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Diss Factsheets
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EC number: 206-058-5 | CAS number: 298-12-4
- Life Cycle description
- Uses advised against
- Endpoint summary
- Appearance / physical state / colour
- Melting point / freezing point
- Boiling point
- Density
- Particle size distribution (Granulometry)
- Vapour pressure
- Partition coefficient
- Water solubility
- Solubility in organic solvents / fat solubility
- Surface tension
- Flash point
- Auto flammability
- Flammability
- Explosiveness
- Oxidising properties
- Oxidation reduction potential
- Stability in organic solvents and identity of relevant degradation products
- Storage stability and reactivity towards container material
- Stability: thermal, sunlight, metals
- pH
- Dissociation constant
- Viscosity
- Additional physico-chemical information
- Additional physico-chemical properties of nanomaterials
- Nanomaterial agglomeration / aggregation
- Nanomaterial crystalline phase
- Nanomaterial crystallite and grain size
- Nanomaterial aspect ratio / shape
- Nanomaterial specific surface area
- Nanomaterial Zeta potential
- Nanomaterial surface chemistry
- Nanomaterial dustiness
- Nanomaterial porosity
- Nanomaterial pour density
- Nanomaterial photocatalytic activity
- Nanomaterial radical formation potential
- Nanomaterial catalytic activity
- Endpoint summary
- Stability
- Biodegradation
- Bioaccumulation
- Transport and distribution
- Environmental data
- Additional information on environmental fate and behaviour
- Ecotoxicological Summary
- Aquatic toxicity
- Endpoint summary
- Short-term toxicity to fish
- Long-term toxicity to fish
- Short-term toxicity to aquatic invertebrates
- Long-term toxicity to aquatic invertebrates
- Toxicity to aquatic algae and cyanobacteria
- Toxicity to aquatic plants other than algae
- Toxicity to microorganisms
- Endocrine disrupter testing in aquatic vertebrates – in vivo
- Toxicity to other aquatic organisms
- Sediment toxicity
- Terrestrial toxicity
- Biological effects monitoring
- Biotransformation and kinetics
- Additional ecotoxological information
- Toxicological Summary
- Toxicokinetics, metabolism and distribution
- Acute Toxicity
- Irritation / corrosion
- Sensitisation
- Repeated dose toxicity
- Genetic toxicity
- Carcinogenicity
- Toxicity to reproduction
- Specific investigations
- Exposure related observations in humans
- Toxic effects on livestock and pets
- Additional toxicological data
Specific investigations: other studies
Administrative data
- Endpoint:
- specific investigations: other studies
- Type of information:
- other: Literature data
- Adequacy of study:
- other information
- Study period:
- 2000
- Rationale for reliability incl. deficiencies:
- other: Literature data
Data source
Reference
- Reference Type:
- publication
- Title:
- Oxalate synthesis in mammals: Properties and subcellular distribution of serine:pyruvate / alanine:glyoxylate aminotransferase in the liver
- Author:
- Ichiyama R., Xue H.H., Oda T., Uchida C., sugiyama T., Maeda-Nakai E., Sato K., Nagai E., Watanabe S., Takayama T.
- Year:
- 2 000
- Bibliographic source:
- Molecular Urol. 4(4), 333-340
Materials and methods
- Principles of method if other than guideline:
- The aim of this study was to describe oxalate production in mammals from the perspective of the properties and the subcelllular distribution of serine:pyruvate/alanine:glyoxylate aminotransferase (SPT/AGT).
- GLP compliance:
- not specified
Test material
- Reference substance name:
- Automatically generated during migration to IUCLID 6, no data available
- IUPAC Name:
- Automatically generated during migration to IUCLID 6, no data available
- Details on test material:
- Glyoxylate
Constituent 1
Test animals
- Species:
- other: mammal
Results and discussion
- Details on results:
- Primary hyperoxaluria Type 1 (PH1) is caused by a functional deficiency of a liver enzyme, serine:pyruvate/alanine:glyoxylate aminotrasferase (SPT/AGT), which catalyses transamination between L-serine or L-alanine as an amino acid substrate and glyoxylate or pyruvate as an alpha-keto acid substrate.
A high affinity for glyoxylate is a notable feature of this enzyme, suggesting a role in glyoxylate metabolism in vivo.
Another conspicuous feature of SPT/AGT is it species-specific and food habit-dependent subcellular distribution. Thus, the enzyme is located in peroxisomes in herbivores and man, largely in mitochondria in carnivores and in both the organelles in rodents.
The mechanism of the species-specific dual organelle localization of SPT/AGT is either transcription of the gene from two different start sites or loss of the upstream translation initiation ATG codon by mutations. It appears that the mitochondrial versus peroxisomal distribution of SPT/AGT in different animal species is indispensable in meeting the metabolic needs caused by their respective food habits.
As for the peroxisomal localization, glycolate is contained in plants much more than in animal tissues and when ingested, it is converted to glyoxylate, an immediate precursor of oxalate, in liver peroxisomes.
Therefore, peroxisomal localization of SPT/AGT may be indispensable for herbivore to convert the glyoxylate formed in peroxisomes into glycine in situ rather than forming oxalate. On the other hand, recent studies showed that SPT/AGT contributed substantially to serine metabolism in rabbit, human and dog livers; i.e., irrespective of its mitochondrial or peroxisomal localization.
Thus, the mitochondrial localization of SPT/AGT was not a prerequisite for the metabolism of L-serine. Another source of Glyoxylate is the metabolism of L-hyroxyproline and in this case, the enzyme responsible for the glyoxylate formation has been reported to be a mitochondrial matrix enzyme.
Collagen accounts for about 30 % of total animal proteins and contains about 13 % (w/w) hydroxyproline. It is therefore possible that both mitochondrial and peroxisomal SPT/AGT contribute to the metabolism of glyoxylate and serine, but the subcellular site for glyoxylate metabolism is different in herbivores and carnivores.
Applicant's summary and conclusion
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