Catalase

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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). Catalase-peroxidase (CAT KatG) is a bifunctional enzyme with both catalase and peroxidase activities. CAT KatG cofactor is a 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). Catalase-phenol oxidase (CATPO) is a heme-containing CAT which shows phenol oxidase activity.


Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide.

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.[13] 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.


3D Structures of catalase

Updated on 28-February-2014

1qqw, 1dgb, 1dgf, 1f4j – hCAT - human

4cat – CAT – Penicillium janthinellum

1iph, 1gge, 1ye9, 4bfl – EcCAT Hpii – Escherichia coli

1u2j, 1u2k – EcCAT Hpi C terminal

1u2l – EcCAT KatG

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)

4blc, 1tgu, 1th3, 3nwl – bCAT – Bovine

1a4e – CAT A – yeast

2cag, 1e93, 1m85, 1mqf, 1h7k – PmCAT – Proteus mirabilis

1h6n, 3hb6 - PmCAT (mutant)

1hbz, 1gwe, 1gwf – MlCAT – Micrococcus lysodeikticus

1m7s – CAT CatF – Pseudomonas syringae

1qwl, 2iqf – HpCAT – Helicobacter pylori

1si8 – CAT – Enterococcus Faecalis

1sj2, 2cca – MtCAT KatG – Mycobacterium tuberculosis

2ccd, 4c50, 4c51 - MtCAT KatG (mutant)

1ub2 – CAT – Synechococcus elongatus

1mwv, 2b2o, 2b2q, 2fxg, 2fxh, 2fxj – BpCAT KatG – Burkholderia pseudomallei

1x7u, 2dv1, 2dv2, 3n3r - BpCAT KatG (mutant)

1itk, 2a9e, 3n3s, 3uw8 – HmCAT KatG – Haloarcula marismortui
3vlh, 3vlk, 3vlm – HmCAT KatG (mutant)
1sy7 – NcCAT-1 – Neurospora crassa

3ej6, 3zj4, 3zj5, 4aj9, 4bim – NcCAT-3

2j2m – CAT – Exiguobacterium oxidotolerans

2isa – CAT – Vibrio salmonicida

2xf2 - 2iuf – PjCAT – Penicillium janthinellum

2xq1 – CAT – Pichia angusta
4e37 – CAT – Pseudomonas aeruginosa
3ut2 – CAT – rice blast fungus

Catalase binary complexes

7cat, 8cat – bCAT + NADPH

2cah - PmCAT + NADPH

1gwh - MlCAT + NADPH

3n3o - BpCAT KatG + NAD

1nm0 – PmCAT + formiate

1qwm - HpCAT + formic acid

1dgg – hCAT + CN
3vli, 3vlj - HmCAT KatG (mutant) + CN
3vll - HmCAT KatG (mutant) + salicylhydroxamic acid
1th2 – bCAT + N3

3rgp, 3re8 – bCAT + NO

3rgs – bCAT + NH3

2b2r, 2b2s - BpCAT KatG + O

2iuf – PjCAT + O

3n3n - BpCAT KatG + INH

3n3p - BpCAT KatG + INH + AMP

3n3q - BpCAT KatG + INH

3n3h - BpCAT KatG (mutant) + INH

1dgh – hCAT + amino-triazole

1th4 - bCAT + amino-triazole

1ggf - EcCAT Hpii (mutant) + H2O2
3vu3 – EcCAT Hpii + HFQ
4b7f, 4b7h – CgCAT + NADPH + NO – Corynebacterium glutamicum
4b7g – CgCAT + NADPH

Pseudocatalase Mn-containing

1jku – LpPCAT-Mn – Lactobacillus plantarum

1o9i – LpPCAT-Mn (mutant)

2cwl – TtPCAT-Mn Mn-free – Thermus thermophilus

2v8u - TtPCAT-Mn

2v8t - TtPCAT-Mn + chloride

1jkv - LpPCAT-Mn + N3

Catalase-phenol oxidase

4aue, 4aul, 4aum, 4aun, 4b2y, 4b31, 4b40, 4b5k, 4b7a - CATPO - Scytalidium thermophilum

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Michal Harel, Alexander Berchansky, Karsten Theis, Ann Taylor

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