Details of Xenobiotics-DME Interaction (XEOTIC)

General Information of Drug-Metabolizing Enzyme (DME ID: DME1512)
DME Name L-Lactate dehydrogenase (ldh), Lactobacillus casei DME Info
UniProt ID
LDH_LACCA
EC Number    EC: 1.1.1.27     (Click to Show/Hide the Complete EC Tree)
Oxidoreductase
CH-OH donor oxidoreductase
NAD/NADP oxidoreductase
EC: 1.1.1.27
Lineage    Species: Lactobacillus casei     (Click to Show/Hide the Complete Species Lineage)
Kingdom: Bacteria
Phylum: Firmicutes
Class: Bacilli
Order: Lactobacillales
Family: Lactobacillaceae
Genus: Lactobacillus
Species: Lactobacillus casei
Subspecies: Lactobacillus casei ATCC 393
Interactome
Interactions between Xenobiotics and DME (XEOTIC)
      Amino Acid(s), Peptide(s) or Protein(s)
                  Peptide Click to Show/Hide the Full List of Xenobiotics:      11 Xenobiotics
                              Bacteriocin lacticin Q Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO03771   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Bacteriocin lacticin Q inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [1]
                              Bacteriocin lactocyclicin Q Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO03775   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Bacteriocin lactocyclicin Q inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei (MIC = 2.27 microM) [2], [3]
                              Bacteriocin LSEI_2163 Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO03967   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Bacteriocin LSEI_2163 inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [4]
                              Lantibiotic carnocin-UI49 Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO03803   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Lantibiotic carnocin-UI49 inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [5]
                              Nosiheptide Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO04332   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Nosiheptide inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei (MIC = 0.003 ug/ml) [6], [7]
                              Penocin A Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO04521   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Penocin A inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [8], [9]
                              Plantaricin E Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO04616   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Plantaricin E inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei (MIC = 0.02 microM) [10], [11]
                              Plantaricin F Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO04617   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Plantaricin F inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei (MIC = 0.02 microM) [11], [12]
                              Subpeptin JM4-A Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO05004   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Subpeptin JM4-A inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [13]
                              Subpeptin JM4-B Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO05005   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Subpeptin JM4-B inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [13]
                              Weissellin-A Click to Show/Hide the Detail Inhibition
                                 XEOTIC ID XEO05283   XEOTIC Info Gene Form Protein
                                 Classification Peptide
                                 DME Modulation Weissellin-A inhibits the drug-metabolizing activity of L-Lactate dehydrogenase (ldh) from Lactobacillus casei [14]
References
1 Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of gram-positive bacteria. Appl Environ Microbiol. 2007 May;73(9):2871-7.
2 Identification and characterization of lactocyclicin Q, a novel cyclic bacteriocin produced by Lactococcus spstrain QU 12. Appl Environ Microbiol. 2009 Mar;75(6):1552-8.
3 Identification and characterization of leucocyclicin Q, a novel cyclic bacteriocin produced by Leuconostoc mesenteroides TK41401. Appl Environ Microbiol. 2011 Nov;77(22):8164-70.
4 Characterization of putative class II bacteriocins identified from a non-bacteriocin-producing strain Lactobacillus casei ATCC 334. Appl Microbiol Biotechnol. 2013 Jan;97(1):237-46.
5 Purification and characterization of a new bacteriocin isolated from a Carnobacterium sp. Appl Environ Microbiol. 1992 May;58(5):1417-22.
6 Nosiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework. ACS Chem Biol. 2009 Oct 16;4(10):855-64.
7 Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin. Mol Cell. 2008 Apr 11;30(1):26-38.
8 Comparative genomics of the lactic acid bacteria. Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15611-6.
9 Data mining and characterization of a novel pediocin-like bacteriocin system from the genome of Pediococcus pentosaceus ATCC 25745. Microbiology. 2006 Jun;152(Pt 6):1649-59.
10 The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system. Appl Environ Microbiol. 1994 Jan;60(1):160-6.
11 Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. Biochim Biophys Acta. 2008 Nov;1784(11):1711-9.
12 Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A. Appl Environ Microbiol. 1998 Jun;64(6):2269-72.
13 Purification and characterization of two novel antimicrobial peptides Subpeptin JM4-A and Subpeptin JM4-B produced by Bacillus subtilis JM4. Curr Microbiol. 2005 Nov;51(5):292-6.
14 Purification, amino acid sequence and characterization of the class IIa bacteriocin weissellin A, produced by Weissella paramesenteroides DX. Bioresour Technol. 2011 Jun;102(12):6730-4.

If you find any error in data or bug in web service, please kindly report it to Dr. Yin and Dr. Li.