3-Aminopiperid-2-one, an unusual metabolite in the urine of a patient with hyperammonaemia, hyperornithinaemia and homocitrullinuria

Fell, Vanessa; Pollitt, R. J.

doi:10.1016/0009-8981(78)90185-7

Cited by 12 publications

(6 citation statements)

References 9 publications

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“…First evidence that this conversion actually took place in humans stemmed from the observation of an additional ninhydrin-positive substance in the urine of patients suffering from hyperornithinemia. It could indeed be verified that the structure of this substance was 3-amino-piperidone, which is the chemical name of ornithine-lactam [3,4]. In the late 1970s, when this research was performed, the analytical techniques were incapable to detect ornithine-lactam in plasma, but it was suspected that it is also present in plasma.…”

Section: Introductionmentioning

confidence: 92%

Identification and quantification of the atypical metabolite ornithine-lactam in human plasma by liquid chromatography–tandem mass spectrometry (LC–MS/MS)

Martens‐Lobenhoffer

Becker²,

Freude³

et al. 2009

Journal of Chromatography B

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Section: Introductionmentioning

confidence: 92%

Identification and quantification of the atypical metabolite ornithine-lactam in human plasma by liquid chromatography–tandem mass spectrometry (LC–MS/MS)

Martens‐Lobenhoffer

Becker²,

Freude³

et al. 2009

Journal of Chromatography B

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“…The stoichiometry of 1.14 mol ATP hydrolyzed to AMP/mol Orn‐lactam24 indicates that the conversion to Orn‐lactam contributes 88% to Orn editing. Orn‐lactam constitutes 0.49% of Orn in human plasma62 and accumulates in patients with hyperornithinemia 63,64 …”

Section: Chemistry Of Editingmentioning

confidence: 99%

Quality control in tRNA charging

Jakubowski

2011

WIREs RNA

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Faithful translation of the genetic code during protein synthesis is fundamental to the growth, development, and function of living organisms. Aminoacyl-tRNA synthetases (AARSs), which define the genetic code by correctly pairing amino acids with their cognate tRNAs, are responsible for 'quality control' in the flow of information from a gene to a protein. When differences in binding energies of amino acids to an AARS are inadequate, editing is used to achieve high selectivity. Editing occurs at the synthetic active site by hydrolysis of noncognate aminoacyl-adenylates (pretransfer editing) and at a dedicated editing site located in a separate domain by deacylation of mischarged aminoacyl-tRNA (posttransfer editing). Access of nonprotein amino acids, such as homocysteine or ornithine, to the genetic code is prevented by the editing function of AARSs, which functionally partitions amino acids present in living cells into protein and nonprotein amino acids. Continuous editing is part of the tRNA aminoacylation process in living organisms from bacteria to human beings. Preventing mistranslation by the clearance of misactivated amino acids is crucial to cellular homeostasis and has a role in etiology of disease. Although there is a strong selective pressure to minimize mistranslation, some organisms possess error-prone AARSs that cause mistranslation. Elevated levels of mistranslation and the synthesis of statistical proteins can be beneficial for pathogens by increasing phenotypic variation essential for the evasion of host defenses.

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“…The cyclic B-lactam of omithine, 3-amino-2-piperidone ( Fig. 2) (30,106), is found in urine and, at lower concentrations, in plasma from patients with gyrate atrophy and other conditions associated with hyperomithinemia (reviewed in reference 144). However, the mechanism of its formation from ornithine is not known.…”

Section: Edmtng In Living Cellsmentioning

confidence: 99%