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| | <StructureSection load='1sm9' size='340' side='right'caption='[[1sm9]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1sm9' size='340' side='right'caption='[[1sm9]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sm9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10573 Atcc 10573]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SM9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SM9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sm9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Yamadazyma_tenuis Yamadazyma tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SM9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=1sm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sm9 OCA], [http://pdbe.org/1sm9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sm9 RCSB], [http://www.ebi.ac.uk/pdbsum/1sm9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sm9 ProSAT]</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=1sm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sm9 OCA], [https://pdbe.org/1sm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sm9 RCSB], [https://www.ebi.ac.uk/pdbsum/1sm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sm9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYL1_CANTE XYL1_CANTE] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aldehyde reductase]] | |
| - | [[Category: Atcc 10573]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kavanagh, K L]] | + | [[Category: Yamadazyma tenuis]] |
| - | [[Category: Leitgeb, S]] | + | [[Category: Kavanagh KL]] |
| - | [[Category: Nidetzky, B]] | + | [[Category: Leitgeb S]] |
| - | [[Category: Petschacher, B]] | + | [[Category: Nidetzky B]] |
| - | [[Category: Wilson, D K]] | + | [[Category: Petschacher B]] |
| - | [[Category: Akr2b5]]
| + | [[Category: Wilson DK]] |
| - | [[Category: Aldo-keto reductase]]
| + | |
| - | [[Category: Beta-alpha-barrel]]
| + | |
| - | [[Category: Coenzyme specificity]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Xylose metabolism]]
| + | |
| Structural highlights
Function
XYL1_CANTE Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
CtXR (xylose reductase from the yeast Candida tenuis; AKR2B5) can utilize NADPH or NADH as co-substrate for the reduction of D-xylose into xylitol, NADPH being preferred approx. 33-fold. X-ray structures of CtXR bound to NADP+ and NAD+ have revealed two different protein conformations capable of accommodating the presence or absence of the coenzyme 2'-phosphate group. Here we have used site-directed mutagenesis to replace interactions specific to the enzyme-NADP+ complex with the aim of engineering the co-substrate-dependent conformational switch towards improved NADH selectivity. Purified single-site mutants K274R (Lys274-->Arg), K274M, K274G, S275A, N276D, R280H and the double mutant K274R-N276D were characterized by steady-state kinetic analysis of enzymic D-xylose reductions with NADH and NADPH at 25 degrees C (pH 7.0). The results reveal between 2- and 193-fold increases in NADH versus NADPH selectivity in the mutants, compared with the wild-type, with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity. Catalytic reaction profile analysis demonstrated that all mutations produced parallel effects of similar magnitude on ground-state binding of coenzyme and transition state stabilization. The crystal structure of the double mutant showing the best improvement of coenzyme selectivity versus wild-type and exhibiting a 5-fold preference for NADH over NADPH was determined in a binary complex with NAD+ at 2.2 A resolution.
The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.,Petschacher B, Leitgeb S, Kavanagh KL, Wilson DK, Nidetzky B Biochem J. 2005 Jan 1;385(Pt 1):75-83. PMID:15320875[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Petschacher B, Leitgeb S, Kavanagh KL, Wilson DK, Nidetzky B. The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography. Biochem J. 2005 Jan 1;385(Pt 1):75-83. PMID:15320875 doi:10.1042/BJ20040363
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