|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5cgz' size='340' side='right'caption='[[5cgz]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5cgz' size='340' side='right'caption='[[5cgz]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cgz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Psepk Psepk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CGZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CGZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">galB, PP_2515 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160488 PSEPK])</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=5cgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgz OCA], [https://pdbe.org/5cgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cgz RCSB], [https://www.ebi.ac.uk/pdbsum/5cgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgz ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-oxalmesaconate_hydratase 4-oxalmesaconate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.83 4.2.1.83] </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=5cgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgz OCA], [http://pdbe.org/5cgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cgz RCSB], [http://www.ebi.ac.uk/pdbsum/5cgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GALB_PSEPK GALB_PSEPK]] Catalyzes the conversion of oxalomesaconic acid enol (OMAenol) to 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). Mediates the third step of gallate degradation pathway.<ref>PMID:21219457</ref> | + | [https://www.uniprot.org/uniprot/GALB_PSEPK GALB_PSEPK] Catalyzes the conversion of oxalomesaconic acid enol (OMAenol) to 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). Mediates the third step of gallate degradation pathway.<ref>PMID:21219457</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-oxalmesaconate hydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psepk]] | + | [[Category: Pseudomonas putida KT2440]] |
| - | [[Category: Brott, A S]] | + | [[Category: Brott AS]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Kimber MS]] |
| - | [[Category: Mazurkewich, S]] | + | [[Category: Mazurkewich S]] |
| - | [[Category: Seah, S Y.K]] | + | [[Category: Seah SYK]] |
| - | [[Category: Galb]]
| + | |
| - | [[Category: Gallic acid]]
| + | |
| - | [[Category: Helical hairpin]]
| + | |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Hydratase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Metalloenzyme]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
GALB_PSEPK Catalyzes the conversion of oxalomesaconic acid enol (OMAenol) to 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). Mediates the third step of gallate degradation pathway.[1]
Publication Abstract from PubMed
Bacterial catabolism of lignin and its breakdown products is of interest for applications in industrial processing of ligno-biomass. The gallate degradation pathway of Pseudomonas putida KT2440 requires a 4-carboxy-2-hydroxymuconate (CHM) hydratase (GalB) which has 12% sequence identity to a previously identified CHM hydratase (LigJ) from Sphingomonas sp. SYK-6. The structure of GalB was determined and found to be a member of the PIG-L N-acetyl glucosamine deacetylase family, and is structurally distinct from the amidohydrolase fold of LigJ. LigJ has the same stereo-specificity as GalB, providing an example of convergent evolution for catalytic conversion of a common metabolite in bacterial aromatic degradation pathways. Purified GalB contained bound Zn2+ cofactor; however the enzyme is capable using Fe2+ and Co2+ with similar efficiencies. The general base aspartate in the PIG-L deacetylases is an alanine in GalB; replacement of the alanine with aspartate decreased the GalB catalytic efficiency for CHM by 9.5 x 104 fold and the variant enzyme did not have any detectable hydrolase activity. Kinetic analyses and pH dependency studies of the wild-type and variant enzymes suggests roles for the Glu48 and His164 in the catalytic mechanism. Comparison to the PIG-L deacetylases has led to a proposed mechanism for GalB wherein Glu48 positions and activates the metal ligated water for the hydration reaction and His164 acts as a catalytic acid.
Structural and Kinetic Characterization of the 4-Carboxy-2-Hydroxymuconate Hydratase from the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas putida KT2440.,Mazurkewich S, Brott AS, Kimber MS, Seah SY J Biol Chem. 2016 Feb 11. pii: jbc.M115.682054. PMID:26867578[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nogales J, Canales A, Jimenez-Barbero J, Serra B, Pingarron JM, Garcia JL, Diaz E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol Microbiol. 2011 Jan;79(2):359-74. doi: 10.1111/j.1365-2958.2010.07448.x. Epub, 2010 Nov 16. PMID:21219457 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07448.x
- ↑ Mazurkewich S, Brott AS, Kimber MS, Seah SY. Structural and Kinetic Characterization of the 4-Carboxy-2-Hydroxymuconate Hydratase from the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas putida KT2440. J Biol Chem. 2016 Feb 11. pii: jbc.M115.682054. PMID:26867578 doi:http://dx.doi.org/10.1074/jbc.M115.682054
|
