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Literature summary for 1.13.11.49 extracted from
- The chlorite dismutase (HemQ) from Staphylococcus aureus has a redox-sensitive heme and is associated with the small colony variant phenotype (2013), J. Biol. Chem., 288, 23488-23504.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene hemQ, overexpression in Escherichia coli, complementation of the hemQ-defective Staphylococcus aureus mutant | Staphylococcus aureus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) | substrate inhibition at higher concentrations over 0.2 mM | Staphylococcus aureus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | heme enzyme | Staphylococcus aureus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chlorite | Staphylococcus aureus | - |
chloride + O2 | - |
? | |
| chlorite | Staphylococcus aureus COL | - |
chloride + O2 | - |
? | |
| additional information | Staphylococcus aureus | although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates | ? | - |
? | |
| additional information | Staphylococcus aureus COL | although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
gene hemQ | - |
| Staphylococcus aureus COL | - |
gene hemQ | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli by anion exchange chromatography and gel filtration | Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chlorite | - |
Staphylococcus aureus | chloride + O2 | - |
? | |
| chlorite | - |
Staphylococcus aureus COL | chloride + O2 | - |
? | |
| additional information | although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates | Staphylococcus aureus | ? | - |
? | |
| additional information | HemQ uses heme or porphyrin-like organic molecules as substrates. At pH 6.8, the enzyme exhibits relatively weak peroxidase activity with the reductant 2,2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid], kinetics, overview | Staphylococcus aureus | ? | - |
? | |
| additional information | although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates | Staphylococcus aureus COL | ? | - |
? | |
| additional information | HemQ uses heme or porphyrin-like organic molecules as substrates. At pH 6.8, the enzyme exhibits relatively weak peroxidase activity with the reductant 2,2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid], kinetics, overview | Staphylococcus aureus COL | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chlorite dismutase | - |
Staphylococcus aureus |
| HemQ | - |
Staphylococcus aureus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Staphylococcus aureus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
assay at | Staphylococcus aureus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | HemQ's equilibrium affinity for heme is in the low micromolar range. Holo-HemQ reconstituted with heme exhibits heme lysis after less than 50 turnovers with peroxide and less than 10 turnovers with chlorite. The heme-free apoprotein aggregates or unfolds over time. HemQ uses heme or porphyrin-like organic molecules as substrates. Heme in HemQ degrades in the presence of relatively small numbers of equivalents of H2O2, chlorite, or peracetic acid | Staphylococcus aureus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | The chlorite dismutases (C-family proteins) are a widespread family of heme-binding proteins | Staphylococcus aureus |
| malfunction | a Staphylococcus aureus strain with an inactivated hemQ gene is generated and shown to be a slow growing small colony variant under aerobic but not anaerobic conditions. The DELTAhemQ mutant accumulates coproporphyrin specifically under aerobic conditions. Phenotypes, overview | Staphylococcus aureus |
| physiological function | similar substrate role for heme or porphyrin, with possible sensor-regulator functions for the protein | Staphylococcus aureus |
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