scholarly journals Characterization of cerebral microvasculature in transgenic mice with endothelium targeted over-expression of GTP-cyclohydrolase I

2015 ◽  
Vol 1625 ◽  
pp. 198-205 ◽  
Author(s):  
Anantha Vijay R. Santhanam ◽  
Livius V. d’Uscio ◽  
Zvonimir S. Katusic
Keyword(s):  
Transgenic Mice ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase ◽  
Over Expression ◽  
Cerebral Microvasculature

Characterization of transgenic mice with the expression of phenylalanine hydroxylase and GTP cyclohydrolase I in the skin

2005 ◽  
Vol 14 (7) ◽  
pp. 535-542 ◽  
Author(s):  
Rikke Christensen ◽  
Leena Alhonen ◽  
Jarmo Wahlfors ◽  
Maria Jakobsen ◽  
Thomas G. Jensen
Keyword(s):  
Transgenic Mice ◽  
Phenylalanine Hydroxylase ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase

Molecular Characterization of HPH-1: A Mouse Mutant Deficient in GTP Cyclohydrolase I Activity

1994 ◽  
Vol 203 (3) ◽  
pp. 1675-1681 ◽  
Author(s):  
M. Gutlich ◽  
I. Ziegler ◽  
K. Witter ◽  
B. Hemmens ◽  
L. Hultner ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Mouse Mutant ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase

Crystallization and preliminary crystallographic characterization of GTP cyclohydrolase I from Escherichia coli

1992 ◽  
Vol 226 (4) ◽  
pp. 1279-1281 ◽  
Author(s):  
Cornelia Schmid ◽  
Rudolf Ladenstein ◽  
Hartmut Luecke ◽  
Robert Huber ◽  
Adelbert Bacher
Keyword(s):  
Escherichia Coli ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase

scholarly journals Characterization of Mouse and Human GTP Cyclohydrolase I Genes

1995 ◽  
Vol 270 (17) ◽  
pp. 10062-10071 ◽  
Author(s):  
Hiroshi Ichinose ◽  
Tamae Ohye ◽  
Yoichi Matsuda ◽  
Tada-aki Hori ◽  
Nenad Blau ◽  
...  
Keyword(s):  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase

Enzymic characterization of Bacillus subtilis GTP cyclohydrolase I. Evidence for a chemical dephosphorylation of dihydroneopterin triphosphate

1995 ◽  
Vol 306 (2) ◽  
pp. 371-377 ◽  
Author(s):  
A De Saizieu ◽  
P Vankan ◽  
A P GM van Loon
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Folic Acid ◽  
Physiological Role ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase ◽  
Folate Biosynthesis

GTP cyclohydrolase I catalyses the first committing step in the biosynthesis of the pterin moiety of folic acid: conversion of GTP to dihydroneopterin triphosphate. GTP cyclohydrolase I of Bacillus subtilis was purified to homogeneity and shown to have a homo-octameric structure. The enzyme had an apparent Km for GTP of 4 microM and, in the absence of cations, a Vmax. of 80 nmol/min per mg of protein. K+ ions moderately increased its Vmax., whereas UTP and Ca2+ and Mg2+ ions drastically increased its Km for GTP. Dihydrofolate and other products of the folate and tetrahydrobiopterin pathways did not inhibit GTP cyclohydrolase I. In addition to their effect on the enzyme activity, Ca2+ and Mg2+ ions catalysed the chemical dephosphorylation of dihydroneopterin triphosphate to non-cyclic dihydroneopterin monophosphate, the substrate for the phosphomonoesterase reaction in folate biosynthesis. This dephosphorylation was specific and did not require the action of a phosphatase. We suggest a physiological role for Ca2+ ions and UTP in regulation of folate biosynthesis at the levels of GTP cyclohydrolase I and dephosphorylation of dihydroneopterin triphosphate.

scholarly journals Biochemical and functional characterization of Plasmodium falciparum GTP cyclohydrolase I

2014 ◽  
Vol 13 (1) ◽  
pp. 150 ◽  
Author(s):  
Krittikorn Kümpornsin ◽  
Namfon Kotanan ◽  
Pornpimol Chobson ◽  
Theerarat Kochakarn ◽  
Piyaporn Jirawatcharadech ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Functional Characterization ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase
Sign in / Sign up

Export Citation Format

Share Document