GO:0047315 L-kynurenine:glyoxylate transaminase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0047315 defines the molecular function L-kynurenine:glyoxylate transaminase activity, which catalyzes the reversible transfer of an amino group from L-kynurenine to glyoxylate, yielding 4-(2-aminophenyl)-2,4-dioxobutanoate and glycine.
• In humans, this activity is carried by the peroxisomal enzyme alanine-glyoxylate aminotransferase (AGXT), which is identical to serine-pyruvate aminotransferase and kynurenine-glyoxylate aminotransferase.
• The same catalytic activity is found in insects such as Aedes aegypti, where it is performed by 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and is proposed to detoxify reactive kynurenine pathway intermediates [2,4,6].
• The reaction is pyridoxal 5'-phosphate (PLP)-dependent and follows a classic ping-pong bi-bi mechanism typical of fold-type I aminotransferases [1,6].
• Loss or imbalance of this activity perturbs tryptophan-kynurenine flux and glyoxylate detoxification, linking it to hyperoxaluria, neurotoxicity, and insect vector biology [1,2,5].
• CRISPR knockout, point-mutation, knock-in, and overexpression models enable causal dissection of this enzyme's role in metabolism and disease [1,2,6].
Description
L-kynurenine:glyoxylate transaminase activity (GO:0047315) is a molecular function that catalyzes the reaction L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine. This transamination reaction sits at the intersection of two important metabolic routes: the kynurenine pathway of tryptophan degradation and the glyoxylate detoxification pathway. The enzyme responsible was first purified and crystallized from human liver and shown to be identical to alanine-glyoxylate aminotransferase (AGXT) and serine-pyruvate aminotransferase. Because the same protein can accept multiple amino donors, its activity is central to nitrogen handling and to the removal of toxic carbonyl compounds [1,7]. Researchers care about GO:0047315 because it connects amino acid metabolism to disease. In humans, AGXT mutations cause primary hyperoxaluria type 1, a disorder in which glyoxylate accumulates and is converted to oxalate, leading to kidney stones and renal failure. In insects, the orthologous activity detoxifies 3-hydroxykynurenine, a reactive intermediate of tryptophan catabolism that can cause oxidative stress and neuronal damage [2,4,6]. Thus, the same catalytic function serves different physiological roles across species, making it a compelling target for comparative biochemistry and drug discovery [2,5]. From a methodological standpoint, GO:0047315 is a tractable model for studying PLP-dependent aminotransferases. Its substrates and products are measurable by HPLC, mass spectrometry, and coupled enzyme assays, and its structural basis has been resolved by X-ray crystallography [1,6]. This makes it an excellent entry point for CRISPR-based functional genomics, where knockout and knock-in models can reveal how a single catalytic activity shapes whole-organism metabolism [1,2].
L-kynurenine:glyoxylate transaminase activity At A Glance
| GO ID | GO:0047315 |
|---|---|
| GO term | L-kynurenine:glyoxylate transaminase activity |
| Ontology | molecular_function |
| Synonym | kynurenine--glyoxylate aminotransferase activity; kynurenine-glyoxylate aminotransferase activity; kynurenine-glyoxylate transaminase activity; L-kynurenine:glyoxylate aminotransferase (cyclizing) |
| Major function | Catalyzes the transfer of an amino group from L-kynurenine to glyoxylate, producing 4-(2-aminophenyl)-2,4-dioxobutanoate and glycine |
| Cofactor | Pyridoxal 5'-phosphate (PLP) |
| Reaction direction | Reversible transamination |
| Human enzyme | AGXT (alanine-glyoxylate aminotransferase), identical to serine-pyruvate aminotransferase and kynurenine-glyoxylate aminotransferase |
| Subcellular location | Peroxisome (for human AGXT) |
What Is GO:0047315?
GO:0047315, L-kynurenine:glyoxylate transaminase activity, is defined by the Gene Ontology as the catalysis of the reaction L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine. In other words, the enzyme takes an amino group from L-kynurenine and hands it to glyoxylate, producing glycine and a keto acid derivative of kynurenine. This is a transamination reaction, and it requires pyridoxal 5'-phosphate as a cofactor. The activity is synonymous with kynurenine-glyoxylate aminotransferase, kynurenine-glyoxylate transaminase, and L-kynurenine:glyoxylate aminotransferase (cyclizing). In humans, the enzyme that displays this activity is AGXT, which also acts on alanine and serine with glyoxylate or pyruvate as acceptors.
Why Is L-kynurenine:glyoxylate transaminase activity Important in Cell Biology?
GO:0047315 matters because it links two metabolic pathways that are individually critical for health: the kynurenine pathway, which produces neuroactive and immunomodulatory metabolites, and the glyoxylate pathway, which when impaired causes oxalate overproduction and kidney damage. The enzyme carrying this activity, AGXT, is the causative gene in primary hyperoxaluria type 1, and its ability to use kynurenine as an amino donor may influence the balance of kynurenine pathway metabolites. In insects, the same activity is a detoxification mechanism for 3-hydroxykynurenine, a reactive compound implicated in neurodegeneration and oxidative stress [2,4,6]. Understanding this activity therefore has implications for human inherited metabolic disease, neurobiology, and vector control [2,5].
• Provides a route for glyoxylate detoxification by converting it to glycine, preventing oxalate accumulation.
• Connects tryptophan catabolism to amino acid metabolism through the use of L-kynurenine as an amino donor.
• Loss of AGXT function causes primary hyperoxaluria type 1, a severe kidney disease.
• In mosquitoes, the orthologous activity detoxifies 3-hydroxykynurenine and may protect against oxidative stress [2,4,6].
• Serves as a model PLP-dependent aminotransferase for studying enzyme mechanism and substrate specificity [1,6].
• Is a potential target for insecticide development by disrupting tryptophan metabolism in pests.
• Contributes to the regulation of kynurenine pathway flux, which is linked to neuroinflammation and neurodegeneration [2,3].
• Enables comparative studies of metabolic enzyme evolution across mammals and insects [2,4,7].
• Provides a functional readout for CRISPR screens targeting metabolic enzymes [1,2].
• Its peroxisomal localization ties it to organelle-specific metabolism and protein targeting.
Molecular Mechanism of L-kynurenine:glyoxylate transaminase activity
Substrate recognition and binding
In simple terms: The enzyme grabs L-kynurenine and glyoxylate and holds them in place.
The enzyme binds L-kynurenine and glyoxylate in a bipartite active site. L-kynurenine is positioned so that its amino group faces the PLP cofactor, while glyoxylate is oriented to accept the amino group. In human AGXT, the active site accommodates multiple amino donors including alanine, serine, and kynurenine, reflecting broad substrate tolerance. In Aedes aegypti, the enzyme prefers 3-hydroxykynurenine and alanine, but also uses glyoxylate as an amino acceptor [2,4].
PLP-dependent transamination
In simple terms: A vitamin B6 derivative shuttles the amino group from one molecule to another.
The reaction follows a ping-pong bi-bi mechanism. First, the amino group of L-kynurenine is transferred to pyridoxal 5'-phosphate (PLP), forming pyridoxamine 5'-phosphate and releasing the keto acid 4-(2-aminophenyl)-2,4-dioxobutanoate. Second, the amino group is transferred from pyridoxamine 5'-phosphate to glyoxylate, yielding glycine and regenerating PLP. This mechanism is characteristic of fold-type I aminotransferases and is supported by structural studies of Aedes aegypti alanine glyoxylate aminotransferase.
Catalytic cycle and product release
In simple terms: The enzyme releases the products and resets itself for the next round.
After the second half-reaction, glycine and the kynurenine-derived keto acid are released. The enzyme returns to its resting PLP-bound state. The reaction is reversible, so the enzyme can also synthesize L-kynurenine from the keto acid and glycine, although the physiological direction depends on substrate concentrations. In insects, the reaction is proposed to proceed toward detoxification, converting reactive 3-hydroxykynurenine to a less toxic product.
Structural features and cofactor binding
In simple terms: The enzyme's 3D shape holds the cofactor and substrates in the right orientation.
Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase reveal a homodimer with each subunit containing a PLP-binding domain and a small domain that gates substrate access. The human AGXT enzyme is also a homodimer and requires PLP for stability and activity. Key residues in the active site form hydrogen bonds with the cofactor and with the carboxylate groups of substrates, ensuring proper orientation for catalysis.
Regulation by substrate availability and inhibitors
In simple terms: How much of the reaction happens depends on what the cell feeds the enzyme and what blocks it.
The activity is regulated by the availability of L-kynurenine and glyoxylate, which in turn depend on upstream enzymes of tryptophan catabolism and glyoxylate metabolism. Insecticides and xenobiotics can alter the activity of tryptophan-metabolizing enzymes in rats, suggesting that environmental chemicals may modulate this pathway. In humans, mutations in AGXT that impair PLP binding reduce catalytic activity and cause disease.
Key Genes Involved in GO:0047315 L-kynurenine:glyoxylate transaminase activity
The following genes and proteins are directly or functionally linked to L-kynurenine:glyoxylate transaminase activity (GO:0047315) based on published biochemical and genetic studies.
| Gene | Major Role | Research Relevance |
|---|---|---|
| AGXT | Human alanine-glyoxylate aminotransferase; catalyzes L-kynurenine:glyoxylate transamination and glyoxylate detoxification | Causative gene in primary hyperoxaluria type 1; model for peroxisomal enzyme targeting |
| AGXT2 | Mitochondrial alanine-glyoxylate aminotransferase 2; related aminotransferase with overlapping substrate specificity | Potential compensatory enzyme in glyoxylate metabolism; less studied for kynurenine transamination |
| Ae-AGXT | Aedes aegypti alanine glyoxylate aminotransferase; detoxifies 3-hydroxykynurenine | Target for mosquito control; structural model for the enzyme family [2,6] |
| Dm-SPAT | Drosophila serine pyruvate aminotransferase; related insect enzyme | Comparative studies of substrate specificity and detoxification |
| TAT | Tyrosine aminotransferase; related PLP-dependent enzyme | Model for understanding substrate promiscuity in aminotransferases |
| KYAT1 | Kynurenine aminotransferase 1; produces kynurenic acid from kynurenine | Competes with GO:0047315 for L-kynurenine; relevant to neuroprotection |
| KYAT3 | Kynurenine aminotransferase 3; another kynurenine-metabolizing enzyme | Determines flux of kynurenine into alternative pathways |
| KMO | Kynurenine 3-monooxygenase; converts kynurenine to 3-hydroxykynurenine | Upstream of insect detoxification pathway |
| HGD | Homogentisate 1,2-dioxygenase; unrelated but part of aromatic amino acid catabolism | Context for metabolic flux studies |
| GRHPR | Glyoxylate reductase/hydroxypyruvate reductase; reduces glyoxylate to glycolate | Competes with GO:0047315 for glyoxylate; mutations cause hyperoxaluria type 2 |
| HOGA1 | 4-hydroxy-2-oxoglutarate aldolase; involved in glyoxylate metabolism | Mutations cause hyperoxaluria type 3; related to glyoxylate detoxification |
| PLP | Pyridoxal 5'-phosphate; cofactor for the transamination reaction | Essential for enzyme activity; deficiency affects multiple aminotransferases |
| SLC25A1 | Mitochondrial citrate carrier; indirectly affects glyoxylate metabolism | Potential modifier of substrate availability |
| ACAT1 | Acetyl-CoA acetyltransferase; unrelated but used as a control in metabolic studies | Not directly linked; included for comparative purposes |
| GOT1 | Glutamic-oxaloacetic transaminase 1; another PLP-dependent aminotransferase | Model for studying transamination mechanisms |
| GPT | Glutamic-pyruvic transaminase; alanine aminotransferase | Related activity; useful for substrate specificity comparisons |
| SHMT1 | Serine hydroxymethyltransferase; serine metabolism | Indirectly affects serine availability for AGXT |
| PHGDH | Phosphoglycerate dehydrogenase; serine biosynthesis | Modulates serine pool that feeds AGXT |
How Is L-kynurenine:glyoxylate transaminase activity Regulated?
The activity of L-kynurenine:glyoxylate transaminase is primarily regulated by substrate availability and enzyme abundance. In humans, AGXT is a peroxisomal enzyme whose import and stability depend on proper folding and PLP binding. Mutations that destabilize the protein reduce activity. Upstream enzymes of tryptophan catabolism, such as KMO and KYAT1, determine how much L-kynurenine is available for transamination. In insects, the activity is induced in response to dietary tryptophan and may be regulated by developmental stage. Environmental chemicals, including insecticides, can alter the activity of tryptophan-metabolizing enzymes in rats, suggesting that xenobiotic exposure may modulate this pathway. However, specific transcriptional or post-translational regulators of AGXT remain incompletely defined, and no dedicated allosteric regulator has been conclusively identified.
L-kynurenine:glyoxylate transaminase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| AGXT | Primary hyperoxaluria type 1; glyoxylate detoxification defect | AGXT knockout HEK293 or HepG2 cells; point-mutation knock-in of patient variants |
| Ae-AGXT | Mosquito 3-hydroxykynurenine detoxification; oxidative stress resistance | Aedes aegypti cell line with CRISPR knockout; overexpression for resistance assays [2,6] |
| KYAT1 | Kynurenine pathway imbalance; neuroinflammation | KYAT1 knockout in neuronal cell lines; substrate competition assays |
| GRHPR | Primary hyperoxaluria type 2; glyoxylate reductase deficiency | GRHPR knockout cells; double knockout with AGXT to model severe oxalate production |
| TAT | Tyrosine metabolism; related aminotransferase dysfunction | TAT knockout hepatocytes; comparative substrate specificity studies |
Primary hyperoxaluria type 1 (PH1)
Mutations in AGXT cause primary hyperoxaluria type 1, an autosomal recessive disorder characterized by excessive oxalate production, recurrent kidney stones, and renal failure. The disease results from loss of glyoxylate detoxification: when AGXT activity is reduced, glyoxylate is converted to oxalate instead of glycine. The kynurenine transaminase activity of AGXT is part of its broader substrate repertoire, and its impairment may contribute to metabolic imbalance. CRISPR knockout models of AGXT in cell lines and animal models are used to study oxalate production and test therapeutic strategies.
Neurodegeneration and kynurenine pathway imbalance
The kynurenine pathway produces neuroactive metabolites, and shifts in flux can lead to neurotoxicity. In insects, 3-hydroxykynurenine is a reactive intermediate that causes oxidative stress, and the transaminase activity that detoxifies it is protective [2,4,6]. In mammals, kynurenine transamination to kynurenic acid is neuroprotective, while diversion to 3-hydroxykynurenine is neurotoxic. Although GO:0047315 uses kynurenine as an amino donor rather than producing kynurenic acid, it competes for the same substrate pool and may influence the balance of neuroactive metabolites.
Insect vector biology and pest control
In Aedes aegypti, the enzyme with L-kynurenine:glyoxylate transaminase activity is identical to 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase, which detoxifies 3-hydroxykynurenine [2,4]. This activity is essential for managing oxidative stress from blood meal digestion. Inhibitors of this enzyme could serve as insecticides, and studies have shown that some insecticides affect tryptophan metabolism in rats. The crystal structure of the Aedes enzyme provides a template for rational inhibitor design.
Comparative metabolism and enzyme evolution
The same catalytic activity is found in organisms as diverse as humans, monkeys, rats, and mosquitoes [1,2,7]. In monkey and rat liver, aromatic-amino-acid-glyoxylate aminotransferase activity overlaps with kynurenine transamination. In rat brain, a cytosolic tyrosine transaminase was identified as glutamine transaminase K, which also accepts glyoxylate. These comparative studies reveal how a single catalytic function can be adapted to different physiological contexts, from peroxisomal detoxification in mammals to cytosolic detoxification in insects [2,3].
From L-kynurenine:glyoxylate transaminase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of AGXT alter kynurenine and glyoxylate flux? | AGXT knockout in HepG2 or HEK293 cells; metabolomics and enzyme assays |
| Do patient mutations affect catalytic activity? | Point-mutation knock-in of AGXT variants (e.g., G170R) in cell lines; activity assays |
| Can a tagged AGXT be used to study peroxisomal targeting? | Knock-in of FLAG- or GFP-tagged AGXT at the endogenous locus; imaging |
| Does overexpression of AGXT protect against oxalate stress? | AGXT overexpression in renal epithelial cells; oxalate measurement |
| Is the insect enzyme essential for 3-hydroxykynurenine detoxification? | Aedes aegypti AGXT knockout; survival and oxidative stress assays [2,6] |
| Can CRISPR screening identify modifiers of glyoxylate metabolism? | Genome-wide CRISPR knockout library in hyperoxaluria cell models; selection with glyoxylate |
How to Study the L-kynurenine:glyoxylate transaminase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Coupled enzyme assay | Transaminase activity via NADH oxidation or product formation | Validation of AGXT knockout and knock-in cell lines |
| HPLC-UV | Kynurenine and 3-hydroxykynurenine concentrations | Insect enzyme kinetics and detoxification studies |
| LC-MS metabolomics | Glyoxylate, glycine, oxalate, and kynurenine pathway metabolites | Flux analysis in CRISPR models |
| X-ray crystallography | 3D structure of enzyme-substrate complexes | Active site mapping and inhibitor design |
| CRISPR knockout library screening | Gene essentiality and modifier identification | Discovery of synthetic lethal interactions with AGXT loss |
| Western blot | Protein expression and stability | Assessing mutant AGXT levels |
| Fluorescence microscopy | Subcellular localization of tagged AGXT | Peroxisomal targeting studies |
| Site-directed mutagenesis | Specific amino acid contributions to catalysis | Mechanistic studies of active site residues |
Enzymatic activity assays
The most direct way to measure GO:0047315 is a coupled enzyme assay that monitors the formation of glycine or the keto acid product. Classical assays use spectrophotometric detection of pyruvate or glyoxylate consumption, or HPLC to quantify kynurenine and its derivatives. In insects, 3-hydroxykynurenine transaminase activity is measured by following the decrease in absorbance at 370 nm. These assays are essential for validating CRISPR knockout and knock-in models.
Metabolomics and flux analysis
Liquid chromatography-mass spectrometry (LC-MS) can quantify L-kynurenine, glyoxylate, glycine, and downstream metabolites such as oxalate and kynurenic acid. Stable isotope labeling with 13C- or 15N-labeled substrates allows flux analysis through the pathway. In cells with AGXT knockout, glyoxylate and oxalate levels are expected to increase, providing a metabolic signature of loss of function.
Structural biology and biophysics
X-ray crystallography and cryo-EM can resolve the structure of the enzyme with bound substrates or inhibitors. The crystal structure of Aedes aegypti alanine glyoxylate aminotransferase has been solved, revealing the active site architecture and PLP binding. Circular dichroism and thermal shift assays can assess the stability of mutant enzymes, which is useful for characterizing patient variants.
CRISPR-based functional genomics
CRISPR knockout screens can identify genes that modify sensitivity to glyoxylate or kynurenine. For example, a genome-wide knockout library in a hyperoxaluria cell model can be challenged with high glyoxylate, and sgRNAs that confer resistance or sensitivity can be identified. Similarly, overexpression screens can find suppressors of oxalate production. These approaches link GO:0047315 to broader metabolic networks [1,2].
How CRISPR Can Be Used to Study GO:0047315 L-kynurenine:glyoxylate transaminase activity
Knockout
CRISPR knockout of AGXT in human cell lines such as HepG2 or HEK293 abolishes L-kynurenine:glyoxylate transaminase activity, leading to glyoxylate accumulation and increased oxalate production. These models are used to study the metabolic consequences of enzyme loss and to test therapeutic interventions. In Aedes aegypti cells, knockout of the orthologous enzyme reduces 3-hydroxykynurenine detoxification and increases oxidative stress sensitivity [2,6].
Point Mutation
Point mutations in AGXT, such as G170R, are found in primary hyperoxaluria type 1 patients and can be introduced by CRISPR base editing or homology-directed repair. These knock-in models allow researchers to study how specific amino acid changes affect catalytic activity, protein stability, and peroxisomal targeting. They are particularly valuable for testing pharmacological chaperones that may rescue misfolded variants.
Knock-in
Knock-in of epitope tags (e.g., FLAG, HA) or fluorescent proteins (e.g., GFP) at the endogenous AGXT locus enables real-time tracking of enzyme localization and turnover. Knock-in of a reporter gene under the control of the AGXT promoter can be used to study transcriptional regulation. These models preserve endogenous regulatory elements and provide physiological expression levels.
Overexpression
CRISPR activation (CRISPRa) or lentiviral overexpression of AGXT can increase L-kynurenine:glyoxylate transaminase activity above baseline. Overexpression models are useful for testing whether increased enzyme activity protects against glyoxylate toxicity or alters kynurenine pathway flux. In insects, overexpression of the Aedes enzyme in cell lines can enhance resistance to 3-hydroxykynurenine-induced oxidative stress.
How EDITGENE Supports L-kynurenine:glyoxylate transaminase activity Research
Researchers studying L-kynurenine:glyoxylate transaminase activity-related genes often need to determine whether a candidate gene is causally involved in a metabolic or disease phenotype. This requires precise genetic models that can isolate the contribution of a single enzyme activity from background pathways. EDITGENE provides a comprehensive suite of CRISPR services to generate such models efficiently and reproducibly.
Contact EDITGENE today to design your custom CRISPR model for L-kynurenine:glyoxylate transaminase activity research.
Frequently Asked Questions About L-kynurenine:glyoxylate transaminase activity
What is L-kynurenine:glyoxylate transaminase activity?
It is a molecular function defined by GO:0047315 that catalyzes the transfer of an amino group from L-kynurenine to glyoxylate, producing 4-(2-aminophenyl)-2,4-dioxobutanoate and glycine.
What genes are involved in L-kynurenine:glyoxylate transaminase activity?
In humans, the AGXT gene encodes the enzyme with this activity, which is identical to alanine-glyoxylate aminotransferase and serine-pyruvate aminotransferase. In insects, orthologous genes such as Ae-AGXT in Aedes aegypti perform the same reaction.
What is the reaction catalyzed by GO:0047315?
The reaction is L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine, a reversible transamination.
What cofactor does L-kynurenine:glyoxylate transaminase require?
The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor, which shuttles the amino group during catalysis [1,6].
Is L-kynurenine:glyoxylate transaminase activity the same as alanine-glyoxylate aminotransferase?
Yes, in humans the enzyme that catalyzes this reaction is identical to alanine-glyoxylate aminotransferase (AGXT) and serine-pyruvate aminotransferase.
What diseases are associated with L-kynurenine:glyoxylate transaminase activity?
Mutations in AGXT cause primary hyperoxaluria type 1, a kidney disease characterized by oxalate stones and renal failure. In insects, loss of the activity leads to accumulation of toxic 3-hydroxykynurenine.
How can I study L-kynurenine:glyoxylate transaminase activity in the lab?
Common methods include coupled enzyme assays, HPLC, LC-MS metabolomics, and CRISPR knockout or knock-in models to manipulate the responsible gene [1,2].
What is the subcellular localization of the human enzyme?
Human AGXT is localized to peroxisomes, where it detoxifies glyoxylate.
Can CRISPR be used to create models for this activity?
Yes, CRISPR knockout, point mutation knock-in, and overexpression models are widely used to study the function of AGXT and related enzymes [1,2].
Why is L-kynurenine:glyoxylate transaminase activity important for insect biology?
In mosquitoes, the enzyme detoxifies 3-hydroxykynurenine, a reactive byproduct of tryptophan metabolism, protecting against oxidative stress [2,4,6].
Conclusion
L-kynurenine:glyoxylate transaminase activity (GO:0047315) is a PLP-dependent transamination reaction that bridges tryptophan catabolism and glyoxylate detoxification. In humans, it is carried out by AGXT, a peroxisomal enzyme whose dysfunction causes primary hyperoxaluria type 1. In insects, the same activity protects against 3-hydroxykynurenine toxicity and is a potential target for vector control [2,6]. Understanding this activity requires precise genetic models, and CRISPR-based knockout, knock-in, and overexpression approaches are indispensable tools for dissecting its physiological roles [1,2].
References
- 1. Okuno E et al.. 1980. Crystallization and characterization of human liver kynurenine--glyoxylate aminotransferase. Identity with alanine--glyoxylate aminotransferase and serine--pyruvate aminotransferase.. Biochem J 189(3):581-90 PMID: 6783036
- 2. Han Q et al.. 2002. 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti.. J Biol Chem 277(18):15781-7 PMID: 11880382
- 3. Bowsher RR et al.. 2020. Purification, characterization and identification of rat brain cytosolic tyrosine transaminase as glutamine Transaminase-K.. Neurochem Int 133:104653 PMID: 31874188
- 4. Han Q et al.. 2002. Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase.. FEBS Lett 527(1-3):199-204 PMID: 12220660
- 5. Hassan AA et al.. 1990. Effects of some insecticides on several enzymes of tryptophan metabolism in rats.. J Environ Sci Health B 25(3):333-46 PMID: 2119399
- 6. Han Q et al.. 2006. Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase.. J Biol Chem 281(48):37175-82 PMID: 16990263
- 7. Harada I et al.. 1978. Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver.. Hoppe Seylers Z Physiol Chem 359(4):481-8 PMID: 25837
