Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NaOCl | the heme iron directly reacts with NaOCl. The heme reduces NaOCl toxicity towards Mb side-chains. The oxidized (Fe3+) form of Mb (metMB) peroxidase activity is significantly decreased after incubation with NaOCl and NaCN, but not with NaOCl alone | Equus caballus | |
NaOCl | the heme iron directly reacts with NaOCl. The heme reduces NaOCl toxicity towards Mb side-chains. The oxidized (Fe3+) form of Mb (metMB) peroxidase activity is significantly decreased after incubation with NaOCl and NaCN, but not with NaOCl alone | Mus musculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | required, located in the heme group | Equus caballus | |
Fe2+ | required, located in the heme group | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Equus caballus | substrate specificity analysis, overview | ? | - |
- |
|
additional information | Mus musculus | substrate specificity analysis, overview | ? | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Equus caballus | P68082 | - |
- |
Mus musculus | P04247 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
heart | - |
Equus caballus | - |
heart | - |
Mus musculus | - |
quadriceps | - |
Mus musculus | - |
skeletal muscle | - |
Equus caballus | - |
skeletal muscle | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 | - |
Equus caballus | oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O | - |
? | |
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 | - |
Mus musculus | oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O | - |
? | |
3,3',5,5'-tetramethylbenzidine + 2 H+ + H2O2 | - |
Equus caballus | ? + 2 H2O | - |
? | |
3,3',5,5'-tetramethylbenzidine + 2 H+ + H2O2 | - |
Mus musculus | ? + 2 H2O | - |
? | |
additional information | substrate specificity analysis, overview | Equus caballus | ? | - |
- |
|
additional information | substrate specificity analysis, overview | Mus musculus | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
Mb peroxidase | - |
Equus caballus |
Mb peroxidase | - |
Mus musculus |
metMb peroxidase | - |
Equus caballus |
metMb peroxidase | - |
Mus musculus |
myoglobin | - |
Equus caballus |
myoglobin | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.1 | - |
assay at | Mus musculus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
metMb peroxidase activity is pH-dependent, increasing as pH decreases from 7.4 to 6.1, which is biologically relevant to anaerobic vertebrate muscle when incurring intracellular lactic acidosis | Equus caballus |
additional information | - |
metMb peroxidase activity is pH-dependent, increasing as pH decreases from 7.4 to 6.1, which is biologically relevant to anaerobic vertebrate muscle when incurring intracellular lactic acidosis | Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | myoglobin (Mb) is the predominant oxygen-binding heme protein in vertebrate skeletal muscle and heart | Equus caballus | |
heme | myoglobin (Mb) is the predominant oxygen-binding heme protein in vertebrate skeletal muscle and heart | Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | acetylation of tyrosine residues would inhibit peroxidase activity | Equus caballus |
malfunction | Tyr103 acetylation significantly reduces the rate of ferrylMb auto-reduction, indicating the role of tyrosine residues as intramolecular substrates | Mus musculus |
additional information | role of tyrosine residues in Mb peroxidase activity | Equus caballus |
additional information | role of tyrosine residues in Mb peroxidase activity, overview. Residue Y103 is important in orienting certain substrates in the heme pocket | Mus musculus |
physiological function | although their function is most commonly associated with facilitating oxygen storage and diffusion, myoglobin (Mb) has also been implicated in cellular antioxidant defense. The oxidized (Fe3+) form of Mb (metMB) can react with hydrogen peroxide (H2O2) to produce ferrylmyoglobin (ferrylMb). FerrylMb can be reduced back to metMb for another round of reaction with H2O2. Horse skeletal muscle Mb displays peroxidase activity using 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) as reducing substrates, as well as the biologically-relevant substrates NADH/NADPH, ascorbate, caffeic acid, and resveratrol. FerrylMb can be reduced by both ethanol and acetaldehyde. MetMb reacts with hypochlorite in a heme-dependent fashion, indicating that Mb could play a role in hypochlorite detoxification. Mb peroxidase activity might be an important antioxidant mechanism in vertebrate cardiac and skeletal muscle under a variety of physiological conditions, such as those that might occur in contracting skeletal muscle or during hypoxia | Equus caballus |
physiological function | although their function is most commonly associated with facilitating oxygen storage and diffusion, myoglobin (Mb) has also been implicated in cellular antioxidant defense. The oxidized (Fe3+) form of Mb (metMB) can react with hydrogen peroxide (H2O2) to produce ferrylmyoglobin (ferrylMb). FerrylMb can be reduced back to metMb for another round of reaction with H2O2. Horse skeletal muscle Mb displays peroxidase activity using 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) as reducing substrates, as well as the biologically-relevant substrates NADH/NADPH, ascorbate, caffeic acid, and resveratrol. FerrylMb can be reduced by both ethanol and acetaldehyde. MetMb reacts with hypochlorite in a heme-dependent fashion, indicating that Mb could play a role in hypochlorite detoxification. Mb peroxidase activity might be an important antioxidant mechanism in vertebrate cardiac and skeletal muscle under a variety of physiological conditions, such as those that might occur in contracting skeletal muscle or during hypoxia | Mus musculus |