Relation Results

Summary

Name L-glutamate(1-)
Synonyms (2S)-2-ammoniopentanedioate (IUPAC), L-glutamate (ChEBI), L-glutamate (UniProt), L-glutamate(1-) (JCBN), L-glutamic acid monoanion (JCBN), L-glutamic acid, ion(1-) (ChemIDplus)
IUPAC hydrogen L-glutamate
Formula C5H8NO4
Primary ID CHEBI:29985
Type small molecule
Relations 36
Pathways Aspartate and asparagine metabolism, Glutamine metabolism, Nucleotide Biosynthesis

Viewer

Type: Score: Layout: SPV 
0.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.80.8GOT1L-glutamate(1-)L-glutamine zwitterionASNSGLULD-fructofuranose 6-phosphate(2-)GFPT1PPATL-aspartate(1-)GAD12-oxoglutarate(2-)GOT2NAALAD2GLSCADgamma-aminobutyric acidGLS25'-xanthylic acidGAD2GMPSAc-Asp-Glu(3-)

Relations

Regulator
Mechanism
target
score
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267510 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267339 Homo sapiens
pmid sentence
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).
Identifier Residue Sequence Organism Cell Line
SIGNOR-268072 Homo sapiens
pmid sentence
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-267189 Homo sapiens
pmid sentence
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-267814 Homo sapiens
pmid sentence
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-266906 Homo sapiens
pmid sentence
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia.
Identifier Residue Sequence Organism Cell Line
SIGNOR-266907 Homo sapiens
pmid sentence
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia.
Identifier Residue Sequence Organism Cell Line
SIGNOR-267426 Homo sapiens
pmid sentence
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: 7 Organism: Homo Sapiens
Pathways:Aspartate and asparagine metabolism, Glutamine metabolism, Nucleotide Biosynthesis
+ up-regulates quantity img/direct-activation.png precursor of L-glutamine zwitterion 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267822 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267535 Homo sapiens
pmid sentence
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
+ down-regulates quantity img/direct_inhibition.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267824 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267813 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267818 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267294 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267508 Homo sapiens
pmid sentence
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
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
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
+ down-regulates quantity img/direct_inhibition.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267551 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of 2-oxoglutarate(2-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-266915 Bos taurus
pmid sentence
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
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
+ down-regulates quantity img/direct_inhibition.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-268063 Homo sapiens
pmid sentence
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
+ down-regulates quantity img/direct_inhibition.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-268059 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of L-aspartate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267512 Homo sapiens
pmid sentence
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
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
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267542 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267518 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-266910 Homo sapiens
pmid sentence
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia.
Publications: 1 Organism: Homo Sapiens
Pathways:Glutamine metabolism
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267421 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of gamma-aminobutyric acid 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267553 Homo sapiens
pmid sentence
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-267550 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-266911 Homo sapiens
pmid sentence
Glutaminase (GLS1/2) catalyzes the conversion of L-glutamine to L-glutamate and ammonia.
Publications: 1 Organism: Homo Sapiens
Pathways:Glutamine metabolism
+ up-regulates quantity img/direct-activation.png precursor of L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-268095 Homo sapiens
pmid sentence
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
+ down-regulates quantity img/direct_inhibition.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267554 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png chemical modification L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267341 Homo sapiens
pmid sentence
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
+ up-regulates quantity img/direct-activation.png precursor of L-glutamate(1-) 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-267540 Homo sapiens
pmid sentence
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
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