| + |
L-glutamate(1-) | up-regulates quantity 
precursor of
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267512 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31422819 |
This is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that exists as cytosolic (GOT1) and intramitochondrial (GOT2) isoforms. Both isoforms catalyze the reversible interconversion of oxaloacetate and glutamate into aspartate and α-ketoglutarate. These enzymes are part of the malate-aspartate shuttle (MAS), a key player in intracellular NAD(H) redox homeostasis (Figure 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266921 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31422819 |
Both isoforms [GOT! AND GOT2] catalyze the reversible interconversion of oxaloacetate and glutamate into aspartate and α-ketoglutarate. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267504 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Nucleotide Biosynthesis |
| + |
L-glutamine zwitterion | up-regulates quantity
precursor of
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266906 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22049910 |
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268072 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267814 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21310273 |
GFPT1 catalyzes the transfer of an amino group from glutamine onto fructose-6-phosphate, yielding glucosamine-6-phosphate (GlcN-6-P) and glutamate. This transamidase reaction has been identified as the first and rate-limiting step of the hexosamine biosynthesis pathway, which is the obligatory source of essential amino sugars for the synthesis of glycoproteins, glycolipids, and proteoglycans |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267426 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28552578 |
CAD is a 243 kDa polypeptide formed by the fusion of four enzymatic domains that initiate the de novo biosynthesis of pyrimidine nucleotides . The first two domains, glutaminase (GLN) and carbamoyl phosphate synthetase (CPS-II), initiate the pathway, catalyzing the formation of carbamoyl phosphate (CP) from bicarbonate, glutamine, and two ATP molecules. Next, the labile CP is partially channeled to the C-terminal aspartate transcarbamoylase (ATC) domain where it reacts with aspartate to form carbamoyl aspartate. Then, carbamoyl aspartate is condensated to dihydroorotate, the cyclic precursor of the pyrimidine ring, by the dihydroorotase (DHO), a Zn metalloenzyme fused between CPS and ATC domains. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267189 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8106516 |
Two Genes for de Novo Purine Nucleotide Synthesis on Human Chromosome 4 Are Closely Linked and Divergently Transcribed” |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266907 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22049910 |
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267339 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 6698284 |
The de novo synthesis of guanosine monophosphate (GMP) involves the oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP) followed by amination to GMP. This latter reaction is catalyzed by GMP synthetase. (XMP: I.-glutamine amidoligase (AMP) EC 6.3.5.2). |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism, Nucleotide Biosynthesis |
| + |
L-glutamate(1-) | up-regulates quantity
precursor of
|
gamma-aminobutyric acid |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267550 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32041144 |
Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce γ-aminobutyric acid (GABA), which exhibits several well-known physiological functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267553 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32041144 |
Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce γ-aminobutyric acid (GABA), which exhibits several well-known physiological functions. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT1 | down-regulates quantity 
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268063 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
GOT1 | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267510 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
Ac-Asp-Glu(3-) | up-regulates quantity
precursor of
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267540 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10085079 |
The neuropeptide N-acetyl-L-aspartate-L-glutamate (NAAG)1 is expressed both in the central nervous system and in the periphery. Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
NAALAD2 | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267542 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10085079 |
The neuropeptide N-acetyl-L-aspartate-L-glutamate (NAAG)1 is expressed both in the central nervous system and in the periphery. Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GFPT1 | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267818 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21310273 |
GFPT1 catalyzes the transfer of an amino group from glutamine onto fructose-6-phosphate, yielding glucosamine-6-phosphate (GlcN-6-P) and glutamate. This transamidase reaction has been identified as the first and rate-limiting step of the hexosamine biosynthesis pathway, which is the obligatory source of essential amino sugars for the synthesis of glycoproteins, glycolipids, and proteoglycans |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism |
| + |
GLS | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266910 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22049910 |
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism |
| + |
GLS2 | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266911 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22049910 |
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267508 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26003525 |
Glutamate oxaloacetate transaminase (GOT) catalyzes the reversible reaction of l-aspartate and α-ketoglutarate into oxaloacetate and L-glutamate and plays a key role in carbon and nitrogen metabolism in all organisms. In human tissues, GOTs are pyridoxal 5'-phosphate-dependent (PLP) enzymes which exist in cytoplasm and mitochondrial forms, GOT1 and GOT2, respectively. GOT1 expression correlates with the growth of several tumors because cancer cells can utilize the amino acid glutamine to fuel anabolic processes, and therefore, GOT1 represents a new therapeutic target in cancer. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267516 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31422819 |
This is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that exists as cytosolic (GOT1) and intramitochondrial (GOT2) isoforms. Both isoforms catalyze the reversible interconversion of oxaloacetate and glutamate into aspartate and α-ketoglutarate. These enzymes are part of the malate-aspartate shuttle (MAS), a key player in intracellular NAD(H) redox homeostasis (Figure 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268070 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Nucleotide Biosynthesis |
| + |
L-glutamate(1-) | up-regulates quantity
precursor of
|
2-oxoglutarate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266915 |
|
|
Bos taurus |
|
| pmid |
sentence |
| 11254391 |
Glutamate dehydrogenase is found in all organisms and catalyses the oxidative deamination of l-glutamate to 2-oxoglutarate. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266924 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11863375 |
Alanine aminotransferase (ALT) catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate, and thereby has a key role in the intermediary metabolism of glucose and amino acids. Two ALT isoenzymes are known to exist, but only one ALT gene has been cloned, GPT. In this study, we cloned a homolog of GPT and named it GPT2, and the corresponding protein ALT2 |
|
| Publications: |
2 |
Organism: |
Bos Taurus, Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
5'-xanthylic acid | up-regulates quantity
precursor of
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268095 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 6698284 |
The de novo synthesis of guanosine monophosphate (GMP) involves the oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP) followed by amination to GMP. This latter reaction is catalyzed by GMP synthetase. (XMP: I.-glutamine amidoligase (AMP) EC 6.3.5.2). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
CAD | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267421 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28552578 |
CAD is a 243 kDa polypeptide formed by the fusion of four enzymatic domains that initiate the de novo biosynthesis of pyrimidine nucleotides . The first two domains, glutaminase (GLN) and carbamoyl phosphate synthetase (CPS-II), initiate the pathway, catalyzing the formation of carbamoyl phosphate (CP) from bicarbonate, glutamine, and two ATP molecules. Next, the labile CP is partially channeled to the C-terminal aspartate transcarbamoylase (ATC) domain where it reacts with aspartate to form carbamoyl aspartate. Then, carbamoyl aspartate is condensated to dihydroorotate, the cyclic precursor of the pyrimidine ring, by the dihydroorotase (DHO), a Zn metalloenzyme fused between CPS and ATC domains. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
| + |
GAD2 | down-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267554 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32041144 |
Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce γ-aminobutyric acid (GABA), which exhibits several well-known physiological functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
PPAT | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267294 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9914248 |
Glutamine PRPP amidotransferase (GPATase) catalyzes the first step of de novo purine biosynthesis, the conversion of 5-phosphoribosyl-(~)l-pyrophosphate (PRPP) to 5-phosphoribosyl-([3)l-amine (PRA). The nitrogen source for the reaction is the amide group of glutamine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
| + |
GMPS | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267341 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 6698284 |
The de novo synthesis of guanosine monophosphate (GMP) involves the oxidation of inosine monophosphate (IMP) to xanthosine monophosphate (XMP) followed by amination to GMP. This latter reaction is catalyzed by GMP synthetase. (XMP: I.-glutamine amidoligase (AMP) EC 6.3.5.2). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism, Nucleotide Biosynthesis |
| + |
D-fructofuranose 6-phosphate(2-) | up-regulates quantity
precursor of
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267813 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21310273 |
GFPT1 catalyzes the transfer of an amino group from glutamine onto fructose-6-phosphate, yielding glucosamine-6-phosphate (GlcN-6-P) and glutamate. This transamidase reaction has been identified as the first and rate-limiting step of the hexosamine biosynthesis pathway, which is the obligatory source of essential amino sugars for the synthesis of glycoproteins, glycolipids, and proteoglycans |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GOT2 | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267518 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31422819 |
This is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that exists as cytosolic (GOT1) and intramitochondrial (GOT2) isoforms. Both isoforms catalyze the reversible interconversion of oxaloacetate and glutamate into aspartate and α-ketoglutarate. These enzymes are part of the malate-aspartate shuttle (MAS), a key player in intracellular NAD(H) redox homeostasis (Figure 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
ASNS | up-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267535 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
GLUL | down-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30158707 |
Glutamine synthetase, encoded by the gene GLUL, is an enzyme that converts glutamate and ammonia to glutamine. certain cell types express glutamine synthetase (GS; also called glutamate-ammonia ligase; GLUL), the enzyme capable of de novo glutamine production from glutamate and ammonia in an ATP and Mg2+/Mn2+ requiring reaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamine metabolism |
| + |
L-glutamate(1-) | up-regulates quantity
precursor of
|
L-glutamine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267822 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30158707 |
Glutamine synthetase, encoded by the gene GLUL, is an enzyme that converts glutamate and ammonia to glutamine. certain cell types express glutamine synthetase (GS; also called glutamate-ammonia ligase; GLUL), the enzyme capable of de novo glutamine production from glutamate and ammonia in an ATP and Mg2+/Mn2+ requiring reaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism, Nucleotide Biosynthesis |
| + |
GAD1 | down-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267551 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32041144 |
Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce γ-aminobutyric acid (GABA), which exhibits several well-known physiological functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT2 | down-regulates quantity
chemical modification
|
L-glutamate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268059 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31422819 |
This is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that exists as cytosolic (GOT1) and intramitochondrial (GOT2) isoforms. Both isoforms catalyze the reversible interconversion of oxaloacetate and glutamate into aspartate and α-ketoglutarate. These enzymes are part of the malate-aspartate shuttle (MAS), a key player in intracellular NAD(H) redox homeostasis (Figure 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
3.0
L-glutamate(1-)