Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis

NAKAMURA, Motoyoshi; Nakajima, Tasuku; OHBA, Yasunori; YAMAUCHI, Seigo; LEE, Byung Rho; Ichishima, Eiji

doi:10.1042/0264-6021:3500537

Cited by 30 publications

(36 citation statements)

References 25 publications

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“…van Gelder et al (1997), Wichers et al (2003), Cho et al (2003), Marusek et al (2006), Halaouili et al (2006), Hernandez-Romero et al (2006, Nakamura et al (2000) and Matoba et al (2006). As already stated, except for the active site, amino acid sequences show considerable variability and it seems to this reviewer that the salvation for understanding the role of PPO in plants and fungi will not come from the description of yet more amino acid sequences.…”

Section: Structure and Molecular Weight Of Ppomentioning

confidence: 86%

“…Indeed, the study of another bacterial tyrosinase, from Ralstonia has shown that possibly the unusually high ratio of hydroxylase/dopa oxidase activity of this particular PPO was linked to the presence of a seventh histidine unit, binding Cu (Hernandez-Romero et al, 2006). The importance of the histidine residues of a fungal PPO, the tyrosinase from Aspergillus oryzyae, expressed in Escherichia coli, has revealed the importance of a previously unrecorded histidine residue (Nakamura et al, 2000). These authors used site directed mutagenesis in their study of the enzyme.…”

Section: Structure and Molecular Weight Of Ppomentioning

confidence: 97%

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Polyphenol oxidases in plants and fungi: Going places? A review

2006

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Section: Structure and Molecular Weight Of Ppomentioning

confidence: 86%

Section: Structure and Molecular Weight Of Ppomentioning

confidence: 97%

Polyphenol oxidases in plants and fungi: Going places? A review

2006

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“…Different fungi have been investigated for the isolation of tyrosinase which has been obtained from Agaricus bisporus [14], Neurospora crassa [15, 16], Amanita muscaria [17], Lentinula edodes [18], Aspergillus oryzae [19], Portabella mushrooms, Pycnoporus sanguineus [20], and Lentinula boryana [21]. …”

Section: Sources Of Tyrosinasementioning

confidence: 99%

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Zaidi

Ali²,

Ali³

et al. 2014

Biochemistry Research International

144

111

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Tyrosinase is a natural enzyme and is often purified to only a low degree and it is involved in a variety of functions which mainly catalyse the o-hydroxylation of monophenols into their corresponding o-diphenols and the oxidation of o-diphenols to o-quinones using molecular oxygen, which then polymerizes to form brown or black pigments. The synthesis of o-diphenols is a potentially valuable catalytic ability and thus tyrosinase has attracted a lot of attention with respect to industrial applications. In environmental technology it is used for the detoxification of phenol-containing wastewaters and contaminated soils, as biosensors for phenol monitoring, and for the production of L-DOPA in pharmaceutical industries, and is also used in cosmetic and food industries as important catalytic enzyme. Melanin pigment synthesized by tyrosinase has found applications for protection against radiation cation exchangers, drug carriers, antioxidants, antiviral agents, or immunogen. The recombinant V. spinosum tryosinase protein can be used to produce tailor-made melanin and other polyphenolic materials using various phenols and catechols as starting materials. This review compiles the recent data on biochemical and molecular properties of microbial tyrosinases, underlining their importance in the industrial use of these enzymes. After that, their most promising applications in pharmaceutical, food processing, and environmental fields are presented.

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“…3). Although this His has not been defined as a copper ligand based on known PDB structures, a previous study has shown that it is essential for copper binding in tyrosinase from Aspergillus oryzae (58). This additional His may play an important role in binding CuB and may help identify copper-dependent tyrosinases in sequence databases.…”

Section: Coppermentioning

confidence: 99%

Comparative Genomics of Trace Element Dependence in Biology

Zhang

Gladyshev

2011

Journal of Biological Chemistry

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Biological trace elements are needed in small quantities but are used by all living organisms. A growing list of trace elementdependent proteins and trace element utilization pathways highlights the importance of these elements for life. In this minireview, we focus on recent advances in comparative genomics of trace elements and explore the evolutionary dynamics of the dependence of user proteins on these elements. Many zinc protein families evolved representatives that lack this metal, whereas selenocysteine in proteins is dynamically exchanged with cysteine. Several other elements, such as molybdenum and nickel, have a limited number of user protein families, but they are strictly dependent on these metals. Comparative genomics of trace elements provides a foundation for investigating the fundamental properties, functions, and evolutionary dynamics of trace element dependence in biology.All organisms require a regular supply of nutrients. The major biological elements, carbon, hydrogen, oxygen, nitrogen, phosphorus, and sulfur, are present in large quantities and are the main constituents of nucleic acids, proteins, lipids, cell walls, and mechanical structures (1, 2). There are also chemical elements, most of which are metals, that are present in small quantities (known as biological trace elements), including cobalt, copper, iron, manganese, molybdenum, nickel, zinc, selenium, and several other elements. The roles of trace elements primarily involve providing proteins with unique catalytic, structural, electron transfer, and other properties. They are used in numerous pathways, and all organisms utilize at least some of these elements (3-5). Their deficiency or mutations in genes that handle these elements often result in abnormal development, metabolic abnormalities, and even death (6 -8).Among trace elements, some such as zinc and iron appear to be used by all organisms (9 -11). Although organisms that survive under iron limitation have been reported (12, 13), it is unclear if they do not use this metal under iron-sufficient conditions. The number of proteins that utilize zinc or iron is large. For instance, Ͼ300 enzyme families require zinc for proper function (14). Metals are used by a wide range of proteins in the form of metal ions (e.g. manganese, copper, and nickel) or complex metal-containing cofactors (e.g. molybdopterin in the case of molybdenum and vitamin B 12 in the case of cobalt) (15-17). Selenium is used mainly in the form of selenocysteine (Sec) 2 residues in proteins (18).From the many studies on the functions of trace elements, metalloproteins emerged as one of the most diverse sets of proteins (19). Some protein families are strictly dependent on certain metals for their function (e.g. copper in cytochrome c oxidase and nickel in urease), whereas other families include both metal-dependent and metal-independent forms or evolved to use alternative metals (e.g. glyoxalase I binds nickel in Escherichia coli but zinc in humans and yeast) (20). In addition, orthologs of selenoproteins exist ...

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Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis

Cited by 30 publications

References 25 publications

Polyphenol oxidases in plants and fungi: Going places? A review

Polyphenol oxidases in plants and fungi: Going places? A review

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Comparative Genomics of Trace Element Dependence in Biology

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