Human Liver 6-Pyruvoyl-Tetrahydropterin Synthase: Expression of the cDNA, Purification and Preliminary Characterization of the Recombinant Protein View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1993

AUTHORS

Beat Thöny , Walter Leimbacher , Nenad Blau , Claus W. Heizmann , Daniel Bürgisser

ABSTRACT

Tetrahydrobiopterin (BH4) is the coenzyme for several monooxygenases such as the aromatic amino acid hydroxylases, the glycerol ether monooxygenase, and the nitric oxide synthases1,2. A lack of BH4 leads to hyperphenylalaninemia and a deficiency of biogenic amine neurotransmitters, which are responsible for severe mental retardation3. The most common form, where BH4 biosynthesis is impaired, is a deficiency in 6-pyruvoyl-tetrahydropterin synthase (PTPS). PTPS catalyzes the second step in the BH4 biosynthetic pathway, the conversion of 7,8-dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin. This triphosphate eliminating reaction requires Mg2+ as a cofactor. As a means to better characterize biochemically the PTPS, we recently cloned the human liver cDNA4. Expression of the recombinant enzyme in E. coli allowed us to isolate and purify the active PTPS in large amounts. This article describes the overproduction and purification, and gives a preliminary characterization of some physical properties of the recombinant human enzyme. More... »

PAGES

187-90

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-2960-6_37

DOI

http://dx.doi.org/10.1007/978-1-4615-2960-6_37

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004773561

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8304107


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