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[[Image:2dqx.jpg|left|200px]]
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{{STRUCTURE_2dqx|  PDB=2dqx  |  SCENE=  }}
'''mutant beta-amylase (W55R) from soy bean'''


==mutant beta-amylase (W55R) from soy bean==
<StructureSection load='2dqx' size='340' side='right'caption='[[2dqx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DQX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=2dqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dqx OCA], [https://pdbe.org/2dqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dqx RCSB], [https://www.ebi.ac.uk/pdbsum/2dqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dqx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q42795_SOYBN Q42795_SOYBN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/2dqx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dqx ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Beta-amylase (EC 3.2.1.2) is starch-hydrolyzing exo-type enzyme that can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. There is a well-known phenomenon called multiple or repetitive attack where the enzyme releases several maltose molecules in a single enzyme-substrate complex. In order to understand it further, we examined the beta-amylase-catalyzed reaction using maltooligosaccharides. The Monte Carlo method was applied for simulation of the beta-amylase-catalyzed reaction including the multiple attack mechanism. Through site-directed mutagenesis, we have successfully prepared a mutant enzyme which may be simulated as a multiple attack action reduced one with retaining significant hydrolytic activity. From the results of X-ray structure analysis of the mutant enzyme, it was clarified that one carboxyl residue plays a very important role in the multiple attack. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme.


==Overview==
Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase.,Ishikawa K, Nakatani H, Katsuya Y, Fukazawa C Biochemistry. 2007 Jan 23;46(3):792-8. PMID:17223700<ref>PMID:17223700</ref>
Beta-amylase (EC 3.2.1.2) is starch-hydrolyzing exo-type enzyme that can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. There is a well-known phenomenon called multiple or repetitive attack where the enzyme releases several maltose molecules in a single enzyme-substrate complex. In order to understand it further, we examined the beta-amylase-catalyzed reaction using maltooligosaccharides. The Monte Carlo method was applied for simulation of the beta-amylase-catalyzed reaction including the multiple attack mechanism. Through site-directed mutagenesis, we have successfully prepared a mutant enzyme which may be simulated as a multiple attack action reduced one with retaining significant hydrolytic activity. From the results of X-ray structure analysis of the mutant enzyme, it was clarified that one carboxyl residue plays a very important role in the multiple attack. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2DQX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQX OCA].
</div>
<div class="pdbe-citations 2dqx" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase., Ishikawa K, Nakatani H, Katsuya Y, Fukazawa C, Biochemistry. 2007 Jan 23;46(3):792-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17223700 17223700]
*[[Amylase 3D structures|Amylase 3D structures]]
[[Category: Beta-amylase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ishikawa, K.]]
[[Category: Ishikawa K]]
[[Category: Amylase mutant sliding soy bean]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 00:59:07 2008''

Latest revision as of 08:28, 25 October 2023

mutant beta-amylase (W55R) from soy bean

2dqx, resolution 2.20Å

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