4mb1: Difference between revisions
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==The Structure of MalL mutant enzyme G202P from Bacillus subtilus== | |||
<StructureSection load='4mb1' size='340' side='right' caption='[[4mb1]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MB1 FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4maz|4maz]], [[4m8u|4m8u]], [[4m56|4m56]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malL, yvdL, BSU34560 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oligo-1,6-glucosidase Oligo-1,6-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.10 3.2.1.10] </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=4mb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mb1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mb1 RCSB], [http://www.ebi.ac.uk/pdbsum/4mb1 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/O16G1_BACSU O16G1_BACSU]] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose. | [[http://www.uniprot.org/uniprot/O16G1_BACSU O16G1_BACSU]] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This account persists despite many investigators noting that denaturation is insufficient to explain the decline in enzymatic rates above Topt. Here we show that it is the change in heat capacity associated with enzyme catalysis (DeltaCdouble daggerp) and its effect on the temperature dependence of DeltaGdouble dagger that determines the temperature dependence of enzyme activity. Through mutagenesis, we demonstrate that the Topt of an enzyme is correlated with DeltaCdouble daggerp and that changes to DeltaCdouble daggerp are sufficient to change Topt without affecting the catalytic rate. Furthermore, using X-ray crystallography and molecular dynamics simulations we reveal the molecular details underpinning these changes in DeltaCdouble daggerp. The influence of DeltaCdouble daggerp on enzymatic rates has implications for the temperature dependence of biological rates from enzymes to ecosystems. | |||
Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates.,Hobbs JK, Jiao W, Easter AD, Parker EJ, Schipper LA, Arcus VL ACS Chem Biol. 2013 Sep 17. PMID:24015933<ref>PMID:24015933</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacsu]] | [[Category: Bacsu]] | ||
[[Category: Oligo-1,6-glucosidase]] | [[Category: Oligo-1,6-glucosidase]] | ||
[[Category: Arcus, V L | [[Category: Arcus, V L]] | ||
[[Category: Easter, A D | [[Category: Easter, A D]] | ||
[[Category: Hobbs, J K | [[Category: Hobbs, J K]] | ||
[[Category: Jiao, W | [[Category: Jiao, W]] | ||
[[Category: Parker, E J | [[Category: Parker, E J]] | ||
[[Category: Schipper, L A | [[Category: Schipper, L A]] | ||
[[Category: Alpha glucosidase]] | [[Category: Alpha glucosidase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 11:42, 24 December 2014
The Structure of MalL mutant enzyme G202P from Bacillus subtilusThe Structure of MalL mutant enzyme G202P from Bacillus subtilus
Structural highlights
Function[O16G1_BACSU] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose. Publication Abstract from PubMedThe increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This account persists despite many investigators noting that denaturation is insufficient to explain the decline in enzymatic rates above Topt. Here we show that it is the change in heat capacity associated with enzyme catalysis (DeltaCdouble daggerp) and its effect on the temperature dependence of DeltaGdouble dagger that determines the temperature dependence of enzyme activity. Through mutagenesis, we demonstrate that the Topt of an enzyme is correlated with DeltaCdouble daggerp and that changes to DeltaCdouble daggerp are sufficient to change Topt without affecting the catalytic rate. Furthermore, using X-ray crystallography and molecular dynamics simulations we reveal the molecular details underpinning these changes in DeltaCdouble daggerp. The influence of DeltaCdouble daggerp on enzymatic rates has implications for the temperature dependence of biological rates from enzymes to ecosystems. Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates.,Hobbs JK, Jiao W, Easter AD, Parker EJ, Schipper LA, Arcus VL ACS Chem Biol. 2013 Sep 17. PMID:24015933[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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