Database for Polyphenol Utilized Proteins from gut microbiota
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Subfamily Sequences


Literature Information

Title Identification and functional expression of genes encoding flavonoid O‐ and C‐glycosidases in intestinal bacteria
Author Annett Braune, Wolfram Engst, Michael Blaut
DOI 10.1111/1462-2920.12864
Abstract Gut bacteria play a crucial role in the metabolism of dietary flavonoids and thereby influence the bioactivity of these compounds in the host. The intestinal Lachnospiraceae strain CG19‐1 and Eubacterium cellulosolvens are able to deglycosylate C‐ and O‐coupled flavonoid glucosides. Growth of strain CG19‐1 in the presence of the isoflavone C‐glucoside puerarin (daidzein 8‐C‐glucoside) led to the induction of two proteins (DfgC, DfgD). Heterologous expression of the encoding genes (dfgC, dfgD) in Escherichia coli revealed no C‐deglycosylating activity in the resulting cell extracts but cleavage of flavonoid O‐glucosides such as daidzin (daidzein 7‐O‐glucoside). The recombinant DfgC and DfgD proteins were purified and characterized with respect to their quaternary structure, substrate and cofactor specificity. The products of the corresponding genes (dfgC, dfgD) from E. cellulosolvens also catalysed the O‐deglycosylation of daidzin following their expression in E. coli. In combination with three recombinant proteins encoded by adjacent genes in E. cellulosolvens (dfgA, dfgB, dfgE), DfgC and DfgD from E. cellulosolvens catalysed the deglycosylation of the flavone C‐glucosides homoorientin (luteolin 6‐C‐glucoside) and isovitexin (apigenin 6‐C‐glucoside). Even intact cells of E. coli expressing the five E. cellulosolvens genes cleaved these flavone C‐glucosides and, also, flavonoid O‐glucosides to the corresponding aglycones.

Experimental results

  • Enzyme

Uniprot ID: I5AX49

Protein: Uncharacterized protein

Organism: [Eubacterium] cellulosolvens 6

Length: 147 AA

Taxonomic identifier: 633697 [NCBI]

  • Pfam
Source Domain Start End E-value (Domain) Coverage
Pfam-A - - - - -

Program: hmmscan

Version: 3.1b2 (February 2015)

Method: hmmscan --domtblout hmmscan.tbl --noali -E 1e-5 pfam query.fa

Date: Mon Jul 20 14:32:16 2020

Description:

None

  • Reaction

Catalyse reaction with expression of I5AX46/I5AX47/I5AX48/I5AX49/I5AX50 simultaneously

daidzindaidzein + glucose

[L1]daidzin
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[R1]daidzein
plus
[R2]glucose

References


  1. Holm L, Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease[J]. Proteins: Structure, Function, and Bioinformatics, 1997, 28(1): 72-82. 

  2. Nygaard P, Duckert P, Saxild H H. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis[J]. Journal of Bacteriology, 1996, 178(3): 846-853. 

  3. Jabri E, Carr M B, Hausinger R P, et al. The crystal structure of urease from Klebsiella aerogenes[J]. Science, 1995, 268(5213): 998-1004. 


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