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Literature summary for 1.17.1.4 extracted from

  • Sarauli, D.; Borowski, A.; Peters, K.; Schulz, B.; Fattakhova-Rohlfing, D.; Leimkuehler, S.; Lisdat, F.
    Investigation of the pH-dependent impact of sulfonated polyaniline on bioelectrocatalytic activity of xanthine dehydrogenase (2016), ACS Catal., 6, 7152-7159 .
No PubMed abstract available
Search for more literature for 1.17.1.4

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain TP1000 Rhodobacter capsulatus

Protein Variants

Protein Variants Comment Organism
additional information pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Macroporous ITO electrodes are used as an immobilization platform for the fabrication of HX-sensitive electrodes. The efficient polymer/enzyme interaction can be advantageously combined with the open structure of an electrode material of controlled pore size, resulting in good processability, stability, and defined signal transfer in the presence of a substrate. Method development and evaluation, overview Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxanthine + NAD+ + 2 H2O Rhodobacter capsulatus
-
 urate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus O54050 AND O54051 small and large subunits encoded by genes xdhA and xdhB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain TP1000 by nickel affinity and anion exchange chromatography, followed by gel filtration Rhodobacter capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + NAD+ + 2 H2O
-
 Rhodobacter capsulatus urate + NADH + H+
-
 ?
additional information pH-dependent bioelectrocatalytic activity of the redox enzyme xanthine dehydrogenase (XDH) in the presence of sulfonated polyaniline PMSA1 (poly(2-methoxyaniline-5-sulfonic acid)-co-aniline), electron transfer from the hypoxanthine (HX)-reduced enzyme to the polymer. The enzyme shows bioelectrocatalytic activity on indium tin oxide (ITO) electrodes, when the polymer is present. Depending on solution pH, different processes can be identified. Not only product-based communication with the electrode but also efficient polymer-supported bioelectrocatalysis occur. Substrate-dependent catalytic currents can be obtained in acidic and neutral solutions, although the highest activity of XDH with natural reaction partners is in the alkaline region. Operation of the enzyme electrode without addition of the natural cofactor of XDH is feasible. Method development and evaluation, overview Rhodobacter capsulatus ?
-
 ?

Synonyms

Synonyms Comment Organism
XDH
-
 Rhodobacter capsulatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Rhodobacter capsulatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Rhodobacter capsulatus

pH Range

pH Minimum pH Maximum Comment Organism
4.5 9 the enzyme is highly active at pH 5.0-8.0, shows low activity at pH 9.0, and is inactive above Rhodobacter capsulatus