Catalase: Difference between revisions
No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 11: | Line 11: | ||
[[Catalase 2CAG bcce2014]].<br /> | [[Catalase 2CAG bcce2014]].<br /> | ||
See also [[Catalase (Hebrew)]]. | See also [[Catalase (Hebrew)]]. | ||
== 3D Structures of catalase == | |||
[[Catalase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
== 3D Structures of catalase == | == 3D Structures of catalase == | ||
| Line 26: | Line 30: | ||
**[[4blc]], [[1tgu]], [[1th3]], [[3nwl]], [[5gkn]] – bCAT – Bovine<br /> | **[[4blc]], [[1tgu]], [[1th3]], [[3nwl]], [[5gkn]] – bCAT – Bovine<br /> | ||
**[[3j7b]] – bCAT – MicroED<br /> | **[[3j7b]] – bCAT – MicroED<br /> | ||
**[[6jnu]], [[6jnt]] – bCAT – Cryo EM<br /> | |||
**[[1a4e]] – CAT A – yeast<br /> | **[[1a4e]] – CAT A – yeast<br /> | ||
**[[2cag]], [[1e93]], [[1m85]], [[1mqf]], [[1h7k]] – PmCAT – ''Proteus mirabilis''<br /> | **[[2cag]], [[1e93]], [[1m85]], [[1mqf]], [[1h7k]] – PmCAT – ''Proteus mirabilis''<br /> | ||
| Line 45: | Line 50: | ||
**[[4cab]] – CAT – ''Deinococcus radiodurans''<br /> | **[[4cab]] – CAT – ''Deinococcus radiodurans''<br /> | ||
**[[4qol]] – BpCAT – ''Bacillus pumilus''<br /> | **[[4qol]] – BpCAT – ''Bacillus pumilus''<br /> | ||
**[[5yem]], [[5y17]], [[5xzn]], [[5xzm]], [[5xy4]], [[5xvz]] – CAT (mutant) – ''Mycothermus thrmophilus''<br /> | |||
*Catalase binary complexes | *Catalase binary complexes | ||
| Line 103: | Line 109: | ||
**[[3vli]], [[3vlj]] - HmCAT KatG (mutant) + CN<br /> | **[[3vli]], [[3vlj]] - HmCAT KatG (mutant) + CN<br /> | ||
**[[3vll]] - HmCAT KatG (mutant) + salicylhydroxamic acid<br /> | **[[3vll]] - HmCAT KatG (mutant) + salicylhydroxamic acid<br /> | ||
**[[5sw6]], [[5sx0]] - BpCAT KatG + O<br /> | **[[5sw6]], [[5sx0]], [[6mq1]] - BpCAT KatG + O<br /> | ||
**[[5kt9]] - BpCAT KatG (mutant) + O2<br /> | **[[5kt9]] - BpCAT KatG (mutant) + O2<br /> | ||
**[[6b9b]] - BpCAT KatG + maltose<br /> | |||
**[[5sxq]]- BpCAT KatG + isonicotinic acid<br /> | **[[5sxq]]- BpCAT KatG + isonicotinic acid<br /> | ||
**[[6mpy]], [[6mq0]] - BpCAT KatG + hydrazine derivative<br /> | |||
**[[5sxs]] - BpCAT KatG + isonicotinic acid + hydrazine + AMP<br /> | **[[5sxs]] - BpCAT KatG + isonicotinic acid + hydrazine + AMP<br /> | ||
**[[5sxt]] - BpCAT KatG + isonicotinic acid + hydrazine<br /> | **[[5sxt]] - BpCAT KatG + isonicotinic acid + hydrazine<br /> | ||
Revision as of 10:49, 29 April 2019
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).[1] 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).[2] Catalase-phenol oxidase (CATPO) is a heme-containing CAT which shows phenol oxidase activity.[3]
Catalase is a , each polypeptide chain is over 500 amino acids long. It contains that allow the enzyme to react with the hydrogen peroxide. in E. coli catalase.[4] Water molecules are shown as red spheres. 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.[5] See more details in Ann Taylor/Catalase 3D Structures of catalase
|
| ||||||||||
3D Structures of catalase3D Structures of catalase
Updated on 29-April-2019
ReferencesReferences
- ↑ Purwar N, McGarry JM, Kostera J, Pacheco AA, Schmidt M. Interaction of Nitric Oxide with Catalase: Structural and Kinetic Analysis. Biochemistry. 2011 May 6. PMID:21524057 doi:10.1021/bi200130r
- ↑ Bertrand T, Eady NA, Jones JN, Jesmin, Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA. Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J Biol Chem. 2004 Sep 10;279(37):38991-9. Epub 2004 Jul 1. PMID:15231843 doi:10.1074/jbc.M402382200
- ↑ Koclar Avci G, Coruh N, Bolukbasi U, Ogel ZB. Oxidation of phenolic compounds by the bifunctional catalase-phenol oxidase (CATPO) from Scytalidium thermophilum. Appl Microbiol Biotechnol. 2013 Jan;97(2):661-72. doi: 10.1007/s00253-012-3950-2., Epub 2012 Feb 28. PMID:22370948 doi:http://dx.doi.org/10.1007/s00253-012-3950-2
- ↑ Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli. Proteins. 2001 Aug 15;44(3):270-81. PMID:11455600
- ↑ Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli. Proteins. 2001 Aug 15;44(3):270-81. PMID:11455600