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Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase
Archives of Biochemistry and Biophysics, 1956Abstract A transamidinase which catalyzes the reversible reaction, l -arginine + glycine guanidinoacetic acid + l -ornithine, has been obtained from hog kidney and purified about 80-fold. Ornithine exerts a strong product inhibition which influences the reaction rates; conditions are given for obtaining initial rates.
S, RATNER, O, ROCHOVANSKY
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Cellular bioenergetics of guanidinoacetic acid: the role of mitochondria
Journal of Bioenergetics and Biomembranes, 2015Guanidinoacetic acid (GAA) is a natural precursor of creatine, and a possible substrate for the creatine kinase (CK) enzyme system, serving as a creatine mimetic. Its direct role in cellular bioenergetics has been confirmed in several studies, however GAA utilization by CK seems to be a second-rate as compared to creatine, and compartment-dependent ...
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Urinary Guanidinoacetic Acid Excretion in Gentamicin Nephrotoxicity
1985Bonas et al. reported in 1963 that four patients with kidney disease were shown to excrete markedly decreased amounts of guanidinoacetic acid (GAA) in their urine1.
Hideo Itabashi +2 more
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Dietary guanidinoacetic acid increases brain creatine levels in healthy men
Nutrition, 2017Guanidinoacetic acid (GAA) is an experimental dietary additive that might act as a creatine source in tissues with high-energy requirements. In this case study, we evaluated brain levels of creatine in white matter, gray matter, cerebellum, and thalamus during 8 wk oral GAA administration in five healthy men and monitored the prevalence and severity of
Ostojić, Sergej +4 more
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Biosynthesis of guanidinoacetic acid. II. Mechanism of amidine group transfer
Archives of Biochemistry and Biophysics, 1956Abstract Purified transamidinase has been shown to catalyze the transfer of the amidine group from the donors arginine, guanidinoacetic acid, and canavanine to the acceptors glycine, ornithine, and canaline. All possible donor-acceptor pair combinations can interact at appreciable rates.
S, RATNER, O, ROCHOVANSKY
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Molecular Genetics and Metabolism, 2001
Guanidinoacetate methyltransferase (GAMT) deficiency (McKusick 601240), an inborn error of creatine biosynthesis, is characterized by creatine depletion and accumulation of guanidinoacetate (GAA) in the brain. Treatment by oral creatine supplementation had no effect on the intractable seizures.
A, Schulze +3 more
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Guanidinoacetate methyltransferase (GAMT) deficiency (McKusick 601240), an inborn error of creatine biosynthesis, is characterized by creatine depletion and accumulation of guanidinoacetate (GAA) in the brain. Treatment by oral creatine supplementation had no effect on the intractable seizures.
A, Schulze +3 more
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Biosynthesis of Guanidinoacetic Acid in Isolated Rat Hepatocytes
1985Guanidinoacetic acid (GAA), a precursor of creatine, is formed from arginine and glycine by transamidinationl. GAA formation in rat is not detected in liver homogenates2 or in isolated perfused livers3. Therefore, creatine synthesis in rat liver is regulated by the activity of transamidinase in the kidney4.
Kazumasa Aoyagi +6 more
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IIC - International Review of Intellectual Property and Competition Law, 2023
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An alternative mechanism for guanidinoacetic acid to affect methylation cycle
Medical Hypotheses, 2014Guanidinoacetic acid (also known as glycocyamine; GAA) is an endogenous substance which occurs in humans and plays a central role in the biosynthesis of creatine. The formation of creatine from GAA consumes methyl groups, and increases production of homocysteine. GAA may have the potential to stimulate insulin secretion.
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Nephron, 1993
Most chronic renal failure (CRF) patients show low serum concentrations of guanidinoacetic acid (GAA). In this study, the author investigated the impaired metabolism of GAA in CRF focusing on the transformation of arginine (Arg) to GAA by analyzing CRF rabbits using 14C-Arg.
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Most chronic renal failure (CRF) patients show low serum concentrations of guanidinoacetic acid (GAA). In this study, the author investigated the impaired metabolism of GAA in CRF focusing on the transformation of arginine (Arg) to GAA by analyzing CRF rabbits using 14C-Arg.
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