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  • pyruvate
  • Kinetic Properties of Pyruvate Ferredoxin Oxidoreductase of Intestinal Sulfate-Reducing Bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. (pjmonline.org)
  • In this paper we present for the first time the specific activity of pyruvate-ferredoxin oxidoreductase and the kinetic properties of the enzyme in cell-free extracts of both D. piger Vib-7 and Desulfomicrobium sp. (pjmonline.org)
  • The spectral analysis of the puri-fied pyruvate-ferredoxin oxidoreductase from the cell-free extracts was demonstrated. (pjmonline.org)
  • Initial (instantaneous) reaction velocity (V0), maximum amount of the product of reaction (Pmax), the reaction time (half saturation period) and maximum velocity of the pyruvate-ferredoxin oxidoreductase reaction (Vmax) were defined. (pjmonline.org)
  • The reaction of this enzyme has been most exten-sively studied in the forward (oxidative decarboxyla-tion) direction beginning with a series of seminal stud-ies published in 1971 by Raeburn and Rabinowitz which have isolated and characterized pyruvate-ferredoxin oxidoreductase. (pjmonline.org)
  • As far as we are aware, pyruvate-ferredoxin oxidoreductase from intestinal sulfate-reducing bacteria D. piger and Desulfomicrobium sp. (pjmonline.org)
  • enzymology
  • In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction an aldehyde + H2O + 2 oxidized ferredoxin ⇌ {\displaystyle \rightleftharpoons } an acid + 2 H+ + 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. (wikipedia.org)
  • In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction (indol-3-yl)pyruvate + CoA + oxidized ferredoxin ⇌ {\displaystyle \rightleftharpoons } S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin The 3 substrates of this enzyme are (indol-3-yl)pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are S-2-(indol-3-yl)acetyl-CoA, CO2, and reduced ferredoxin. (wikipedia.org)
  • In enzymology, a quinaldate 4-oxidoreductase (EC 1.3.99.18) is an enzyme that catalyzes the chemical reaction quinaldate + acceptor + H2O ⇌ {\displaystyle \rightleftharpoons } kynurenate + reduced acceptor The 3 substrates of this enzyme are quinaldate, acceptor, and H2O, whereas its two products are kynurenate and reduced acceptor. (wikipedia.org)
  • In enzymology, a glucose-fructose oxidoreductase (EC 1.1.99.28) is an enzyme that catalyzes the chemical reaction D-glucose + D-fructose ⇌ {\displaystyle \rightleftharpoons } D-gluconolactone + D-glucitol Thus, the two substrates of this enzyme are D-glucose and D-fructose, whereas its two products are D-gluconolactone and D-glucitol. (wikipedia.org)
  • In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction H2 + quinone ⇌ {\displaystyle \rightleftharpoons } quinol Thus, the two substrates of this enzyme are H2 and quinone, whereas its product is quinol. (wikipedia.org)
  • anaerobic
  • The role of the aerobic phase is to produce sufficiently high cell mass (12.9-14.6 g/l dry weight) and to activate the aerobic branch of the Klebsiella glycerol pathway, whereas in the anaerobic phase there is a rapid initiation of 1,3-propanediol oxidoreductase formation. (springer.com)
  • A fast change from an aerobic to an anaerobic environment led to a redox imbalance, which resulted in the abrupt activation of the anaerobic branch of glycerol utilization, with the occurrence of a high 1,3-propanediol-oxidoreductase activity. (springer.com)
  • PMID
  • A number of different prokaryotic oxidoreductases that require and bind a molybdopterin cofactor have been shown [ PMID: 2015248 , PMID: 3062312 , PMID: 8125918 ] to share a number of regions of sequence similarity. (ebi.ac.uk)