Involvement of a novel copper chaperone in tyrosinase activity and melanin synthesis in Marinomonas mediterranea

López-Serrano, Daniel; Solano, Francisco; Sánchez-Amat, Antonio

doi:10.1099/mic.0.2007/006833-0

Cited by 35 publications

(21 citation statements)

References 39 publications

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“…Enzyme activities were determined according to a modified absorption assay [44], [45]. Protein concentrations were 0.25 mg/ml and 0.1 mg/ml for monophenolase and diphenolase activity experiments, respectively.…”

Section: Methodsmentioning

confidence: 99%

Albinism-Causing Mutations in Recombinant Human Tyrosinase Alter Intrinsic Enzymatic Activity

Dolinska

Kovaleva²,

Backlund

et al. 2014

PLoS ONE

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BackgroundTyrosinase (TYR) catalyzes the rate-limiting, first step in melanin production and its gene (TYR) is mutated in many cases of oculocutaneous albinism (OCA1), an autosomal recessive cause of childhood blindness. Patients with reduced TYR activity are classified as OCA1B; some OCA1B mutations are temperature-sensitive. Therapeutic research for OCA1 has been hampered, in part, by the absence of purified, active, recombinant wild-type and mutant human enzymes.Methodology/Principal FindingsThe intra-melanosomal domain of human tyrosinase (residues 19–469) and two OCA1B related temperature-sensitive mutants, R422Q and R422W were expressed in insect cells and produced in T. ni larvae. The short trans-membrane fragment was deleted to avoid potential protein insolubility, while preserving all other functional features of the enzymes. Purified tyrosinase was obtained with a yield of >1 mg per 10 g of larval biomass. The protein was a monomeric glycoenzyme with maximum enzyme activity at 37°C and neutral pH. The two purified mutants when compared to the wild-type protein were less active and temperature sensitive. These differences are associated with conformational perturbations in secondary structure.Conclusions/SignificanceThe intramelanosomal domains of recombinant wild-type and mutant human tyrosinases are soluble monomeric glycoproteins with activities which mirror their in vivo function. This advance allows for the structure – function analyses of different mutant TYR proteins and correlation with their corresponding human phenotypes; it also provides an important tool to discover drugs that may improve tyrosinase activity and treat OCA1.

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Section: Methodsmentioning

confidence: 99%

Albinism-Causing Mutations in Recombinant Human Tyrosinase Alter Intrinsic Enzymatic Activity

Dolinska

Kovaleva²,

Backlund

et al. 2014

PLoS ONE

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“…This proteinspecific chaperone for copper uptake seems characteristic of bacteria, since higher organisms rely on general homeostasis systems. 57,58 The genetic organization of plant PPOs (Figure 2) is more complicated and often reveals the presence of multiple gene copies in the genome. They generally do not present introns.…”

Section: G E N E T I C I N F O R M a T I O N A N D G E N E O R G A Nmentioning

confidence: 99%

Structure, Spectroscopy, and Function of Tyrosinase; Comparison with Hemocyanin and Catechol Oxidase

Tepper¹,

Lonardi²,

Bubacco³

et al. 2004

Handbook of Metalloproteins

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This article deals with tyrosinase, an enzyme that converts monophenols into diphenols and subsequently into orthoquinones with concomitant use of molecular oxygen as the source of oxygen atoms and oxidizing equivalents. The enzyme occurs widespread in nature. Its active center consists of a dinuclear copper site. The occurrence of tyrosinases and their biological function is reviewed. Information about primary (aa sequence, genetic organization), secondary, and tertiary structures is reviewed and, where appropriate, compared with similar information about related proteins with a dinuclear Cu site (hemocyanins, catechol oxidase). Methods to produce and purify tyrosinase are reviewed. Spectroscopic studies (optical; EPR, NMR, EXAFS) are reviewed in relation to the enzyme mechanism, which is discussed at the end of the article.

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“…There was one copy of an operon responsible for melanin synthesis from L -tyrosine [6]. The genes forming part of this operon are Marme_3962, encoding a tyrosinase (PpoB1), and Marme_3961, which encodes a membrane protein (PpoB2) involved in copper delivery to the tyrosinase [44]. BLAST-based searches using the sequence of this M. mediterranea tyrosinase against the Proteobacteria deposited in IMG as of Sept 2011 retrieved only 18 hits at a cutoff value of <e -20 .…”

Section: Insights From Genome Sequencementioning

confidence: 99%

Complete genome sequence of the melanogenic marine bacterium Marinomonas mediterranea type strain (MMB-1T).

Lucas-Elı́o

Goodwin

Woyke

et al. 2012

Stand. Genomic Sci.

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Marinomonas mediterranea MMB-1 T Solano & Sanchez-Amat 1999 belongs to the family Oceanospirillaceae within the phylum Proteobacteria . This species is of interest because it is the only species described in the genus Marinomonas to date that can synthesize melanin pigments, which is mediated by the activity of a tyrosinase. M. mediterranea expresses other oxidases of biotechnological interest, such as a multicopper oxidase with laccase activity and a novel L-lysine-epsilon-oxidase. The 4,684,316 bp long genome harbors 4,228 protein-coding genes and 98 RNA genes and is a part of the G enomic E ncyclopedia of B acteria and A rchaea project.

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Involvement of a novel copper chaperone in tyrosinase activity and melanin synthesis in Marinomonas mediterranea

Cited by 35 publications

References 39 publications

Albinism-Causing Mutations in Recombinant Human Tyrosinase Alter Intrinsic Enzymatic Activity

Albinism-Causing Mutations in Recombinant Human Tyrosinase Alter Intrinsic Enzymatic Activity

Structure, Spectroscopy, and Function of Tyrosinase; Comparison with Hemocyanin and Catechol Oxidase

Complete genome sequence of the melanogenic marine bacterium Marinomonas mediterranea type strain (MMB-1T).

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