cabrera N, Torres-Larios A, Garcia-Torres I, Enriquez-Flores S, Perez-Montfort R Biochim Biophys Acta. 2018 Mar 20;1862(6):1401-1409. doi:, 10.1016/j.bbagen.2018.03.019. PMID:29571745[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cabrera N, Torres-Larios A, Garcia-Torres I, Enriquez-Flores S, Perez-Montfort R. Differential effects on enzyme stability and kinetic parameters of mutants related to human triosephosphate isomerase deficiency. Biochim Biophys Acta. 2018 Mar 20;1862(6):1401-1409. doi:, 10.1016/j.bbagen.2018.03.019. PMID:29571745 doi:http://dx.doi.org/10.1016/j.bbagen.2018.03.019
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