A unique dual activity amino acid hydroxylase in Toxoplasma gondii.

The genome of the protozoan parasite Toxoplasma gondii was found to contain two genes encoding tyrosine hydroxylase; that produces L-DOPA. The encoded enzymes metabolize phenylalanine as well as tyrosine with substrate preference for tyrosine. Thus the enzymes catabolize phenylalanine to tyrosine an...

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Autores principales:	Elizabeth A Gaskell, Judith E Smith, John W Pinney, Dave R Westhead, Glenn A McConkey
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/23a920e4401849d9831e1872affd2616
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spelling	oai:doaj.org-article:23a920e4401849d9831e1872affd26162021-11-25T06:16:45ZA unique dual activity amino acid hydroxylase in Toxoplasma gondii.1932-620310.1371/journal.pone.0004801https://doaj.org/article/23a920e4401849d9831e1872affd26162009-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19277211/?tool=EBIhttps://doaj.org/toc/1932-6203The genome of the protozoan parasite Toxoplasma gondii was found to contain two genes encoding tyrosine hydroxylase; that produces L-DOPA. The encoded enzymes metabolize phenylalanine as well as tyrosine with substrate preference for tyrosine. Thus the enzymes catabolize phenylalanine to tyrosine and tyrosine to L-DOPA. The catalytic domain descriptive of this class of enzymes is conserved with the parasite enzyme and exhibits similar kinetic properties to metazoan tyrosine hydroxylases, but contains a unique N-terminal extension with a signal sequence motif. One of the genes, TgAaaH1, is constitutively expressed while the other gene, TgAaaH2, is induced during formation of the bradyzoites of the cyst stages of the life cycle. This is the first description of an aromatic amino acid hydroxylase in an apicomplexan parasite. Extensive searching of apicomplexan genome sequences revealed an ortholog in Neospora caninum but not in Eimeria, Cryptosporidium, Theileria, or Plasmodium. Possible role(s) of these bi-functional enzymes during host infection are discussed.Elizabeth A GaskellJudith E SmithJohn W PinneyDave R WestheadGlenn A McConkeyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 3, p e4801 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Elizabeth A Gaskell Judith E Smith John W Pinney Dave R Westhead Glenn A McConkey A unique dual activity amino acid hydroxylase in Toxoplasma gondii.
description	The genome of the protozoan parasite Toxoplasma gondii was found to contain two genes encoding tyrosine hydroxylase; that produces L-DOPA. The encoded enzymes metabolize phenylalanine as well as tyrosine with substrate preference for tyrosine. Thus the enzymes catabolize phenylalanine to tyrosine and tyrosine to L-DOPA. The catalytic domain descriptive of this class of enzymes is conserved with the parasite enzyme and exhibits similar kinetic properties to metazoan tyrosine hydroxylases, but contains a unique N-terminal extension with a signal sequence motif. One of the genes, TgAaaH1, is constitutively expressed while the other gene, TgAaaH2, is induced during formation of the bradyzoites of the cyst stages of the life cycle. This is the first description of an aromatic amino acid hydroxylase in an apicomplexan parasite. Extensive searching of apicomplexan genome sequences revealed an ortholog in Neospora caninum but not in Eimeria, Cryptosporidium, Theileria, or Plasmodium. Possible role(s) of these bi-functional enzymes during host infection are discussed.
format	article
author	Elizabeth A Gaskell Judith E Smith John W Pinney Dave R Westhead Glenn A McConkey
author_facet	Elizabeth A Gaskell Judith E Smith John W Pinney Dave R Westhead Glenn A McConkey
author_sort	Elizabeth A Gaskell
title	A unique dual activity amino acid hydroxylase in Toxoplasma gondii.
title_short	A unique dual activity amino acid hydroxylase in Toxoplasma gondii.
title_full	A unique dual activity amino acid hydroxylase in Toxoplasma gondii.
title_fullStr	A unique dual activity amino acid hydroxylase in Toxoplasma gondii.
title_full_unstemmed	A unique dual activity amino acid hydroxylase in Toxoplasma gondii.
title_sort	unique dual activity amino acid hydroxylase in toxoplasma gondii.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/23a920e4401849d9831e1872affd2616
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A unique dual activity amino acid hydroxylase in Toxoplasma gondii.

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