Partial Purification and Characterization of GTP Cyclohydrolase I from Spinach Leaves

Sohta, Yasuko; Ohta, Tomoko; Masada, Masahiro

doi:10.1007/978-1-4615-2960-6_31

Yasuko Sohta⁴,
Tomoko Ohta⁴ &
Masahiro Masada⁴

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 338))

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Abstract

GTP cyclohydrolase I catalyzes the formation of dihydroneopterin triphosphate and formate from GTP. This reaction is the first step in the biosynthetic pathways of cofactors such as tetrahydrofolate and tetrahydrobiopterin. GTP cyclohydrolase I has been purified and well characterized in several bacterial species such as Escherichia coli (1), Lactobacillus plantarum (2), Comamoanus sp. (3), Seratia indica (4), and Bacillus stearothermophilus(5). There were also several attempts which involved purification and characterization of this\ enzyme from animals including human(6), chicken(7), rat(8), mouse(9), and Drosophila (10).

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Authors and Affiliations

Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University, Matsudo 648, Chiba, Japan
Yasuko Sohta, Tomoko Ohta & Masahiro Masada

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Yasuko Sohta
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Tomoko Ohta
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Masahiro Masada
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Editors and Affiliations

Dept of Pharmacology College of Medicine, Universily of South Alabama, Mobile, AL, 36688, USA
June E. Ayling
Dept. of Biochemistry College of Medicine, University of South Alabama, Mobile, AL, 36688, USA
M. Gopal Nair
College of Medicine, Universily of South Alabama, Mobile, AL, 36688, USA
Charles M. Baugh

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Sohta, Y., Ohta, T., Masada, M. (1993). Partial Purification and Characterization of GTP Cyclohydrolase I from Spinach Leaves. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_31

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DOI: https://doi.org/10.1007/978-1-4615-2960-6_31
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6287-6
Online ISBN: 978-1-4615-2960-6
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