New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins
Abstract
Tyrosinases are widely distributed in nature. They are copper-containing oxidases belonging to the type 3 copper protein family, together with catechol oxidases and haemocyanins. Tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair in mammals, where two more enzymes, the tyrosinase-related proteins (Tyrps), participate in the pathway. The structure and catalytic mechanism of mammalian tyrosinases have been extensively studied but they are not completely understood because of the lack of information on the tertiary structure. The availability of crystallographic data of one plant catechol oxidase and one bacterial tyrosinase has improved the model of the three-dimensional structure of the active site of the enzyme. Furthermore, sequence comparison of tyrosinase and the Tyrps reveals that the three orthologue proteins share many key structural features, because of their common origin from an ancestral gene, although the specific residues responsible for their different catalytic capabilities have not been identified yet. This review summarizes our current knowledge of tyrosinase and Tyrps structure and function and describes the catalytic mechanism of tyrosinase and Dct/Tyrp2, which are better characterized.
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Copper is a cofactor of tyrosinase, the main enzyme involved in synthesis of the skin pigment melanin.
“Furthermore, Cu is a cofactor of tyrosinase, the main enzyme involved in synthesis of the skin pigment melanin [128].”
From Bioactive Compounds for Skin Health: A Review (2021) · cites this paper as [128]
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- Authors
- Olivares, C., & Solano, F.
- Affiliations
- Universidad de Murcia (ES)
- ORCID
- Solano, Francisco
- Venue
- Pigment Cell & Melanoma Research
- Publisher
- Wiley
- Published
- 2009-10-14
- Volume
- 22
- Issue
- 6
- Pages
- 750-760
- ISSN
- 1755-1471 (ISSN-L)
- 1755-148X
- OpenAlex
- W1972557284
- Cited by
- 312
- References
- 127
- Citations by year
- 2026: 12 · 2025: 17 · 2024: 21 · 2023: 14 · 2022: 23 · 2021: 23 · 2020: 14 · 2019: 11 · 2018: 18 · 2017: 21 · 2016: 17 · 2015: 15 · 2014: 24 · 2013: 15 · 2012: 35
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Pigment Cell & Melanoma Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- tyrosinase, tyrosinase-related proteins, catechol oxidase, active site structure, catalytic mechanism, melanogenesis, skin pigmentation, hair pigmentation, crystal structure
- MeSH terms
- Amino Acid Sequence, Animals, Catechol Oxidase, Humans, Isoenzymes, Melanins, Models, Molecular, Molecular Sequence Data, Monophenol Monooxygenase, Molecular Structure, Sequence Alignment, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Catalytic Domain
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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