1m9h

From Proteopedia

(Difference between revisions)

Revision as of 06:54, 18 August 2021

Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor

Structural highlights

1m9h is a 1 chain structure with sequence from Corsp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1a80
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DKGA_CORSC] Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.

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

Corynebacterium 2,5-Diketo-D-gluconic acid reductase (2,5-DKGR) catalyzes the reduction of 2,5-diketo-D-gluconic acid (2,5-DKG) to 2-Keto-L-gulonic acid (2-KLG). 2-KLG is an immediate precursor to L-ascorbic acid (vitamin C), and 2,5-DKGR is, therefore, an important enzyme in a novel industrial method for the production of vitamin C. 2,5-DKGR, as with most other members of the aldo-keto reductase (AKR) superfamily, exhibits a preference for NADPH compared to NADH as a cofactor in the stereo-specific reduction of substrate. The application of 2,5-DKGR in the industrial production of vitamin C would be greatly enhanced if NADH could be efficiently utilized as a cofactor. A mutant form of 2,5-DKGR has previously been identified that exhibits two orders of magnitude higher activity with NADH in comparison to the wild-type enzyme, while retaining a high level of activity with NADPH. We report here an X-ray crystal structure of the holo form of this mutant in complex with NADH cofactor, as well as thermodynamic stability data. By comparing the results to our previously reported X-ray structure of the holo form of wild-type 2,5-DKGR in complex with NADPH, the structural basis of the differential NAD(P)H selectivity of wild-type and mutant 2,5-DKGR enzymes has been identified.

Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase.,Sanli G, Banta S, Anderson S, Blaber M Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. PMID:14718658^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sanli G, Banta S, Anderson S, Blaber M. Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. PMID:14718658 doi:10.1110/ps.03450704

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m9h"

@@ Line 3: / Line 3: @@
 <StructureSection load='1m9h' size='340' side='right'caption='[[1m9h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m9h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corsp Corsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M9H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1m9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corsp Corsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M9H 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a80|1a80]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a80|1a80]]</div></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=1m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9h OCA], [http://pdbe.org/1m9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m9h RCSB], [http://www.ebi.ac.uk/pdbsum/1m9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9h 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=1m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9h OCA], [https://pdbe.org/1m9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m9h RCSB], [https://www.ebi.ac.uk/pdbsum/1m9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DKGA_CORSC DKGA_CORSC]] Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.
+[[https://www.uniprot.org/uniprot/DKGA_CORSC DKGA_CORSC]] Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 1m9h" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Group:SMART:2010 Pingry SMART Team Models|SMART:2010 Pingry SMART Team Models]]
 == References ==
 <references/>

1m9h

From Proteopedia

Revision as of 06:54, 18 August 2021

Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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