Heme oxygenase: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, Michal Harel, Alexander Berchansky

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-{{STRUCTURE_2dy5|  PDB=2dy5  | SIZE=400| SCENE= |right|   CAPTION=Rat heme oxygenase complex with imidazole derivative and Cl- ion (green), [[2dy5]] }}
+<StructureSection load='2dy5' size='350' side='right' caption='Rat heme oxygenase complex with imidazole derivative and Cl- ion (green) (PDB entry [[2dy5]])' scene=''>
 __TOC__
 ==='''General Information'''===
 ----
-'''Heme Oxygenase''' (HO) is a member of the Hemoprotein family and catalyzes the Oxygen-dependent cleavage of the porphyrin ring of heme, using reducing equivalents like NADH to produce biliverdin, iron and CO <ref name="HO">PMID:17253780</ref>. HO consists of two main isoforms which are present in mammals, HO-1 and HO-2. The two isoforms are products of different genes, are different molecular sizes (32 kDa and 36 kDa respectively) and contain a different primary structure showing only 58% homology <ref name="HO1">PMID:15522396</ref>. However studies have shown that the two isoforms share a region with 100% secondary structure homology which is believed to be the catalytic site of the protein<ref name="HO"/>. The heme oxygenase isoforms are not free throughout the body but sequestered to certain tissues. The Heme oxygenase -1 is strongly expressed in the spleen and liver whereas Heme Oxygenase-2 is strongly expressed in the brain, testis and vascular systems<ref name="sc1">PMID:12909459</ref>.
+'''Heme Oxygenase''' (HO) is a member of the [[Hemeproteins|Hemoprotein family]] and catalyzes the Oxygen-dependent cleavage of the porphyrin ring of heme, using reducing equivalents like NADH to produce biliverdin, iron and CO <ref name="HO">PMID:17253780</ref>. HO consists of two main isoforms which are present in mammals, HO-1 and HO-2. The two isoforms are products of different genes, are different molecular sizes (32 kDa and 36 kDa respectively) and contain a different primary structure showing only 58% homology <ref name="HO1">PMID:15522396</ref>. However studies have shown that the two isoforms share a region with 100% secondary structure homology which is believed to be the catalytic site of the protein<ref name="HO"/>. The heme oxygenase isoforms are not free throughout the body but sequestered to certain tissues.
+*'''Heme oxygenase -1''' is inducible and is strongly expressed in the spleen and liver.
+*'''Heme Oxygenase-2''' is expressed constitutively and is strongly expressed in the brain, testis and vascular systems<ref name="sc1">PMID:12909459</ref>.
 ==='''Ligand'''===
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 ==Additional Resources==
-For additional information, See: [[Cancer]] <br />
+For additional information, see:
-For additional information, See: [[NADPH Cytochrome P450 Oxidoreductase]] <br />
+*[[Cancer]]
+*[[NADPH Cytochrome P450 Oxidoreductase]]
+*[[Hemeproteins]]
 ==3D structures of heme oxygenase==
+[[Heme oxygenase 3D structures]]
-''Updated February 2013''
+</StructureSection>
-===Heme oxygenase===
-[[2z68]], [[1wzd]], [[1wzf]], [[1wzg]], [[1iw0]], [[1iw1]], [[4goh]] – CdHO – ''Coreynebacterium diphtheriae''<BR />
-[[1wnv]], [[1wnw]], [[1wnx]] – CdHO (mutant) <BR />
-[[1ubb]], [[1dve]], [[1dvg]] – rHO – rat<BR />
-[[1irm]] – rHO-apo<BR />
-[[3gas]] – HO – ''Helicobacter pylori''<BR />
-[[1xk1]], [[1xk0]], [[1xjz]], [[1xk2]], [[1oyk]], [[1oyl]], [[1oze]], [[1ozr]] - hHO-1 (mutant) – human<BR />
-[[1n45]], [[1n3u]] – hHO-1<BR />
-[[2rgz]], [[2qpp]], [[2q32]] – hHO-2 (mutant) <BR />
-[[1wov]], [[1wow]] – SyHO-2 – ''Synechocystis''<BR />
-[[1we1]] – HO-1 – ''Cyanobacterium synechocystis''<BR />
-[[1p3t]], [[1j77]] – NmHO-1 – ''Nisseria meningitides''
-===Heme oxygenase complex with NO===
-[[1j02]] - rHO-1 + NO<BR />
-[[1kx3]], [[1ozl]], [[1ozw]], [[1xk3]] - hHO-1 (mutant) + NO<BR />
-[[1wox]] – SyHO-2 + NO<BR />
-[[1p3u]] - NmHO-1 + NO<BR />
-===Heme oxygenase with verdoheme===
-[[3moo]] – CdHO + verdoheme-N3<BR />
-[[2zvu]] – rHO-1 + verdoheme<BR />
-[[1twn]] - hHO-1 + verdoheme<BR />
-[[1twr]] - hHO-1 + verdoheme-NO<BR />
-===Heme oxygenase complex with reaction products===
-[[1p3v]] - NmHO-1 + CO<BR />
-[[1ulx]], [[1ix4]] - rHO-1 + CO<BR />
-[[1j2c]] - rHO-1 + biliverdine<BR />
-[[1s8c]] - hHO-1 + biliverdine<br />
-[[4gpc]], [[4gpf]], [[4gph]] - CdHO + biliverdine<br />
-===Heme oxygenase binary complexes===
-[[3i8r]], [[3i9t]] – CdHO + DTT<BR />
-[[1v8x]] – CdHO + O2<BR />
-[[4g7l]] – rHO-1 + O2<br />
-[[4g7p]], [[4g7t]], [[4g7u]], [[4g8p]], [[4g8u]], [[4g8w]], [[4g98]], [[4g99]] – rHO-1 + CO<br />
-[[3i9u]] – rHO-1 + DTE <BR />
-[[2e7e]], [[1ix3]] – rHO-1 + CN<BR />
-[[1ivj]] - rHO-1 + N3>br />
-[[1vgi]] - rHO-1 + Xe<BR />
-[[2dy5]] - rHO-1 + azole derivative<BR />
-[[3k4f]], [[3hok]], [[3czy]], [[3tgm]] – hHO-1 + azole derivative<BR />
-[[1ni6]] – hHO-1 + trehalose<BR />
-[[1s13]] - hHO-1 + 2-phenylheme<BR />
-[[1t5p]] - hHO-1 + 12-phenylheme<br />
-[[2zdo]] – SaHO + hemin – ''Staphylococcus aureus''<br />
-[[2zdp]] – SaHO + Co<br />
-[[3lgm]], [[3lgn]], [[3qgp]], [[4fnh]] – SaHO + heme<br />
-[[4fni]] – SaHO + heme + CN
 ==References==