| + |
GOT2 | down-regulates quantity 
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268060 |
|
|
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 |
| + |
L-asparagine zwitterion | up-regulates quantity 
precursor of
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24657844 |
Recently, we structurally and biochemically characterized the enzyme human L-asparaginase 3 (hASNase3), which possesses L-asparaginase activity and belongs to the N-terminal nucleophile superfamily of enzymes. l-Asparaginases (EC 3.5.1.1; l-asparagine amidohydrolase; l-ASNase2) are enzymes that primarily catalyze the conversion of l-asparagine (l-Asn) to l-aspartic acid (l-Asp) and ammonia, although some of them are able to also hydrolyze l-glutamine (l-Gln) to l-glutamic acid (l-Glu) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
PAICS | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267321 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33179964 |
The next two reactions (steps 6 and 7) involve carb oxylation of AIR to 4-carboxy-5-aminoimidazole ribonu cleotide (CAIR) and ligation of the carboxy group of CAIR with an amide group derived from Asp in an ATP dependent reaction forming 4-(N-succinylcarboxamide)- 5-aminoimidazole ribonucleotide (SAICAR). These reac tions are catalyzed by the bifunctional enzyme phosphoribosylaminoimidazole carboxylase/phosphori bosylaminoimidazole succinocarboxamide synthetase (PAICS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
beta-alanine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267547 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22718265 |
Animal glutamate decarboxylase (GDC), aspartate decarboxylase (ADC, also called aspartate α-decarboxylase or aspartate 1-decarboxylase) and cysteine sulfinic acid decarboxylase (CSADC) catalyze the decarboxylation of α-carboxyl group of glutamate, aspartate and cysteine sulfinic acid to produce γ-aminobutyric acid (GABA), β-alanine and hypotaurine, respectively; these amine products play important role in living organisms. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267544 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22718265 |
Animal glutamate decarboxylase (GDC), aspartate decarboxylase (ADC, also called aspartate α-decarboxylase or aspartate 1-decarboxylase) and cysteine sulfinic acid decarboxylase (CSADC) catalyze the decarboxylation of α-carboxyl group of glutamate, aspartate and cysteine sulfinic acid to produce γ-aminobutyric acid (GABA), β-alanine and hypotaurine, respectively; these amine products play important role in living organisms. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
SAICAR(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267320 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33179964 |
The next two reactions (steps 6 and 7) involve carb oxylation of AIR to 4-carboxy-5-aminoimidazole ribonu cleotide (CAIR) and ligation of the carboxy group of CAIR with an amide group derived from Asp in an ATP dependent reaction forming 4-(N-succinylcarboxamide)- 5-aminoimidazole ribonucleotide (SAICAR). These reac tions are catalyzed by the bifunctional enzyme phosphoribosylaminoimidazole carboxylase/phosphori bosylaminoimidazole succinocarboxamide synthetase (PAICS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
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-aspartate(1-) | up-regulates quantity
precursor of
|
N-acetyl-L-aspartate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267519 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19524112 |
The biosynthetic enzyme, aspartate-N-acetyltransferase (Asp-NAT; EC 2.3.1.17) is a CNS specific enzyme that catalyzes the transfer of acetate from acetyl-CoA to L-aspartate forming NAA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
NAT8L | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267521 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19524112 |
The biosynthetic enzyme, aspartate-N-acetyltransferase (Asp-NAT; EC 2.3.1.17) is a CNS specific enzyme that catalyzes the transfer of acetate from acetyl-CoA to L-aspartate forming NAA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
N-carbamoyl-L-aspartate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267423 |
|
|
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: | Nucleotide Biosynthesis |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
N(6)-(1,2-dicarboxylatoethyl)-AMP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268131 |
|
|
|
|
| pmid |
sentence |
| 10496970 |
Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. |
|
| Publications: |
1 |
| Pathways: | Nucleotide Biosynthesis |
| + |
GADL1 | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267545 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22718265 |
Animal glutamate decarboxylase (GDC), aspartate decarboxylase (ADC, also called aspartate α-decarboxylase or aspartate 1-decarboxylase) and cysteine sulfinic acid decarboxylase (CSADC) catalyze the decarboxylation of α-carboxyl group of glutamate, aspartate and cysteine sulfinic acid to produce γ-aminobutyric acid (GABA), β-alanine and hypotaurine, respectively; these amine products play important role in living organisms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
ASPG | up-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267538 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24657844 |
Recently, we structurally and biochemically characterized the enzyme human L-asparaginase 3 (hASNase3), which possesses L-asparaginase activity and belongs to the N-terminal nucleophile superfamily of enzymes. l-Asparaginases (EC 3.5.1.1; l-asparagine amidohydrolase; l-ASNase2) are enzymes that primarily catalyze the conversion of l-asparagine (l-Asn) to l-aspartic acid (l-Asp) and ammonia, although some of them are able to also hydrolyze l-glutamine (l-Gln) to l-glutamic acid (l-Glu) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
CSAD | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267548 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22718265 |
Animal glutamate decarboxylase (GDC), aspartate decarboxylase (ADC, also called aspartate α-decarboxylase or aspartate 1-decarboxylase) and cysteine sulfinic acid decarboxylase (CSADC) catalyze the decarboxylation of α-carboxyl group of glutamate, aspartate and cysteine sulfinic acid to produce γ-aminobutyric acid (GABA), β-alanine and hypotaurine, respectively; these amine products play important role in living organisms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine 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-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. |
|
| 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). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Nucleotide Biosynthesis |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267529 |
|
|
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, Nucleotide Biosynthesis |
| + |
ADSS2 | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267345 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10496970 |
Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Nucleotide Biosynthesis |
| + |
ASPA | up-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17194761 |
N-acetyl-l-aspartate (NAA) is one of the most abundant amino acid derivatives found in the vertebrate brain, second only to glutamate. Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspartate to aspartate and acetate in the vertebrate brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
CAD | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267424 |
|
|
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: | Nucleotide Biosynthesis |
| + |
N-acetyl-L-aspartate(2-) | up-regulates quantity
precursor of
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267525 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17194761 |
N-acetyl-l-aspartate (NAA) is one of the most abundant amino acid derivatives found in the vertebrate brain, second only to glutamate. Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspartate to aspartate and acetate in the vertebrate brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism |
| + |
GOT1 | up-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267506 |
|
|
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 |
| + |
ASNS | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267531 |
|
|
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 |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
L-asparagine zwitterion |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268069 |
|
|
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 |
| + |
GOT2 | up-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267514 |
|
|
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 |
| + |
ADSS1 | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267346 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10496970 |
Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Nucleotide Biosynthesis |
| + |
GOT1 | down-regulates quantity
chemical modification
|
L-aspartate(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268064 |
|
|
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 |
3.0
L-aspartate(1-)