Manganese peroxidase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_3m5q| PDB=3m5q | SIZE=400| SCENE= |right|CAPTION=Heme-containing glycosylated manganese peroxidase complex with Mn+2 ion, [[3m5q]] }}
+
{{STRUCTURE_3m5q| PDB=3m5q | SIZE=400| SCENE= |right|CAPTION=Heme-containing glycosylated manganese peroxidase complex with glycerol, Mn+2 (purple) and Ca+2 (green) ions [[3m5q]] }}
-
<!--
+
== Function ==
-
Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
+
'''Manganese peroxidase''' (MnP) catalyzes the conversion of Mn+2 to Mn+3 using hydrogen peroxide. MnP contains a heme group and needs calcium ion for activity. MnP is involved in lignin degradation. MnP is produced by wood-rotting fungi<ref>PMID:10712608</ref>.
-
Or use the four-green-boxes-button to insert scrollable text adjacent
+
-
to a Jmol applet. Check out the other buttons as well!
+
-
-->
+
-
'''Manganese peroxidase''' (MnP) catalyzes the conversion of Mn+2 to Mn+3 using hydrogen peroxide. MnP contains a heme group and needs calcium ion for activity. MnP is involved in lignin degradation. MnP is produced by wood-rotting fungi. Mn+3 in a chelated form is a powerful oxidizing agent which is able to mineralize lignin to CO2.
+
 +
== Relevance ==
 +
Mn+3 in a chelated form is a powerful oxidizing agent which is able to mineralize lignin to CO2.
 +
 +
== Structural highlights ==
 +
The Mn binding site of MnP contains the heme group which coordinates with the ion. The heme group is coordinated mostly by aromatic side chains<ref>PMID:20356630</ref>.
==3D structures of manganese peroxidase==
==3D structures of manganese peroxidase==
Line 20: Line 21:
[[4czo]], [[4czp]] – CsMnP + Mn<br />
[[4czo]], [[4czp]] – CsMnP + Mn<br />
[[4czq]], [[4czr]] – CsMnP + Cd<br />
[[4czq]], [[4czr]] – CsMnP + Cd<br />
-
 
+
== References ==
 +
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:32, 17 April 2016

Template:STRUCTURE 3m5q

Contents

Function

Manganese peroxidase (MnP) catalyzes the conversion of Mn+2 to Mn+3 using hydrogen peroxide. MnP contains a heme group and needs calcium ion for activity. MnP is involved in lignin degradation. MnP is produced by wood-rotting fungi[1].

Relevance

Mn+3 in a chelated form is a powerful oxidizing agent which is able to mineralize lignin to CO2.

Structural highlights

The Mn binding site of MnP contains the heme group which coordinates with the ion. The heme group is coordinated mostly by aromatic side chains[2].

3D structures of manganese peroxidase

Updated on 17-April-2016

1mnp, 1yyd, 1yyg, 1yzp, 3m8m – PcMnP – Phanerochaete chrysosporium
1mn1, 1mn2 – PcMnP (mutant)
1yzr – PcMnP + Sm
3m5q – PcMnP + Mn
4bm1, 4bm2, 4bm3, 4bm4 – MnP 4 – Pleurotus ostreatus
4czn – CsMnP – Ceriporiopsis subvermispora
4czo, 4czp – CsMnP + Mn
4czq, 4czr – CsMnP + Cd

References

  1. ↑ Youngs HL, Sundaramoorthy M, Gold MH. Effects of cadmium on manganese peroxidase competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur J Biochem. 2000 Mar;267(6):1761-9. PMID:10712608
  2. ↑ Sundaramoorthy M, Gold MH, Poulos TL. Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J Inorg Biochem. 2010 Jun;104(6):683-90. Epub 2010 Mar 6. PMID:20356630 doi:10.1016/j.jinorgbio.2010.02.011

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Manganese_peroxidase"
Personal tools