Asset Details
Do you wish to reserve the book?
A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii
Do you wish to request the book?
A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
A Unique Dual Activity Amino Acid Hydroxylase in Toxoplasma gondii
2009
Overview
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.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Animals
/ Biology
/ Cell Biology/Microbial Physiology and Metabolism
/ Cloning
/ E coli
/ Enzymes
/ Gene Expression Regulation, Developmental
/ Genes
/ Genomes
/ Genomics
/ Humans
/ Levodopa
/ Molecular Biology/Bioinformatics
/ Peptides
/ Phenylalanine Hydroxylase - genetics
/ Phenylalanine Hydroxylase - metabolism
/ Proteins
/ Protozoa
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
/ Rats
/ Recombinant Fusion Proteins - metabolism
/ RNA, Messenger - biosynthesis
/ Sequence Homology, Amino Acid
/ Toxoplasma - growth & development
/ Tyrosine
