NDLI: A robust metallo-oxidase from the hyperthermophilic bacterium Aquifex aeolicus.

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A robust metallo-oxidase from the hyperthermophilic bacterium Aquifex aeolicus.

Content Provider	Semantic Scholar
Author	Fernandes, André Luíz Teixeira Soares, Cláudio M. Pereira, Manuela M. Huber, Robert Grass, Gregor Martins, Lígia O.
Copyright Year	2007
Abstract	The gene, Aquifex aeolicus AAC07157.1, encoding a multicopper oxidase (McoA) and localized in the genome as part of a putative copper-resistance determinant, has been cloned, over-expressed in Escherichia coli and the recombinant enzyme purified to homogeneity. The purified enzyme shows spectroscopic and biochemical characteristics typical of the well-characterized multicopper oxidase family of enzymes. McoA presents higher specificity (k(cat)/K(m)) for cuprous and ferrous ions than for aromatic substrates and is therefore designated as a metallo-oxidase. Addition of copper is required for maximal catalytic efficiency. A comparative model structure of McoA has been constructed and a striking structural feature is the presence of a methionine-rich region (residues 321-363), reminiscent of those found in copper homeostasis proteins. The kinetic properties of a mutant enzyme, McoADeltaP321-V363, deleted in the methionine-rich region, provide evidence for the key role of this region in the modulation of the catalytic mechanism. McoA has an optimal temperature of 75 degrees C and presents remarkable heat stability at 80 and 90 degrees C, with activity lasting for up to 9 and 5 h, respectively. McoA probably contributes to copper and iron homeostasis in A. aeolicus.
File Format	PDF HTM / HTML
DOI	10.1111/j.1742-4658.2007.05803.x
PubMed reference number	17451433
Journal	Medline
Volume Number	274
Issue Number	11
Alternate Webpage(s)	https://www.itqb.unl.pt/martins/index_files/FEBS_2007.pdf
Alternate Webpage(s)	http://www.itqb.unl.pt/martins/index_files/FEBS_2007.pdf
Alternate Webpage(s)	https://doi.org/10.1111/j.1742-4658.2007.05803.x
Journal	The FEBS journal
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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