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Literature summary for 1.11.1.16 extracted from

  • Mannino, M.H.; Patel, R.S.; Eccardt, A.M.; Perez Magnelli, R.A.; Robinson, C.L.C.; Janowiak, B.E.; Warren, D.E.; Fisher, J.S.
    Myoglobin as a versatile peroxidase implications for a more important role for vertebrate striated muscle in antioxidant defense (2019), Comp. Biochem. Physiol. B, 234, 9-17 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.16

Inhibitors

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Equus caballus P68082
-
-
Mus musculus P04247
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Equus caballus
-
heart
-
 Mus musculus
-
quadriceps
-
 Mus musculus
-
skeletal muscle
-
 Equus caballus
-
skeletal muscle
-
 Mus musculus
-

Substrates and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1
-
 assay at Mus musculus

pH Range

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

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

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