trigger enzyme: catabolic glutamate dehydrogenase induced by arginine, ornithine or proline, subject to carbon catabolite repression
function
arginine utilization, controls the activity of GltC
product
trigger enzyme: glutamate dehydrogenase (major)
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.2|Utilization of amino acids] → [category|SW 2.3.2.1|Utilization of glutamine/ glutamate][category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.2|Utilization of amino acids] → [category|SW 2.3.2.4|Utilization of arginine/ ornithine][category|SW 3|Information processing] → [category|SW 3.4|Regulation of gene expression] → [category|SW 3.4.2|Transcription factors and their control] → [category|SW 3.4.2.7|Control of transcription factor (other than two-component system)][category|SW 3|Information processing] → [category|SW 3.4|Regulation of gene expression] → [category|SW 3.4.3|Trigger enzyme] → [category|SW 3.4.3.2|Trigger enzymes that control gene expression by protein-protein interaction with transcription factors]This gene is a member of the following [SW|regulons]
[SW|AbrB regulon], [SW|AhrC regulon], [SW|CcpA regulon], [SW|RocR regulon], [SW|SigL regulon]Gene
Coordinates on the chromosome (coding sequence)
3,880,740 -> 3,882,014
Phenotypes of a mutant
Poor growth on complex media such as SP (sporulation medium). No growth in minimal media with arginine as the only carbon source. Rapid accumulation of suppressor mutants ([gene|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|''gudB1'']]])sensitive to ß-lactam antibiotics such as cefuroxime and to fosfomycin (suppressed by activation of ''[gene|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|gudB]'') due to the downregulation of the [SW|SigW regulon] [Pubmed|22178969]transcription profile of a ''[gene|56CBEBCFEF5CFB4A0175498338C7AF2F45EAA3E3|rocG] [gene|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|gudB]'' mutant strain: [http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE34383&submit.x=22&submit.y=9 GEO] [Pubmed|22178969]The protein
Catalyzed reaction/ biological activity
L-glutamate H2O NAD = 2-oxoglutarate NH3 NADH H (according to Swiss-Prot), controls the activity of the [protein|87BCAE725B02860156D50E1783F6DB68510C811E|GltC] transcription activator [Pubmed|17608797] Protein family
Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot)Paralogous protein(s)
[protein|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|GudB]Kinetic information
KM [glutamate] = 2.9 mM, KM [ammonium] = 18 mM [Pubmed|20630473][SW|Cofactors]
Structure
[PDB|3K92] (super-repressor mutant that is capable of constitutive inactivation of [protein|87BCAE725B02860156D50E1783F6DB68510C811E|GltC], E93K mutation) [Pubmed|20630473]Expression and Regulation
[[this]]
Biological materials
Mutant
GP747 (spc), GP726 (aphA3), GP810 (del tet), GP1157 (cat) all available in [SW|Jörg Stülke]'s labExpression vector
expression of native ''rocG'' in ''B. subtilis'': pGP529 (in [SW|pBQ200]), available in [SW|Jörg Stülke]'s lab [Pubmed|18326565]for purification of RocG from ''E. coli'' carrying an N-terminal Strep-tag: pGP902 (in [SW|pGP172]), a series of ''rocG'' variants is also available in [SW|pGP172], available in [SW|Jörg Stülke]'s labfor expression/ purification from ''E. coli'' with N-terminal His-tag and thrombin cleavage site, in [SW|pWH844]: pGP860, available in [SW|Jörg Stülke]'s labpurification from ''B. subtilis'' with an N-terminal Strep-tag, for [SW|SPINE], (in [SW|pGP380]): pGP1709, available in [SW|Jörg Stülke]'s labtwo-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labAntibody
available in [SW|Jörg Stülke]'s lab [Pubmed|17183217]Labs working on this gene/protein
[SW|Linc Sonenshein], Tufts University, Boston, MA, USA [http://www.tufts.edu/sackler/microbiology/faculty/sonenshein/index.html Homepage][SW|Jörg Stülke], University of Göttingen, Germany[http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage][SW|Fabian Commichau] University of Göttingen, Germany[http://genmibio.uni-goettingen.de/index.php?id=130 Homepage]References
Reviews
19698086,8299344,7705101,19895831,22625175 Enzymatic activity of RocG
18603778,16244435,16195607,18326565,9829940,20630473,21965396,25711804 Function in the control of [protein|87BCAE725B02860156D50E1783F6DB68510C811E|GltC] activity
15150225,17994626,17608797,17183217,20630473 Expression of ''rocG
12634342,15150224,10468601,9829940,22900538,20817675,25777015,25880922,27766092 Structural analysis of glutamate dehydrogenase
Bypass of ''rocG'' mutations
21219666,22178973,23785476 Additional publications
23338837,23419162,22178969,24473333