Pyruvate:quinone oxidoreductases (PQOs) catalyse the oxidative decarboxylation of pyruvate to acetate and concomitant reduction of quinone to quinol with the release of CO2. They are thiamine pyrophosphate (TPP) and flavin-adenine dinucleotide (FAD) containing enzymes, which interact with the membrane in a monotopic way.
Sousa F M +2 more
exaly +3 more sources
A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. [PDF]
Cysteine (Cys) residues often play critical roles in proteins, for example, in the formation of structural disulfide bonds, metal binding, targeting proteins to the membranes, and various catalytic functions.
Stefano M Marino, Vadim N Gladyshev
doaj +3 more sources
ABSTRACT The high stereo- and substrate specificities of enzymes have been utilized for microdetermination of amino acids. Here, I review the discovery of l-Arg oxidase from Pseudomonas sp. TPU 7192, l-Lys oxidase/decarboxylase from Burkholderia sp. AIU 395, and enzymes showing apparent l-His oxidase activity from Achromobacter sp.
Daisuke Matsui, Matsui Daisuke
exaly +3 more sources
Dihydroorotate:quinone oxidoreductases (DHOQOs) are membrane bound enzymes responsible for oxidizing dihydroorotate (DHO) to orotate with concomitant reduction of quinone to quinol. They have FMN as prosthetic group and are part of the monotopic quinone reductase superfamily.
Sousa F M, Manuela M Pereira
exaly +3 more sources
An analysis of amino acid composition of a few oxidoreductases by different methods
1. All methods used to analyze amino acid composition of different enzymes agree well with each other. 2. They lead to a relationship between amino acid composition and function of proteins. 3. Cytochrome oxidase is in a class by itself; copper-containing oxidases are closely related as expected.
A, Naqui, J C, Vincent
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FAD/NADH Dependent Oxidoreductases: From Different Amino Acid Sequences to Similar Protein Shapes for Playing an Ancient Function [PDF]
Flavoprotein oxidoreductases are members of a large protein family of specialized dehydrogenases, which include type II NADH dehydrogenase, pyridine nucleotide-disulphide oxidoreductases, ferredoxin-NAD+ reductases, NADH oxidases, and NADH peroxidases, playing a crucial role in the metabolism of several prokaryotes and eukaryotes.
Anna De Grassi +2 more
exaly +4 more sources
Diverging Mineral Chemistry of Iron and Nickel Throughout Earth’s Changing Redox Conditions Reveals Foundation for Their Evolution as Protein Cofactors [PDF]
Iron (Fe) and nickel (Ni) were both foundational to early metabolism, yet their biological trajectories diverged as Earth’s surface redox state changed.
Benjamin I. Jelen +4 more
doaj +2 more sources
Comparative fecal microbiome analysis of the endangered Volcano rabbit (Romerolagus diazi) reveals a microbial core in contrasting habitats of Central Mexico. [PDF]
Herbivores show a larger microbial diversity in their guts than omnivores or carnivores. Bacterial symbionts expand the host digestion capacity by fermenting cellulose and hemicellulose. Comparisons between populations in different distribution areas can
Leslie M Montes-Carreto +3 more
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Ferredoxin-NADP(+) oxidoreductases (FNRs) of Bacillus subtilis (YumC) and Rhodopseudomonas palustris CGA009 (RPA3954) belong to a novel homo-dimeric type of FNR with high amino acid sequence homology to NADPH-thioredoxin reductases. These FNRs were purified from expression constructs in Escherichia coli cells, and their steady-state reactions with [2Fe-
Daisuke Seo, Takeshi Sakurai
exaly +3 more sources
Phosphite inhibits Phytophthora cinnamomi by downregulating oxidoreductases and disrupting energy metabolism [PDF]
Phytophthora root rot caused by the hemibiotrophic oomycete, Phytophthora cinnamomi is a major biotic hindrance in meeting the ever-increasing demand for avocados.
S. Ashok Prabhu +11 more
doaj +2 more sources

