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<StructureSection load='1gge' size='350' side='right' scene='46/467276/Cv/1' caption='E. coli catalase Hpii tetramer showing the heme group, [[1gge]]'>
[[Image:Catalases MotM57.png| Three types of catalases. The first two (human and bacterial) use hemoglobin-bound iron to bind to oxygen, while the third (a pseudocatalase) uses manganese (metals shown in light blue). From [https://pdb101.rcsb.org/motm/57 Molecule of the Month] (RCSB PDB) by David Goodsell based on PDB-IDs [[1qqw]], [[1iph]], and [[1jku]].|thumb|500px|right]]
__TOC__


== Function ==
'''Catalase''' (CAT) catalyzes the conversion of hydrogen peroxide to water and oxygen.  CAT contains porphyrin-heme Fe group which reacts with the hydrogen peroxide.  CAT containing Mn are called pseudocatalase (PCAT).<ref>PMID:21524057</ref>  '''Catalase-peroxidase''' (CAT KatG) is a bifunctional enzyme with both catalase and peroxidase activities.  CAT KatG cofactor is a heme group.  It provides defense against oxidative stress by reducing hydrogen peroxide.  Mutations in CAT KatG can cause resistance to the anti-malarial drug isoniazid (INH).<ref>PMID:15231843</ref>  '''Catalase-phenol oxidase''' (CATPO) is a heme-containing CAT which shows phenol oxidase activity.<ref>PMID:22370948</ref>
'''Catalase''' (CAT) catalyzes the conversion of hydrogen peroxide to water and oxygen.  CAT contains porphyrin-heme Fe group which reacts with the hydrogen peroxide.  CAT containing Mn are called pseudocatalase (PCAT).<ref>PMID:21524057</ref>  '''Catalase-peroxidase''' (CAT KatG) is a bifunctional enzyme with both catalase and peroxidase activities.  CAT KatG cofactor is a heme group.  It provides defense against oxidative stress by reducing hydrogen peroxide.  Mutations in CAT KatG can cause resistance to the anti-malarial drug isoniazid (INH).<ref>PMID:15231843</ref>  '''Catalase-phenol oxidase''' (CATPO) is a heme-containing CAT which shows phenol oxidase activity.<ref>PMID:22370948</ref>


[[Image:Catalase net reaction.png|700px]]


Catalase is a <scene name='46/467276/Cv/2'>tetramer of four polypeptide chains</scene>, each over 500 amino acids long. It contains <scene name='46/467276/Cv/3'>four porphyrin heme (iron) groups</scene> that allow the enzyme to react with the hydrogen peroxide. <scene name='46/467276/Cv/5'>Coordination of heme</scene> in ''E. coli'' catalase.<ref>PMID:11455600</ref>
There are four oxygen atoms total in the reactants. Which do you think will be paired up after the reaction is completed (i.e. in the dixoxygen molecule O<sub>2</sub> from as one of the products)?
 
== Structure ==
<StructureSection load='1gge' size='350' side='right' scene='46/467276/Cv/1' caption='E. coli catalase Hpii tetramer showing the heme groups in yellow. PDB-ID [[1gge]]'>
 
Catalase is a <scene name='46/467276/Cv/2'>tetramer</scene>, each polypeptide chain is over 500 amino acids long. It contains <scene name='46/467276/Cv/3'>four porphyrin heme (iron) groups</scene> that allow the enzyme to react with the hydrogen peroxide. <scene name='46/467276/Cv/7'>Coordination of iron</scene> in ''E. coli'' catalase is by the four nitrogen atoms of the heme molecule, an oxygen from a tyrosine side chain and a water molecule (water molecules are shown as red spheres).<ref>PMID:11455600</ref>
 
As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen. The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr357 in the fifth iron ligand, which can assist in the oxidation of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His74 and Asn147 with reaction intermediates.<ref>PMID:11455600</ref>
 
[[Image:Catalase steps.PNG|center|313px]]


As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen. The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr357 in the fifth iron ligand, which can assist in the oxidation of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His74 and Asn147 with reaction intermediates.<ref>PMID:11455600</ref> <br />
See more details in [[Ann Taylor/Catalase]]<br />
[[Human Erythrocyte Catalase]]<br />
[[Catalase 2CAG bcce2014]].<br />
See also [[Catalase (Hebrew)]].
</StructureSection>
</StructureSection>
== 3D Structures of catalase ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
==pH dependence==
{{#tree:id=OrganizedByTopic|openlevels=0|


*catalase
The following video shows how the rate of the potato catalase depends on the pH. Do you have a hypothesis why both low and high pH slow down the enzyme compared to neutral pH? Which acid/base groups are part of the mechanism described above? How is the structure (shape) of the enzyme affected by changes in pH?


**[[1qqw]], [[1dgb]], [[1dgf]], [[1f4j]] – hCAT - human<br />
<html5media height="300" width="360">https://www.youtube.com/watch?v=58CuZHUe91E</html5media>
**[[4cat]] – CAT – ''Penicillium janthinellum''<br />
**[[1iph]], [[1gge]], [[1ye9]], [[4bfl]] – EcCAT Hpii – ''Escherichia coli''<br />
**[[1u2j]], [[1u2k]] – EcCAT Hpi C terminal<br />
**[[1u2l]] – EcCAT KatG<br />
**[[1cf9]], [[1qf7]], [[1gg9]], [[1ggh]], [[1ggj]], [[1ggk]], [[1p7y]], [[1p7z]], [[1p80]], [[1p81]], [[1qws]], [[3p9p]], [[3p9q]], [[3p9r]], [[3p9s]], [[3pq2]], [[3pq3]], [[3pq4]], [[3pq5]], [[3pq6]], [[3pq7]], [[3pq8]], [[3ttt]], [[3ttu]], [[3ttv]], [[3ttw]], [[3ttx]], [[4enp]], [[4enq]], [[4enr]], [[4ens]], [[4ent]], [[4enu]], [[4env]], [[4enw]] - EcCAT Hpii (mutant)<br />
**[[4blc]], [[1tgu]], [[1th3]], [[3nwl]], [[5gkn]] – bCAT – Bovine<br />
**[[3j7b]] – bCAT – MicroED<br />
**[[1a4e]] – CAT A – yeast<br />
**[[2cag]], [[1e93]], [[1m85]], [[1mqf]], [[1h7k]] – PmCAT – ''Proteus mirabilis''<br />
**[[1h6n]], [[3hb6]] - PmCAT (mutant)<br />
**[[1hbz]], [[1gwe]], [[1gwf]] – MlCAT – ''Micrococcus lysodeikticus''<br />
**[[1m7s]] – CAT CatF – ''Pseudomonas syringae''<br />
**[[1qwl]], [[2iqf]] – HpCAT – ''Helicobacter pylori''<br />
**[[1si8]] – CAT – ''Enterococcus Faecalis''<br />
**[[1sj2]], [[2cca]] – MtCAT KatG – ''Mycobacterium tuberculosis''<br />
**[[2ccd]], [[4c50]], [[4c51]] - MtCAT KatG (mutant)<br />
**[[1ub2]] – CAT – ''Synechococcus elongatus''<br />
**[[5l05]], [[5sw4]], [[5sw5]], [[5sx3]], [[5sx6]], [[5sx7]] – BpCAT KatG – ''Burkholderia pseudomallei''<br />
**[[5l02]], [[5sx1]], [[5sx2]], [[5sxw]], [[5sxx]] - BpCAT KatG (mutant)<br />
**[[1itk]], [[2a9e]], [[3n3s]], [[3uw8]] – HmCAT KatG – ''Haloarcula marismortui'' <br />
**[[3vlh]], [[3vlk]], [[3vlm]] – HmCAT KatG (mutant)<br />
**[[1sy7]] – NcCAT-1 – ''Neurospora crassa''<br />
**[[3ej6]], [[3zj4]], [[3zj5]], [[4aj9]], [[4bim]] – NcCAT-3<br />
**[[2j2m]] – CAT – ''Exiguobacterium oxidotolerans''<br />
**[[2isa]] – CAT – ''Vibrio salmonicida''<br />
**[[2xf2]] - 2iuf – PjCAT – ''Penicillium janthinellum''<br />
**[[2xq1]] – CAT – ''Pichia angusta''<br />
**[[4e37]] – CAT – ''Pseudomonas aeruginosa''<br />
**[[3ut2]] – CAT – rice blast fungus<br />
**[[4cab]] – CAT – ''Deinococcus radiodurans''<br />
**[[4qol]] – BpCAT – ''Bacillus pumilus''<br />


*Catalase binary complexes
==See also==
[[Ann Taylor/Catalase]]<br />
[[Human Erythrocyte Catalase]]<br />
[[Catalase 2CAG bcce2014]].<br />
See also [[Catalase (Hebrew)]].


**[[7cat]], [[8cat]] – bCAT + NADPH <br />
== 3D Structures of catalase ==
**[[2cah]] - PmCAT + NADPH<br />
[[Catalase 3D structures]]
**[[1gwh]] - MlCAT + NADPH<br />
**[[5sxr]] - BpCAT KatG + NAD<br />
**[[1nm0]] – PmCAT + formiate<br />
**[[1qwm]] - HpCAT + formic acid<br />
**[[1dgg]] – hCAT + CN<br />
**[[3vli]], [[3vlj]] - HmCAT KatG (mutant) + CN<br />
**[[3vll]] - HmCAT KatG (mutant) + salicylhydroxamic acid<br />
**[[1th2]] – bCAT + N3<br />
**[[3rgp]], [[3re8]] – bCAT + NO<br />
**[[3rgs]] – bCAT + NH3<br />
**[[5sw6]], [[5sx0]] - BpCAT KatG + O<br />
**[[2iuf]] – PjCAT + O<br />
**[[5sxq]] - BpCAT KatG + INH<br />
**[[5sxs]] - BpCAT KatG + INH + AMP<br />
**[[5sxt]] - BpCAT KatG + INH<br />
**[[3n3h]] - BpCAT KatG (mutant) + INH<br />
**[[1dgh]] – hCAT + amino-triazole<br />
**[[1th4]] - bCAT + amino-triazole<br />
**[[1ggf]] - EcCAT Hpii (mutant) + H2O2<br />
**[[3vu3]] – EcCAT Hpii + HFQ<br />
**[[4b7f]], [[4b7h]] – CgCAT + NADPH + NO – ''Corynebacterium glutamicum''<br />
**[[4b7g]] – CgCAT + NADPH <br />
**[[4qom]] – BpCAT + pyrogallol<br />
**[[4qon]] – BpCAT + catechol<br />
**[[4qoo]] – BpCAT + resorcinol<br />
**[[4qop]] – BpCAT + hydroquinone<br />
**[[4qoq]] – BpCAT + guaiacol<br />
**[[4qom]] – BpCAT + chlorophenol<br />
 
*Pseudocatalase Mn-containing


**[[1jku]] – LpPCAT-Mn – ''Lactobacillus plantarum''<br />
**[[1o9i]] – LpPCAT-Mn (mutant) <br />
**[[2cwl]] – TtPCAT-Mn Mn-free – ''Thermus thermophilus''<br />
**[[2v8u]] - TtPCAT-Mn<br />
**[[2v8t]] - TtPCAT-Mn + chloride<br />
**[[1jkv]] - LpPCAT-Mn + N3<br />


*Catalase-phenol oxidase


**[[4aue]], [[4aul]], [[4aum]], [[4aun]], [[4b2y]], [[4b31]], [[4b40]], [[4b5k]], [[4b7a]] - CATPO - ''Scytalidium thermophilum'' <br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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

Michal Harel, Alexander Berchansky, Ann Taylor, Karsten Theis
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