The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Biochemical studies on the enzymatic deficiencies in hereditary tyrosinemia
Abstract
Experiments are described on the effects of succinylacetone and fumarylacetoacetate on delta-aminolevulinic acid dehydratase, methionine adenosyltransferase and p-OH-phenylpyruvate dioxygenase. delta-Aminolevulinic acid dehydratase from human erythrocytes is inhibited non-competitively by succinylacetone (Ki 0.03 mumol/l) and by fumarylacetoacetate (Ki 0.06 mumol/l). The inhibition by succinylacetone is not prevented by dithiothreitol, but the inhibition by fumarylacetoacetate is not observed if dithiothreitol is present. Methionine adenosyltransferase, partially purified from rabbit liver, is not inhibited by succinylacetone but is inhibited by fumarylacetoacetate: 69% inhibition is observed at 1 mmol/l. Human liver p-OH-phenylpyruvate dioxygenase is not inhibited by succinylacetone or fumarylacetoacetate. It is concluded that secondary enzyme deficiencies observed in hereditary tyrosinemia (delta-aminolevulinic acid dehydratase, methionine adenosyl transferase) are the result of inhibition by succinylacetone and fumarylacetoacetate, accumulating as a result of a primary deficiency of fumarylacetoacetase.
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Presence of SA is diagnostic for HT1.
“and its presence is diagnostic for the disease (2, 8, 9).”
From Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal models for the human genetic disorder hereditary tyrosinemia type 1 (2001) · cites this paper as [2]
SA accumulation is the indirect result of the complete or incomplete block of the FAH enzyme, and SA accumulation has been linked to certain pathological aspects of the disorder.
“SA accumulation is thus the indirect result of the complete or incomplete block of the FAH enzyme, and SA accumulation has been linked to certain pathological aspects of the disorder (1, 2, 37, 38).”
From Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal models for the human genetic disorder hereditary tyrosinemia type 1 (2001) · cites this paper as [2]
FAH deficiency results in the accumulation of fumarylacetoacetate, maleylacetoacetate, and succinylacetone in the liver and kidney, which is believed to be responsible for certain pathological aspects of HT1.
“FAH deficiency results in the accumulation of fumarylacetoacetate, maleylacetoacetate, and succinylacetone (SA) in the liver and kidney, which is believed to be responsible for certain pathological aspects of the disorder (2, 3).”
From Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal models for the human genetic disorder hereditary tyrosinemia type 1 (2001) · cites this paper as [2]
Citations
Cites
On the enzymic defects in hereditary tyrosinemia.
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Inhibition of delta-aminolevulinic acid dehydrase by 4,6-dioxoheptanoic acid.
Tschudy, D. P., Hess, R. A., & Frykholm, B. C. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68717-x · Cited by 113
Excretion of δ-aminolevulinic acid in hereditary tyrosinemia
Gentz, J., Johansson, S., Lindblad, B., Lindstedt, S., & Zetterström, R. (1969) · Clinica Chimica Acta · doi:10.1016/0009-8981(69)90040-0 · Cited by 69
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Research works printed but not linked: 25
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Sorted by citations
Hereditary tyrosinemia type I: Self-induced correction of the fumarylacetoacetase defect
Kvittingen, E. A., Rootwelt, H., Brandtzaeg, P., Bergan, A., & Berger, R. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116393 · Cited by 102
Self-citationAponte, J. L., Sega, G. A., Hauser, L. J., Dhar, M. S., Withrow, C. M., Carpenter, D. A., Rinchik, E. M., Culiat, C. T., & Johnson, D. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.641 · Cited by 68
Berger, R., Van Faassen, H., Taanman, J. W., De Vries, H., & Agsteribbe, E. (1987) · Pediatric Research · doi:10.1203/00006450-198710000-00005 · Cited by 37
Self-citation
Metadata
- Authors
- Berger, R., van Faassen, H., & Smith, G. P. A.
- Affiliations
- University of Groningen (NL)
- Corresponding author
- Berger, R.
- Venue
- Clinica Chimica Acta
- Publisher
- Elsevier BV
- Published
- 1983-10
- Volume
- 134
- Issue
- 1-2
- Pages
- 129-141
- ISSN
- 0009-8981 (ISSN-L)
- OpenAlex
- W2071728697
- Cited by
- 45
- References
- 3
- Citations by year
- 2022: 1 · 2021: 1 · 2018: 2 · 2016: 1 · 2014: 1 · 2012: 2
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Clinica Chimica Acta (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Keywords
- hereditary tyrosinemia, succinylacetone, delta-aminolevulinic acid dehydratase, methionine adenosyltransferase, enzyme inhibition, non-competitive inhibition, dithiothreitol, erythrocytes, liver
- MeSH terms
- Amino Acid Metabolism, Inborn Errors, Porphobilinogen Synthase, Animals, Humans, Kinetics, Methionine Adenosyltransferase, Rabbits, Tyrosine, 4-Hydroxyphenylpyruvate Dioxygenase
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