2npx

From Proteopedia

(Difference between revisions)

Revision as of 09:06, 23 February 2022

NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE

Structural highlights

2npx is a 1 chain structure with sequence from "enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Activity:	NADH peroxidase, with EC number 1.11.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NAPE_ENTFA] Peroxidase whose active site is a redox-active cysteine-sulfenic acid.

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

The structure of the complex between cofactor NADH and the enzyme NADH peroxidase from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been determined by crystal soaking, X-ray data collection, model building of NADH and refinement at 0.24-nm resolution based on the known enzyme structure [Stehle, T., Ahmed, S. A., Claiborne, A. & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344]. Apart from NADH, the catalytic center of the enzyme contains FAD and a cysteine that shuttles between thiolate and sulfenic acid states. Unfortunately, this cysteine was irreversibly oxidized to a cysteine sulfonic acid in the established enzyme structure. Based on the geometry of the catalytic center, we discuss the stabilization of the oxidation-sensitive sulfenic acid and propose a reaction mechanism.

NADH binding site and catalysis of NADH peroxidase.,Stehle T, Claiborne A, Schulz GE Eur J Biochem. 1993 Jan 15;211(1-2):221-6. PMID:8425532^[1]

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

References

↑ Stehle T, Claiborne A, Schulz GE. NADH binding site and catalysis of NADH peroxidase. Eur J Biochem. 1993 Jan 15;211(1-2):221-6. PMID:8425532

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2npx"

@@ Line 3: / Line 3: @@
 <StructureSection load='2npx' size='340' side='right'caption='[[2npx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2npx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2NPX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2npx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NPX FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2npx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2npx OCA], [http://pdbe.org/2npx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2npx RCSB], [http://www.ebi.ac.uk/pdbsum/2npx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2npx 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=2npx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2npx OCA], [https://pdbe.org/2npx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2npx RCSB], [https://www.ebi.ac.uk/pdbsum/2npx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2npx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NAPE_ENTFA NAPE_ENTFA]] Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
+[[https://www.uniprot.org/uniprot/NAPE_ENTFA NAPE_ENTFA]] Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2npx

From Proteopedia

Revision as of 09:06, 23 February 2022

NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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