Details of Host Protein-DME Interaction (HOSPPI)

General Information of Drug-Metabolizing Enzyme (DME ID: DME1139)
DME Name Beta-galactosidase (bgaB), Victivallis vadensis DME Info
UniProt ID
A0A2U1B4D0_9BACT
EC Number    EC: 3.2.1.23     (Click to Show/Hide the Complete EC Tree)
Hydrolases
Glycosylase
O/S-glycosyl compound glycosidase
EC: 3.2.1.23
Lineage    Species: Victivallis vadensis     (Click to Show/Hide the Complete Species Lineage)
Kingdom: Bacteria
Phylum: Lentisphaerae
Class: Lentisphaeria
Order: Victivallales
Family: Victivallaceae
Genus: Victivallis
Species: Victivallis vadensis
Subspecies: Victivallis vadensis ATCC BAA-548
Interactome
Disease Specific Interactions between Host Protein and DME (HOSPPI)
      Drug co-metabolism
               Cometabolized drug: PNA-D-glucopyranoside Click to Show/Hide the Full List of HOSPPI:        2 HOSPPI
                            Glucosidase II beta (PRKCSH) Click to Show/Hide the Cometabolization Info
DME ID DME0546 DME Info
Uniprot ID
GLU2B_HUMAN
Interaction Name PRKCSH-bgaB interaction [1], [2]
Description The interaction, between human Glucosidase II beta and Beta-galactosidase from Victivallis vadensis which collectively metabolize the drug PNA-D-glucopyranoside, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
                            Neutral alpha-glucosidase AB (GANAB) Click to Show/Hide the Cometabolization Info
DME ID DME0547 DME Info
Uniprot ID
GANAB_HUMAN
Interaction Name GANAB-bgaB interaction [1], [2]
Description The interaction, between human Neutral alpha-glucosidase AB and Beta-galactosidase from Victivallis vadensis which collectively metabolize the drug PNA-D-glucopyranoside, is reported to affect the efficacy, safety or bioavailability of this drug via interfering with it metabolism.
References
1 Identification and characterization of a novel beta-galactosidase from Victivallis vadensis ATCC BAA-548, an anaerobic fecal bacterium. J Microbiol. 2012 Dec;50(6):1034-40.
2 The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology. 2000 Aug;10(8):815-27.

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