Glycoside Hydrolase Family 82 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:18:46Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: /* Three-dimensional structures */ changed coloring of figure legend

2011-06-20T07:35:39Z

Three-dimensional structures: changed coloring of figure legend

Spencer Williams at 02:50, 27 May 2011

2011-05-27T02:50:40Z

Spencer Williams at 02:50, 27 May 2011

2011-05-27T02:50:20Z

Harry Brumer: /* Three-dimensional structures */

2011-05-09T14:36:35Z

Three-dimensional structures

Harry Brumer at 07:50, 9 May 2011

2011-05-09T07:50:33Z

Harry Brumer at 07:49, 9 May 2011

2011-05-09T07:49:18Z

Harry Brumer: updated CAZy DB link

2011-05-09T07:46:46Z

updated CAZy DB link

Etienne Rebuffet at 12:09, 6 May 2011

2011-05-06T12:09:42Z

Etienne Rebuffet at 12:07, 6 May 2011

2011-05-06T12:07:50Z

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 <!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]s: ^^^Mirjam Czjzek^^^, ^^^Gurvan Michel^^^, and ^^^Etienne Rebuffet^^^
+* [[Author]]s: [[User:Mirjam Czjzek|Mirjam Czjzek]], [[User:Gurvan Michel|Gurvan Michel]], and [[User:Etienne Rebuffet|Etienne Rebuffet]]
-* [[Responsible Curator]]:  ^^^Mirjam Czjzek^^^
+* [[Responsible Curator]]:  [[User:Mirjam Czjzek|Mirjam Czjzek]]
 ----

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 == Three-dimensional structures ==
-[[Image:gh82_domA.gif|'''Figure 1:''' Movement of domain A induced by substrate binding. <span style="color:#0000ff"> The &beta;-helix is in blue </span>, <span style="color:#ff0000"> the domain A is in red </span> and <span style="color:#00ff00"> the domain B is in green </span>.|frame|right]]
+[[Image:gh82_domA.gif|'''Figure 1:''' Movement of domain A induced by substrate binding.  The &beta;-helix is in <span style="color:#0000ff">blue</span>, domain A is in <span style="color:#ff0000">red</span> and domain B is in <span style="color:#00ff00">green</span>.|frame|right]]
 A crystal structure has only been determined for the iota-carrageenase from ''A. fortis'' and the protein folds into a right-handed parallel β-helix of 10 complete turns with two additional C-terminal domains (A and B) <cite>Michel2001</cite>. The crystal structure of a product complex has shed light on the existence of domain movement of domain A that is closed around the oligo-carrageenan in the complexed form and open in the uncomplexed enzyme ('''Figure 1''') <cite>Michel2003</cite>. Recent discovery of shorter sequences indicates the existence of enzymes devoid of the C-terminal domain A or both domains A and B <cite>Rebuffet2010</cite>.

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 ;First sequence identification and family creation: iota-carrageenase sequences have been first reported for enzymes from ''A. fortis'' and ''Z. galactanivorans'' <cite>Barbeyron2000</cite>.
 ;First sterochemistry determination: GH82 enzymes are inverting as shown by NMR <cite>Barbeyron2000</cite>.
-;First general acid residue identification: Glu245 in the iota-carrageenase from ''Alteromonas fortis'' by site-directed mutagenesis and kinetic analysis <cite>Rebuffet2010</cite>
+;First [[general acid]] residue identification: Glu245 in the iota-carrageenase from ''Alteromonas fortis'' by site-directed mutagenesis and kinetic analysis <cite>Rebuffet2010</cite>
-;First general base residue identification: Asp247 in the iota-carrageenase from ''Alteromonas fortis'' by site-directed mutagenesis and kinetic analysis <cite>Rebuffet2010</cite>.
+;First [[general base]] residue identification: Asp247 in the iota-carrageenase from ''Alteromonas fortis'' by site-directed mutagenesis and kinetic analysis <cite>Rebuffet2010</cite>.
 ;First 3-D structure: iota-carrageenase from ''A. fortis'' <cite>Michel2001</cite>. The structure belongs to the &beta;-helix fold ([{{PDBlink}}1h80 PDB 1h80] and [{{PDBlink}}1ktw PDB 1ktw]).

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 == Substrate specificities ==
-At the moment, all characterised members of [[glycoside hydrolase]] family 82 enzymes cleave the &beta;-1,4 galactosidic bond of the marine algal polysaccharide iota-carrageenan <cite>Barbeyron2000 Rebuffet2010 Hatada2010</cite> yielding products of the neocarrabiose series.
+All characterised members of [[glycoside hydrolase]] family 82 enzymes cleave the &beta;-1,4 galactosidic bond of the marine algal polysaccharide iota-carrageenan <cite>Barbeyron2000 Rebuffet2010 Hatada2010</cite> yielding products of the neocarrabiose series.
 == Kinetics and Mechanism ==
-Family 82 enzymes are [[inverting]] enzymes, as first shown by NMR <cite>Barbeyron2000</cite> on the iota-carrageenase from ''Alteromonas fortis''. The reaction seems to involve a chloride ion which through the Glu222 participated in the polarisation of the catalytic water molecule <cite>Rebuffet2010</cite>.
+Family 82 enzymes operate with an [[inverting]] mechanism, as first shown by NMR <cite>Barbeyron2000</cite> on the iota-carrageenase from ''Alteromonas fortis''. The reaction seems to involve a chloride ion which through the Glu222 participated in the polarisation of the catalytic water molecule <cite>Rebuffet2010</cite>.
 == Catalytic Residues ==
-From structural analysis the catalytic residues have been predicted to be two out of the three candidate amino acids Glu245, Asp247 or Glu310 in the ''A. fortis'' iota-carrageenase <cite>Michel2001</cite>. A study in 2010, which utilized site directed mutagenesis, has confirmed that Glu245 plays the role of the [[general acid]] residue in this [[inverting]] enzyme, while Asp247 is the [[general base]] activating the nucleophilic water molecule  <cite>Rebuffet2010</cite>. However, intriguingly the position of equivalent residues to Asp247 in other iota-carrageenase sequences are not strictly conserved <cite>Rebuffet2010 Hatada2010</cite>.
+From structural analysis the catalytic residues have been predicted to be two out of the three candidate amino acids Glu245, Asp247 or Glu310 in the ''A. fortis'' iota-carrageenase <cite>Michel2001</cite>. A study in 2010, which utilized site directed mutagenesis, has confirmed that Glu245 plays the role of the [[general acid]] residue in this [[inverting]] enzyme, and Asp247 is the [[general base]] activating the nucleophilic water molecule  <cite>Rebuffet2010</cite>. However, intriguingly the position of equivalent residues to Asp247 in other iota-carrageenase sequences are not strictly conserved <cite>Rebuffet2010 Hatada2010</cite>.
 == Three-dimensional structures ==

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 == Three-dimensional structures ==
 [[Image:gh82_domA.gif|'''Figure 1:''' Movement of domain A induced by substrate binding. <span style="color:#0000ff"> The &beta;-helix is in blue </span>, <span style="color:#ff0000"> the domain A is in red </span> and <span style="color:#00ff00"> the domain B is in green </span>.|frame|right]]
-A crystal structure has only been determined for the iota-carrageenase from ''A. fortis'' and the protein folds into a right-handed parallel β-helix of 10 complete turns with two additional C-terminal domains (A and B) <cite>Michel2001</cite>. The crystal structure of a product complex has shed light on the existence of domain movement of domain A that is closed around the oligo-carrageenan in the complexed form and open in the uncomplexed enzyme ('''Figure 1''') <cite>Michel2003</cite>. Recent discovering of shorter sequences shows the existence of enzymes devoid of the C-terminal domain A or both domains A and B <cite>Rebuffet2010</cite>.
+A crystal structure has only been determined for the iota-carrageenase from ''A. fortis'' and the protein folds into a right-handed parallel β-helix of 10 complete turns with two additional C-terminal domains (A and B) <cite>Michel2001</cite>. The crystal structure of a product complex has shed light on the existence of domain movement of domain A that is closed around the oligo-carrageenan in the complexed form and open in the uncomplexed enzyme ('''Figure 1''') <cite>Michel2003</cite>. Recent discovery of shorter sequences indicates the existence of enzymes devoid of the C-terminal domain A or both domains A and B <cite>Rebuffet2010</cite>.
 == Family Firsts ==

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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH82.html
+| colspan="2" |{{CAZyDBlink}}GH82.html
 |}
 </div>