AGXT
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Official Full Name
alanine-glyoxylate aminotransferase
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Overview
This gene is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria. -
Synonyms
AGXT; alanine-glyoxylate aminotransferase; SPAT; serine--pyruvate aminotransferase; AGT; AGT1; AGXT1; glycolicaciduria; L alanine: glyoxylate aminotransferase 1; oxalosis I; PH1; primary hyperoxaluria type 1; serine:pyruvate aminotransferase; SPT; serine-;
- Recombinant Proteins
- Cell & Tissue Lysates
- Antibody
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Rat
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mamanlian cells
- Mammalian Cell
- Mouse
- Wheat Germ
- Yeast
- Flag
- GST
- His
- His (Fc)
- Avi
- His|SUMO
- Myc
- DDK
- MYC
- Myc|DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
AGXT involved in several pathways and played different roles in them. We selected most pathways AGXT participated on our site, such as Alanine and aspartate metabolism, Alanine, aspartate and glutamate metabolism, Biosynthesis of antibiotics, which may be useful for your reference. Also, other proteins which involved in the same pathway with AGXT were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Alanine and aspartate metabolism | DARS;ABAT;AGXT |
| Alanine, aspartate and glutamate metabolism | GLULC;NIT2;GLS2;ASNS;AGXTA;ALDH4A1;RIMKLB;PPAT;ASPA |
| Biosynthesis of antibiotics | LDHAL6A;GALM;UAP1L1;AK8;DLD;CYP51A1;ECHS1;EHHADH;CMBL |
| Carbon metabolism | OGDHA;DLAT;ACSS2;GLDC;GPT2L;TPI1B;MDH1AA;GLUD1B;FBP1B |
| Glycine, serine and threonine metabolism | BPGM;LSM1;GATM;AOC3;GRHPR;AGXT2;CBSA;BHMT;DAO1 |
| Glyoxylate and dicarboxylate metabolism | SHMT2;HAO1;MDH1AA;ACAT2;GLYCTK;ACAT1;CS;PCCB;HYI |
| Glyoxylate metabolism and glycine degradation | DAO1;AGXT;DAO |
| Metabolic pathways | LALBA;UGT2A1;GCDH;POLR3D;FLAD1;NDUFV3;AGPAT9;PON1;MCEE |
AGXT has several biochemical functions, for example, alanine-glyoxylate transaminase activity, amino acid binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AGXT itself. We selected most functions AGXT had, and list some proteins which have the same functions with AGXT. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| alanine-glyoxylate transaminase activity | AGXT2;AGXTA;AGXT;AGXTB |
| amino acid binding | AARS2;TPH2;TPH1;TPH1A;TH;TDO2;GCHFR;DDAH1;PAH |
| protein binding | CCP110;HYPM;C16orf59;ACTN4;KIAA1217;KL;MED11;TSGA10IP;HELT |
| protein homodimerization activity | GSTM3;PRMT8;GDNF;SLIT2;PEX7;B4GALT1;PRLR;IL17F;RAB11FIP4B |
| protein self-association | CCL5;TMEM43;NKX3-1;TNFAIP3;AGTR1A;ZNF496;BCL10;SLC2A1;EPB49 |
| pyridoxal phosphate binding | MARC1;CCBL1;MOSC2;CBSB;DDC;PYGL;ETNPPL;PYGB;SHMT1 |
| receptor binding | HRG;CAPRIN2;CRH;MYO1C;GRP;VTCN1;SRMS;UCN2;SSFA2 |
| serine-pyruvate transaminase activity | AGXT;AGXTA;AGXTB |
| transaminase activity | ETNPPL;AGXT2;GPT2L;GOT1L1;AGXT;GOT2A;PHYKPL;CCBL1;AGXT2L2 |
AGXT has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AGXT here. Most of them are supplied by our site. Hope this information will be useful for your research of AGXT.
ACAT1; SNCAIP
- Q&As
- Reviews
Q&As (10)
Ask a questionAGXT contains a PLP-binding domain, characteristic of aminotransferases, which is critical for its enzymatic activity and substrate specificity.
Yes, mutations in the AGXT gene can cause primary hyperoxaluria type 1 (PH1), a rare autosomal recessive disorder characterized by the overproduction and accumulation of oxalate, resulting in severe kidney and urinary tract complications.
Targeting AGXT enzymatic activity may hold promise for developing therapies to prevent kidney stone formation in non-PH1 patients; however, further research is needed to validate this approach.
AGXT is primarily localized in the peroxisomes, a subcellular organelle responsible for various metabolic processes, including lipid metabolism and detoxification.
Epigenetic modifications, such as DNA methylation or histone acetylation, could potentially regulate AGXT gene expression and activity, affecting oxalate metabolism.
AGXT activity can be regulated by phosphorylation, allosteric modulation, and interaction with other proteins involved in peroxisomal metabolism.
AGXT plays a crucial role in the peroxisomal glyoxylate pathway, converting glyoxylate to glycine to prevent the accumulation of harmful oxalate, which can lead to kidney stone formation.
In PH1 patients, AGXT deficiency impairs the conversion of glyoxylate to glycine, leading to the accumulation of glyoxylate. Excessive glyoxylate is converted to oxalate, which can form kidney stones and cause tissue damage.
AGXT may participate in other cellular processes or metabolic pathways, and its broader functional roles warrant further exploration.
AGXT catalyzes the conversion of glyoxylate and L-alanine to glycine and pyruvate, utilizing PLP as a cofactor.
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