Replacement of L-ornithine with L-lysine for urea cycle enzymes

Paik, Woon Ki; Pearson, Earl; Nochumson, Samuel; Kim, Sangduk

doi:10.1016/0020-711x(77)90139-2

Cited by 3 publications

(5 citation statements)

References 14 publications

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“…The synthesis of homocitrulline is enhanced when lysine or carbamylphosphate is accumulated because homocitrulline is formed from lysine and carbamylphosphate by ornithine transcarbamylase, EC 2.1.3.3 (Paik et al, 1977). Homocitrullinuria is observed in hyperlysinaemia (Ghadimi, 1983), saccharopinuria (Carson et al, 1968) and in hype~ornithinaemia, hyperammonaemia and homocitrullinuria (HHH) syndrome (Walser, 1983), citrullinaemia (Walser, 1983 and hyperargininaemia (Kato, et aL, 1988).…”

Section: Discussionmentioning

confidence: 97%

Homocitrullinuria and homoargininuria in lysinuric protein intolerance

Kato

Sano

Mizutani

1988

J of Inher Metab Disea

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A 14-year-old boy with lysinuric protein intolerance had increased plasma and urinary concentrations of homocitrulline and homoarginine. The accumulation of carbamylphosphate due to depleted supply of ornithine for the urea cycle may be responsible for the enhanced synthesis of homocitrulline and homoarginine. A renal clearance study showed that the tubular transport of homoarginine in the patient was impaired. In lysinuric protein intolerance, membrane transport system for homoarginine may be defective because it is presumed that homoarginine shares a common transport system with the dibasic amino acids.

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Section: Discussionmentioning

confidence: 97%

Homocitrullinuria and homoargininuria in lysinuric protein intolerance

Kato

Sano

Mizutani

1988

J of Inher Metab Disea

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“…Our patient already had high concentrations of homocitrulline and homoarginine in both plasma and urine under endogenous conditions and the accumulation of both amino acids was amplified by lysine loads. Homocitrulline is formed by carbamylation of lysine via ornithine transcarbamylase (EC 2.1.3.3) which mainly converts ornithine to citrulline (Paik et at., 1977). When carbamylphosphate accumulates as a result of retarded metabolism of ornithine through citrulline, homocitrulline formation must be enhanced as seen in the HHH syndrome (Valle and Simell, 1983) and citrullinaemia (Walser, 1983).…”

Section: Discussionmentioning

confidence: 99%

“…However, the appearance of homoargininuria in citrullinaemia due to argininosuccinate synthetase deficiency (Scott-Enmakpor et al, 1972;Matsuda et al, 1979) suggests that homoarginine is directly formed from lysine by transamidinating tysine via glycine transamidinase (EC 2.1.4.1) (Ryan et al, 1969). Inasmuch as arginine is used as a substrate in this metabolism and if homoarginine is metabolized to urea by arginase (Ryan et al, 1968;Paik et al, 1977), excess arginine and arginase deficiency may result in marked accumulation of homoarginine in hyperargininaemia. Increased plasma and cerebrospinal fluid concentrations of homoarginine have been reported in two patients with hyperargininaemia (Marescau et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Homocitrullinuria and homoargininuria in hyperargininaemia

Kato

Sano

Mizutani

et al. 1987

J of Inher Metab Disea

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“…The LKR pathway is assumed to be the primary pathway of lysine degradation in mammals, although this may not be true for avian species. Other enzymes are capable of oxidizing free lysine: lysyl oxidase (Trackman and Kagan, 1979), L-amino acid oxidase (Boulanger andOsteux, 1956, Struck andSizer, 1960), ornithine trancarbamoylase (Paik et al, 1977) and ornithine decarboxylase (Pegg and McGill, 1979).…”

Section: Lysine Degradation In Chickensmentioning

confidence: 99%

“…Lysine and ornithine only differ by one methylene group in their side chains, thus a few enzymes have been shown to act on lysine in-vitro. Paik et al (1977) demonstrated that ornithine transcarbamoylase can use lysine, instead of ornithine, to produce homocitrulline. However, this is unlikely to happen in-vivo since birds lack a functional urea cycle.…”

Section: Lysine Degradation In Chickensmentioning

confidence: 99%

Starvation-induced alterations in hepatic lysine metabolism in different families of rainbow trout (Oncorhynchus mykiss)

Higgins¹

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Starvation Induced Alterations in Hepatic Lysine Metabolism in Different Families of Rainbow Trout (Oncorhynchus mykiss) Angela Higgins This study focused on lysine catabolism by the lysine α-ketoglutarate reductase (LKR) pathway in rainbow trout (RBT). Selective breeding based on feed efficiency in 2 strains (A and B) of RBT generated 2 families within each strain. Eight fish from each of the four families were randomly allotted to individual tanks. Fish were fed until satiation for 3 wks at which time four fish within each family were randomly selected for 2 wks of starvation. After the 2 wk starvation, all fish were harvested. Hepatic in-vitro LKR activity and lysine oxidation (LOX) were measured as was LKR mRNA abundance. Strain A exhibited a 55% reduction in LKR transcripts compared to strain B pooled across both feeding levels (P<0.01). LKR mRNA was decreased (P<0.01) in starved versus fed fish. No differences were detected for LKR activity and LOX between fed and starved fish, between strains or between families. LKR transcripts were positively correlated to weight gain (p<0.01). I'd like to thank Dr. Blemings for all his support and votes of confidence through the uncharted territory of real-time PCR and library screening. Thanks to all my committee members, Drs. Wilson, Panaccione and Rexroad for their time and guidance, Dr. Scott Gahr for showing me numerous lab techniques and assisting in my first library screening, Dr. Jeff Silverstein at the National Center for Cool and Coldwater Aquaculture, for collaborating with our lab and answering all my questions about fish genetics, Dr. Jianbo Yao for his excellent suggestions for improving my library construction, Dr. George Seidel for his superb statistical analysis, Juanita Engles for performing the lysine oxidation experiments, my fellow graduate students, Beth Stinefelt and Aaron Keiss, and our work study, Erin Schenck.

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Replacement of L-ornithine with L-lysine for urea cycle enzymes

Cited by 3 publications

References 14 publications

Homocitrullinuria and homoargininuria in lysinuric protein intolerance

Homocitrullinuria and homoargininuria in lysinuric protein intolerance

Homocitrullinuria and homoargininuria in hyperargininaemia

Starvation-induced alterations in hepatic lysine metabolism in different families of rainbow trout (Oncorhynchus mykiss)

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