On a non‐pyridine nucleotide‐dependent 2‐oxo‐acid reductase of broad substrate specificity from two Proteus species

@article{Neumann1984OnAN,
  title={On a non‐pyridine nucleotide‐dependent 2‐oxo‐acid reductase of broad substrate specificity from two Proteus species},
  author={Stefan Neumann and Helmut Simon},
  journal={FEBS Letters},
  year={1984},
  volume={167}
}
16 Citations
Chiral products from non-pyridine nucleotide-dependent reductases and methods for NAD(P)H regeneration.
TLDR
Two new types of non-pyridine nucleotide-dependent reductase have been identified which are suitable for electro-enzymic reductions in which catalytic amounts of viologens are continuously reduced in an electrochemical cell.
The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein.
TLDR
The membrane-bound non-pyridine nucleotide-dependent enzyme appears in the form of various oligomers of the 80-kDa monomer and belongs to the rare group of molybdoenzymes which possess no further prosthetic groups than the iron-sulphur clusters.
On The Use of Viologen Dyes for Stereospecific Bioreduction
TLDR
Every microorganism having a methylviologen-dependent NAD or NADP reductase can be applied for electromicrobial reductions and the stability of enzymes and pyridine nucleotides under different conditions is reported.
Enzymic Modification at the Mid‐Chain of Fatty Acids
The enzyme systems responsible for the range of mid-chain modifications of natural fatty acids could be considered for industrial scale exploitation. Regio- and stereospecificity of enzymes allows
Regeneration of NAD+ cofactor by photosensitized electron transfer in an immobilized alcohol dehydrogenase system
TLDR
The irradiation with visible light of a photosensitizer dye like methylene blue was used to regenerate by electron transfer the oxidized form of a pyridine nucleotide coenzyme (NAD+) and the enzyme immobilization strongly increased its stability.
Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase.
TLDR
The substrate specificity of dimethyl sulfoxide reductase (DmsABC) of Escherichia coli is characterized by determining Km and Kcat values for 22 different substrates, implicating Km as the major determinant of Kcat/Km values.
Effect of carbon sources and electron acceptors in the growth medium of Proteus spp. on the formation of (R)-2-hydroxycarboxylate viologen oxidoreductase and dimethylsulphoxide reductase
TLDR
The possible physiological role of the HVOR may be as a dissimilatory (R)-lactate dehydrogenase inroteus vulgaris and P. mirabilis and the organisms studied were significantly active with (S)- lactate and NH2CO-MV.
Biosynthesis of the methanogenic cofactors.
  • R. White
  • Chemistry, Biology
    Vitamins and hormones
  • 2001
...
1
2
...

References

SHOWING 1-10 OF 13 REFERENCES
Purification and Properties of Adenylyl Sulfate Reductase from the Phototrophic Sulfur Bacterium, Thiocapsa roseopersicina
TLDR
The properties of the enzyme are compared with those of adenylyl sulfate reductases purified from sulfate-reducing bacteria and thiobacilli and the influence of substrate concentrations on the activity of the enzymes was studied.
Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration
TLDR
Multienzyme reaction systems with simultaneous coenzyme regeneration have been investigated in a continuously operated membrane reactor at bench scale to obtain data which could be used in a kinetic model in order to predict the performance of an enzyme membrane reactor for the continuous production of L‐leucine.
ENZYMIC PROPERTIES OF MALATE DEHYDROGENASE OF BACILLUS SUBTILIS.
  • A. Yoshida
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1965
Disk-Elektrophorese
  • 1968
...
1
2
...