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Literature summary for 1.17.1.4 extracted from

  • Wang, C.H.; Zhang, C.; Xing, X.H.
    Metabolic engineering of Escherichia coli cell factory for highly active xanthine dehydrogenase production (2017), Biores. Technol., 245, 1782-1789 .
    View publication on PubMed
Search for more literature for 1.17.1.4

Cloned(Commentary)

Cloned (Comment) Organism
gene Xdh, recombinant expression in Escherichia coli strain BL21(DE3), co-overexpression with three global regulators from Escherichia coli, IscS, TusA and NarJ and two Escherichia coli as well as two Rhodobacter capsulatus chaperone proteins, i.e. DsbA and DsbB, and NifS and XdhC (UniProt ID Q9X7K2), respectively, to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli Rhodobacter capsulatus

Protein Variants

Protein Variants Comment Organism
additional information succesfull mechanism-based metabolic engineering of Escherichia coli strain BL21(DE3) cell factory for production of functionally active, highly-producing xanthine dehydrogenase by co-overexpression of enzyme XDH from Rhodobacter capsulatus with three global regulators (IscS, TusA and NarJ) and four chaperone proteins (DsbA, DsbB, NifS and XdhC) to aid the formation and ordered assembly of three redox center cofactors of Rhodobacter capsulatus XDH in Escherichia coli. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH, method devlopment, overview. Three helper proteins, NifS, IscS and DsbB improve the specific activity of RcXDH significantly by 30%, 94% and 49%, respectively. The combination of NifS and IscS synergistically increases the specific activity by 1.29fold, and enhances the total enzyme activity by an impressive 3.9fold Rhodobacter capsulatus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the [Fe2-S2] redox center Rhodobacter capsulatus
Molybdenum molybdenum-containing flavoenzyme, in the molybdenum cofactor (Moco) Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xanthine + NAD+ + H2O Rhodobacter capsulatus when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH urate + NADH + H+
-
 ?
xanthine + NAD+ + H2O Rhodobacter capsulatus CGMCC 1.3366 when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH urate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus O54050 AND O54051 genes XdhA and XdhB
-
Rhodobacter capsulatus CGMCC 1.3366 O54050 AND O54051 genes XdhA and XdhB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xanthine + NAD+ + H2O
-
 Rhodobacter capsulatus urate + NADH + H+
-
 ?
xanthine + NAD+ + H2O when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH Rhodobacter capsulatus urate + NADH + H+
-
 ?
xanthine + NAD+ + H2O
-
 Rhodobacter capsulatus CGMCC 1.3366 urate + NADH + H+
-
 ?
xanthine + NAD+ + H2O when catalyzing the sequential oxidation of hypoxanthine to xanthine to uric acid, XDH uses the NAD+ as final electron receptor to produce NADH Rhodobacter capsulatus CGMCC 1.3366 urate + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
XDH
-
 Rhodobacter capsulatus
XdhC
-
 Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
FAD a molybdenum-containing flavoenzyme Rhodobacter capsulatus
molybdenum cofactor Moco Rhodobacter capsulatus
NAD+
-
 Rhodobacter capsulatus
[2Fe-2S]-center
-
 Rhodobacter capsulatus

General Information

General Information Comment Organism
additional information the biosynthesis of functionally active XDH is a multi-step process requiring a series of helper proteins to aid the formation of cofactors and apoproteins and their ordered assembly, in vivo biosynthetic mechanism of active xanthine dehydrogenase in schematic overview. NifS is a cysteine desulfurase, which catalyzes the sulfur transfer from L-cysteine to Moco to form Mo-S bond. Chaperone XDHC binds stoichiometric amount of Moco as a scaffold protein, interacts with NifS for the sulfuration of Moco, protects sulfurated Moco from oxidation, and further transfers to XDH Rhodobacter capsulatus