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Literature summary extracted from
- Using cryo-EM to understand antimycobacterial resistance in the catalase-peroxidase (KatG) from Mycobacterium tuberculosis (2021), Structure, 29, 899-912.e4 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.11.1.21 | purified wild-type and mutant enzymes with bound isoniazid, X-ray diffraction structure determination and analysis at 2.7-3.7 A resolution, dimeric cryo-electronmicroscopic structure of KatGINH. The two protomers are nearly identical, with a root-meansquare deviation (RMSD) value of 0.4 A for Ca atoms when superposing protomer A onto protomer B. There is one notable difference, with protomer B displaying density for residues 206-221. These residues form part of a large loop insertion (LL1), which extends from Glu195 to Asn231 and includes Tyr229 of the MYW catalytic triad. Density for these residues is not observed in protomer A | Mycobacterium tuberculosis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.11.1.21 | T275P | site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled | Mycobacterium tuberculosis |
| 1.11.1.21 | W107R | site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation | Mycobacterium tuberculosis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.21 | Fe2+ | the heme group | Mycobacterium tuberculosis |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.21 | 161000 | - |
gel filtration | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.21 | 2 H2O2 | Mycobacterium tuberculosis | - |
O2 + 2 H2O | - |
? | |
| 1.11.1.21 | 2 H2O2 | Mycobacterium tuberculosis H37Rv | - |
O2 + 2 H2O | - |
? | |
| 1.11.1.21 | 2 H2O2 | Mycobacterium tuberculosis ATCC 25618 | - |
O2 + 2 H2O | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | Mycobacterium tuberculosis | pro-drug activation | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | Mycobacterium tuberculosis H37Rv | pro-drug activation | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | Mycobacterium tuberculosis ATCC 25618 | pro-drug activation | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.21 | Mycobacterium tuberculosis | P9WIE5 | - |
- |
| 1.11.1.21 | Mycobacterium tuberculosis ATCC 25618 | P9WIE5 | - |
- |
| 1.11.1.21 | Mycobacterium tuberculosis H37Rv | P9WIE5 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.21 | 2 H2O2 | - |
Mycobacterium tuberculosis | O2 + 2 H2O | - |
? | |
| 1.11.1.21 | 2 H2O2 | - |
Mycobacterium tuberculosis H37Rv | O2 + 2 H2O | - |
? | |
| 1.11.1.21 | 2 H2O2 | - |
Mycobacterium tuberculosis ATCC 25618 | O2 + 2 H2O | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | pro-drug activation | Mycobacterium tuberculosis | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | enzyme binding structure analysis, modeling, overview | Mycobacterium tuberculosis | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | pro-drug activation | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | enzyme binding structure analysis, modeling, overview | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | pro-drug activation | Mycobacterium tuberculosis ATCC 25618 | ? | - |
? | |
| 1.11.1.21 | isoniazid + H2O2 | enzyme binding structure analysis, modeling, overview | Mycobacterium tuberculosis ATCC 25618 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.11.1.21 | homodimer | 2 * 80000, about sequence calculation | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.11.1.21 | KatG | - |
Mycobacterium tuberculosis |
| 1.11.1.21 | Rv1908c | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.21 | 20 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.21 | 7 | - |
assay at | Mycobacterium tuberculosis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.21 | heme | determination and analysis of the structure of the heme environment of wild-type KatG and KatG bound to isoniazid, overview. The inactivated pro-drug added to the sample is not perturbing the heme site | Mycobacterium tuberculosis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.11.1.21 | malfunction | mutations that render the enzyme unable to activate the pro-drug lead to isoniazid (INH) resistance. For two INH resistance variants, W107R and T275P, significant structural disorder relating to heme uptake and retention is the likely cause for INH resistance, dynamics of heme binding are determined by cryo-electronmicroscopy of wild-type and mutant enzymes at 2.7-3.7 A resolution, overview | Mycobacterium tuberculosis |
| 1.11.1.21 | additional information | KatG structure-function analysis, overview | Mycobacterium tuberculosis |
| 1.11.1.21 | physiological function | KatG from Mycobacterium tuberculosis is a catalase-peroxidase that can utilize and degrade hydrogen peroxide (H2O2) either through functioning as a catalase or as a peroxidase. In Mycobacterium tuberculosis, the multifunctional heme enzyme KatG is indispensable for activation of isoniazid (INH), a first-line pro-drug for treatment of tuberculosis. The activated drug species forms an INH-NAD adduct that subsequently triggers anti-tubercular activity | Mycobacterium tuberculosis |
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