Details of Host Protein-DME Interaction (HOSPPI)

General Information of Drug-Metabolizing Enzyme (DME ID: DME1346)
DME Name Glutamate decarboxylase (gadB), Bifidobacterium angulatum DME Info
UniProt ID
A0A126SV18_9BIFI
EC Number    EC: 4.1.1.15     (Click to Show/Hide the Complete EC Tree)
Lyases
Carbon-carbon lyase
Carboxy-lyase
EC: 4.1.1.15
Lineage    Species: Bifidobacterium angulatum     (Click to Show/Hide the Complete Species Lineage)
Kingdom: Bacteria
Phylum: Actinobacteria
Class: Actinobacteria
Order: Bifidobacteriales
Family: Bifidobacteriaceae
Genus: Bifidobacterium
Species: Bifidobacterium angulatum
Interactome
Disease Specific Interactions between Host Protein and DME (HOSPPI)
      Drug co-metabolism
               Cometabolized drug: L-glutamine Click to Show/Hide the Full List of HOSPPI:      18 HOSPPI
                            Asparagine synthetase (ASNS) Click to Show/Hide the Cometabolization Info
DME ID DME0154 DME Info
Uniprot ID
ASNS_HUMAN
Interaction Name ASNS-gadB interaction [1], [2]
Description The interaction, between human Asparagine synthetase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Glutamate-cysteine ligase catalytic (GCLC) Click to Show/Hide the Cometabolization Info
DME ID DME0485 DME Info
Uniprot ID
GSH1_HUMAN
Interaction Name GCLC-gadB interaction [1], [3]
Description The interaction, between human Glutamate-cysteine ligase catalytic and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Glutamate-cysteine ligase regulatory (GCLM) Click to Show/Hide the Cometabolization Info
DME ID DME0486 DME Info
Uniprot ID
GSH0_HUMAN
Interaction Name GCLM-gadB interaction [1], [4]
Description The interaction, between human Glutamate-cysteine ligase regulatory and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Glutamine amidotransferase (GMPS) Click to Show/Hide the Cometabolization Info
DME ID DME0159 DME Info
Uniprot ID
GUAA_HUMAN
Interaction Name GMPS-gadB interaction [1], [5]
Description The interaction, between human Glutamine amidotransferase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Glutamine-dependent NAD(+) synthetase (NADSYN1) Click to Show/Hide the Cometabolization Info
DME ID DME0155 DME Info
Uniprot ID
NADE_HUMAN
Interaction Name NADSYN1-gadB interaction [1], [6]
Description The interaction, between human Glutamine-dependent NAD(+ synthetase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Glutaminyl-tRNA synthetase (GLNRS) Click to Show/Hide the Cometabolization Info
DME ID DME0157 DME Info
Uniprot ID
SYQ_HUMAN
Interaction Name GLNRS-gadB interaction [1], [7]
Description The interaction, between human Glutaminyl-tRNA synthetase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Glutamyl-tRNA(Gln) amidotransferase B (GATB) Click to Show/Hide the Cometabolization Info
DME ID DME0158 DME Info
Uniprot ID
GATB_HUMAN
Interaction Name GATB-gadB interaction [1], [8]
Description The interaction, between human Glutamyl-tRNA(Gln amidotransferase B and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Hexosephosphate aminotransferase 2 (GFPT2) Click to Show/Hide the Cometabolization Info
DME ID DME0156 DME Info
Uniprot ID
GFPT2_HUMAN
Interaction Name GFPT2-gadB interaction [1], [8]
Description The interaction, between human Hexosephosphate aminotransferase 2 and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Kynurenine aminotransferase I (KYAT1) Click to Show/Hide the Cometabolization Info
DME ID DME0160 DME Info
Uniprot ID
KAT1_HUMAN
Interaction Name KYAT1-gadB interaction [1], [9]
Description The interaction, between human Kynurenine aminotransferase I and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            L-glutamine amidohydrolase (GLS) Click to Show/Hide the Cometabolization Info
DME ID DME0126 DME Info
Uniprot ID
GLSK_HUMAN
Interaction Name GLS-gadB interaction [1], [10]
Description The interaction, between human L-glutamine amidohydrolase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            N-acetylglutamate synthase (NAGS) Click to Show/Hide the Cometabolization Info
DME ID DME0534 DME Info
Uniprot ID
NAGS_HUMAN
Interaction Name NAGS-gadB interaction [1], [11]
Description The interaction, between human N-acetylglutamate synthase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Phosphoribosylformylglycinamidine synthase (PFAS) Click to Show/Hide the Cometabolization Info
DME ID DME0161 DME Info
Uniprot ID
PUR4_HUMAN
Interaction Name PFAS-gadB interaction [1], [8]
Description The interaction, between human Phosphoribosylformylglycinamidine synthase and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Transglutaminase E (TGM3) Click to Show/Hide the Cometabolization Info
DME ID DME0165 DME Info
Uniprot ID
TGM3_HUMAN
Interaction Name TGM3-gadB interaction [1], [8]
Description The interaction, between human Transglutaminase E and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Transglutaminase H (TGM2) Click to Show/Hide the Cometabolization Info
DME ID DME0162 DME Info
Uniprot ID
TGM2_HUMAN
Interaction Name TGM2-gadB interaction [1], [12]
Description The interaction, between human Transglutaminase H and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Transglutaminase K (TGM1) Click to Show/Hide the Cometabolization Info
DME ID DME0166 DME Info
Uniprot ID
TGM1_HUMAN
Interaction Name TGM1-gadB interaction [1], [13]
Description The interaction, between human Transglutaminase K and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Transglutaminase X (TGM5) Click to Show/Hide the Cometabolization Info
DME ID DME0163 DME Info
Uniprot ID
TGM5_HUMAN
Interaction Name TGM5-gadB interaction [1], []
Description The interaction, between human Transglutaminase X and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Transglutaminase Y (TGM6) Click to Show/Hide the Cometabolization Info
DME ID DME0164 DME Info
Uniprot ID
TGM3L_HUMAN
Interaction Name TGM6-gadB interaction [1], [8]
Description The interaction, between human Transglutaminase Y and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Transglutaminase Z (TGM7) Click to Show/Hide the Cometabolization Info
DME ID DME0167 DME Info
Uniprot ID
TGM7_HUMAN
Interaction Name TGM7-gadB interaction [1], [8]
Description The interaction, between human Transglutaminase Z and Glutamate decarboxylase from Bifidobacterium angulatum which collectively metabolize the drug L-glutamine, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
References
1 GABA production and structure of gadB/gadC genes in Lactobacillus and Bifidobacterium strains from human microbiota. Anaerobe. 2016 Dec;42:197-204.
2 A convenient gHMQC-based NMR assay for investigating ammonia channeling in glutamine-dependent amidotransferases: studies of Escherichia coli asparagine synthetase B. Biochemistry. 2007 Apr 24;46(16):4840-9.
3 Kinetic measurement by LC/MS of gamma-glutamylcysteine ligase activity. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Nov 15;827(1):32-8.
4 The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase. Adv Enzymol Relat Areas Mol Biol. 1999;73:209-67, xii.
5 Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry. 2007 May 1;46(17):5131-9.
6 Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste. J Biol Chem. 2006 Nov 3;281(44):33395-402.
7 Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases. Bioorg Med Chem. 2007 Jan 1;15(1):295-304.
8 How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.
9 Determination of kynurenic acid in human serum and its correlation with the concentration of certain amino acids. Clin Chim Acta. 2007 Feb;377(1-2):174-8.
10 Full-length human glutaminase in complex with an allosteric inhibitor. Biochemistry. 2011 Dec 20;50(50):10764-70.
11 Biochemical properties of recombinant human and mouse N-acetylglutamate synthase. Mol Genet Metab. 2006 Mar;87(3):226-32.
12 Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2. Protein Sci. 2006 Nov;15(11):2466-80.
13 A three-dimensional model of the human transglutaminase 1: insights into the understanding of lamellar ichthyosis. J Mol Model. 2007 Jan;13(1):233-46.

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