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Literature summary for 1.3.98.5 extracted from
- Discovery and characterization of HemQ an essential heme biosynthetic pathway component (2010), J. Biol. Chem., 285, 25978-25986 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Bacillus subtilis |
| expressed in Escherichia coli | Mycobacterium tuberculosis |
| expressed in Escherichia coli | Streptomyces coelicolor |
| expressed in Escherichia coli | Cutibacterium acnes |
| expression in Escherichia coli | Bacillus subtilis |
| expression in Escherichia coli | Mycobacterium tuberculosis |
| expression in Escherichia coli | Streptomyces coelicolor |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H156A | the mutant shows less than 10% of wild type activity | Mycobacterium tuberculosis |
| H156C | the mutant shows less than 10% of wild type activity | Mycobacterium tuberculosis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Fe-coproporphyrin III + H2O2 | Bacillus subtilis | - |
harderoheme III + CO2 + H2O | - |
? |  |
| Fe-coproporphyrin III + H2O2 | Mycobacterium tuberculosis | - |
harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | Streptomyces coelicolor | - |
harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | Cutibacterium acnes | - |
harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | Bacillus subtilis | overall reaction | protoheme + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | Mycobacterium tuberculosis | overall reaction | protoheme + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | Streptomyces coelicolor | overall reaction | protoheme + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | Cutibacterium acnes | overall reaction | protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | Bacillus subtilis | - |
protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | Mycobacterium tuberculosis | - |
protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | Streptomyces coelicolor | - |
protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | Cutibacterium acnes | - |
protoheme + CO2 + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Cutibacterium acnes | - |
- |
- |
| Mycobacterium tuberculosis | - |
- |
- |
| Streptomyces coelicolor | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration | Bacillus subtilis |
| HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration | Mycobacterium tuberculosis |
| HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration | Streptomyces coelicolor |
| HisPur metal chelate column chromatography and Sephacryl S-300 gel filtration | Cutibacterium acnes |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Fe-coproporphyrin III + H2O2 | - |
Bacillus subtilis | harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | - |
Mycobacterium tuberculosis | harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | - |
Streptomyces coelicolor | harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | - |
Cutibacterium acnes | harderoheme III + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | overall reaction | Bacillus subtilis | protoheme + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | overall reaction | Mycobacterium tuberculosis | protoheme + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | overall reaction | Streptomyces coelicolor | protoheme + CO2 + H2O | - |
? | |
| Fe-coproporphyrin III + H2O2 | overall reaction | Cutibacterium acnes | protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | - |
Bacillus subtilis | protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | - |
Mycobacterium tuberculosis | protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | - |
Streptomyces coelicolor | protoheme + CO2 + H2O | - |
? | |
| harderoheme III + H2O2 | - |
Cutibacterium acnes | protoheme + CO2 + H2O | - |
? | |
| additional information | HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min | Bacillus subtilis | ? | - |
? | |
| additional information | HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min | Mycobacterium tuberculosis | ? | - |
? | |
| additional information | HemQ additionally possesses minimal peroxidase activity, and as a catalase it has a turnover of over 10000 per min | Streptomyces coelicolor | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 26000, SDS-PAGE | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HemQ | - |
Bacillus subtilis |
| HemQ | - |
Mycobacterium tuberculosis |
| HemQ | - |
Streptomyces coelicolor |
| HemQ | - |
Cutibacterium acnes |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Bacillus subtilis | |
| heme | - |
Mycobacterium tuberculosis | |
| heme | - |
Streptomyces coelicolor | |
| heme | - |
Cutibacterium acnes | |
| heme | heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule | Bacillus subtilis | |
| heme | heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule | Mycobacterium tuberculosis | |
| heme | heme is a high spin ferric iron and is ligated by a conserved histidine with the sixth coordination site available for binding a small molecule | Streptomyces coelicolor | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro | Bacillus subtilis |
| metabolism | the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro | Mycobacterium tuberculosis |
| metabolism | the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro | Streptomyces coelicolor |
| metabolism | the enzyme, along with the terminal two pathway enzymes protoporphyrinogen oxidase HemY and ferrochelatase is required to synthesize heme in vivo and in vitro | Cutibacterium acnes |
| physiological function | the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme | Bacillus subtilis |
| physiological function | the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme | Mycobacterium tuberculosis |
| physiological function | the presence of HemQ along with the terminal two pathway enzymes, protoporphyrinogen oxidase (HemY) and ferrochelatase, is required to synthesize heme in vivo and in vitro. To be fully functional in vitro, HemQ requires the presence of a bound heme | Streptomyces coelicolor |
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