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Literature summary for 6.3.1.2 extracted from
- Regulation of nitrogen metabolism in Mycobacterium tuberculosis: a comparison with mechanisms in Corynebacterium glutamicum and Streptomyces coelicolor (2008), IUBMB Life, 60, 643-650.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the level of glnA1 transcription is upregulated under nitrogen limitation conditions | Corynebacterium glutamicum | |
| additional information | the level of glnA1 transcription is upregulated under nitrogen limitation conditions | Mycobacterium tuberculosis | |
| additional information | the level of glnA1 transcription is upregulated under nitrogen limitation conditions. GlnR is able to function as both an activator and repressor of transcription | Streptomyces coelicolor |
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is an attractive target for development of antimycobacterial drugs | Mycobacterium tuberculosis |
| synthesis | the organism is used for industrial production of L-glutamine | Corynebacterium glutamicum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | glnA1 mutants are attenuated for intracellular growth in human THP-1 macrophages and are unable to infect guinea pigs | Mycobacterium tuberculosis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | a single transcriptional repressor AmtR from the TetR family is involved in enzyme regulation, AmtB is encoded by amtB clustered together with glnK in an operon, glnK encodes for a PII signaling protein which are small trimeric proteins that are able to bind 2-oxoglutarate and play a pivotal role in the regulation of nitrogen metabolism by way of controlling the activity of signal transduction components and key metabolic enzymes. GlnK is not uridylylated but rather adenylylated/de-adenylylated by GlnD | Corynebacterium glutamicum | |
| additional information | a single transcriptional repressor AmtR from the TetR family is involved in enzyme regulation, AmtB is encoded by amtB clustered together with glnK in an operon, glnK encodes for a PII signaling protein which are small trimeric proteins that are able to bind 2-oxoglutarate and play a pivotal role in the regulation of nitrogen metabolism by way of controlling the activity of signal transduction components and key metabolic enzymes. GlnK is not uridylylated but rather adenylylated/de-adenylylated by GlnD | Mycobacterium tuberculosis | |
| additional information | GlnR is able to function as both an activator and repressor of transcription | Streptomyces coelicolor | |
| nitrogen | the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase | Corynebacterium glutamicum |  |
| nitrogen | the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase | Mycobacterium tuberculosis | |
| nitrogen | the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase. Both GSII activity and glnII transcription levels increase during nitrogen starvation of morphologically differentiating cultures while there was no change in glnA1 transcription | Streptomyces coelicolor | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | a much larger amount of GlnA1 is produced than is necessary for normal growth by the organism and a substantial proportion of this is found in the extracellular medium of cell cultures | Mycobacterium tuberculosis | - |
- |
| additional information | GS1 lacks a leader peptide sequence | Mycobacterium tuberculosis | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Corynebacterium glutamicum | |
| Mg2+ | - |
Mycobacterium tuberculosis | |
| Mg2+ | - |
Streptomyces coelicolor | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + NH3 | Mycobacterium tuberculosis | only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | Streptomyces coelicolor | only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, the transcriptional regulator GlnR is involved in regulation of the enzyme activity and is able to function as both an activator and repressor of transcription, overview. GSII probably plays and important role in mycelial development as well as differential glnA1 and glnII transcriptional regulation | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | Corynebacterium glutamicum | the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | Mycobacterium tuberculosis H37Rv | only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis | ADP + phosphate + L-glutamine | - |
? | |
| additional information | Streptomyces coelicolor | transcriptional regulation as part of the nitrogen assimilation system, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | - |
gene glnA1 or cg2429 encoding a GSI-beta-subtype enzyme GlnA1 as the functional enzyme form in the organism, gene glnA2 encodes a GSI-alpha-subtype | - |
| Mycobacterium tuberculosis | - |
four highly homolgous GSI protein sequences GlnA1, encoded by gene Rv2220, GlnA2, GlnA3, and GlnA4 | - |
| Mycobacterium tuberculosis H37Rv | - |
four highly homolgous GSI protein sequences GlnA1, encoded by gene Rv2220, GlnA2, GlnA3, and GlnA4 | - |
| Streptomyces coelicolor | P15106 | four highly homolgous GSI protein sequences GlnA1, GlnA2, GlnA3, and GlnA4 | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | GlnA1 is subject to posttranslational modification, while GlnA2 is not | Corynebacterium glutamicum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | a much larger amount of GlnA1 is produced than is necessary for normal growth by the organism and a substantial proportion of this is found in the extracellular medium of cell cultures | Mycobacterium tuberculosis | - |
| mycelium | - |
Streptomyces coelicolor | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + NH3 | - |
Mycobacterium tuberculosis | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | - |
Streptomyces coelicolor | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis | Mycobacterium tuberculosis | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, the transcriptional regulator GlnR is involved in regulation of the enzyme activity and is able to function as both an activator and repressor of transcription, overview. GSII probably plays and important role in mycelial development as well as differential glnA1 and glnII transcriptional regulation | Streptomyces coelicolor | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview | Corynebacterium glutamicum | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | GlnA1 is essential for survival in vitro, while GlnA2 is probably not | Corynebacterium glutamicum | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | - |
Mycobacterium tuberculosis H37Rv | ADP + phosphate + L-glutamine | - |
? | |
| ATP + L-glutamate + NH3 | only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis | Mycobacterium tuberculosis H37Rv | ADP + phosphate + L-glutamine | - |
? | |
| additional information | transcriptional regulation as part of the nitrogen assimilation system, overview | Streptomyces coelicolor | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Glutamine synthetase | - |
Corynebacterium glutamicum |
| Glutamine synthetase | - |
Mycobacterium tuberculosis |
| Glutamine synthetase | - |
Streptomyces coelicolor |
| GS type-1 | - |
Corynebacterium glutamicum |
| GSI | - |
Corynebacterium glutamicum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Corynebacterium glutamicum | |
| ATP | - |
Mycobacterium tuberculosis | |
| ATP | - |
Streptomyces coelicolor | |
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