T3824
Tyrosinase from mushroom
lyophilized powder, ≥1000 unit/mg solid
Synonym(s):
Catechol Oxidase, Monophenol Monooxygenase, Monophenol, dihydroxyphenylalanine:oxygen oxidoreductase, Polyphenol Oxidase
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All Photos(8)
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
fungus (mushroom)
Quality Level
form
lyophilized powder
specific activity
≥1000 unit/mg solid
mol wt
119.5 kDa by electrophoresis
128 kDa by sedimentation velocity diffusion
133 kDa by LS
application(s)
diagnostic assay manufacturing
shipped in
wet ice
storage temp.
−20°C
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General description
Isoelectric point (pI): 4.7-5
pH optimum is 6-7
Molecular weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis.
Tyrosinase is a copper-containing oxidase, which has activity for both catechols and cresol. It is responsible for browning reactions. The enzyme is reported to have two binding sites for aromatic substrates and a different binding site for oxygen-copper. The copper is probably Cu(I), with inactivation involving oxidation to Cu(II) ion.
pH optimum is 6-7
Molecular weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis.
Tyrosinase is a copper-containing oxidase, which has activity for both catechols and cresol. It is responsible for browning reactions. The enzyme is reported to have two binding sites for aromatic substrates and a different binding site for oxygen-copper. The copper is probably Cu(I), with inactivation involving oxidation to Cu(II) ion.
Tyrosinase is a copper-containing oxidase with activity for catechols and cresol. Tyrosinase participates in the conversion of tyrosine to dihydroxyphenylalanine (DOPA), and polymerization of DOPA leads to melanin formation. Tyrosinase has a role in browning reactions. The enzyme is said to have two binding sites for aromatic substrates and a distinct binding site for oxygen-copper.
Application
Tyrosinase activity has been assessed in a study that developed an alternative therapeutic agent for treating hyperpigmentation. Tyrosinase has also been used in a study to investigate the oculocutaneous albinism phenotype in the Pakistani population.
Biochem/physiol Actions
Converts tyrosine to L-DOPA or tyramine to dopamine
Physical properties
Isoelectric point (pI): 4.7-5
pH optimum is 6-7
Molecular weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis.
pH optimum is 6-7
Molecular weight: 128 kDa by sedimentation velocity diffusion; 133 kDa by light-scattering measurements, and 119.5 kDa by electrophoresis.
Unit Definition
One unit = ΔA280 of 0.001 per min at pH 6.5 at 25 °C in 3 mL reaction mix containing L-tyrosine.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Previous studies have reported that estrogen hormone promotes melanogenesis while progesterone inhibits it. A selective estrogen receptor modulator (SERM), tamoxifen, has been shown to promote melanogenesis; however, to date, there have been no reports on the effects of a selective
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The critical review describes the known dicopper systems mediating the aromatic hydroxylation of monophenolic substrates. Such systems are of interest as structural and functional models of the type 3 copper enzyme tyrosinase, which catalyzes the ortho-hydroxylation of tyrosine to DOPA
Thomas J Jaworek et al.
Orphanet journal of rare diseases, 7, 44-44 (2012-06-28)
Oculocutaneous albinism (OCA) is caused by a group of genetically heterogeneous inherited defects that result in the loss of pigmentation in the eyes, skin and hair. Mutations in the TYR, OCA2, TYRP1 and SLC45A2 genes have been shown to cause
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A novel, integrated experimental and modeling framework was applied to an inhibition-based bi-enzyme (IBE) electrochemical biosensor to detect acetylcholinesterase (AChE) inhibitors that may trigger neurological diseases. The biosensor was fabricated by co-immobilizing AChE and tyrosinase (Tyr) on the gold working
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