Results 41 to 50 of about 151,994 (387)

Hydroperoxylation by Hydroxyethylphosphonate Dioxygenase [PDF]

open access: yesJournal of the American Chemical Society, 2009
Hydroxyethylphosphonate dioxygenase (HEPD) catalyzes the O(2)-dependent cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate (2-HEP) to afford hydroxymethylphosphonate (HMP) and formate without input of electrons or use of any organic cofactors. Two mechanisms have been proposed to account for this reaction.
Whitteck, John T.   +2 more
openaire   +2 more sources

Indoleamine 2,3-Dioxygenase and Tolerance: Where Are We Now?

open access: yesFrontiers in Immunology, 2017
Cells expressing IDO suppress innate and adaptive immunity to promote tolerance by catabolizing the amino acid tryptophan (Trp) and other indole compounds.
A. Mellor, H. Lemos, Lei Huang
semanticscholar   +1 more source

First Betalain-Producing Bacteria Break the Exclusive Presence of the Pigments in the Plant Kingdom

open access: yesmBio, 2019
The biosynthesis of antioxidant pigments, namely, betalains, was believed to be restricted to Caryophyllales plants. This paper changes this paradigm, and enzyme mining from bacterial hosts promoted the discovery of bacterial cultures producing betalains.
Luis Eduardo Contreras-Llano   +4 more
doaj   +1 more source

Isolation and characterization of Alicycliphilus denitrificans strain BC, which grows on benzene with chlorate as the electron acceptor [PDF]

open access: yes, 2008
A bacterium, strain BC, was isolated from a benzene-degrading chlorate-reducing enrichment culture. Strain BC degrades benzene in conjunction with chlorate reduction.
Broeke, H., ten   +8 more
core   +2 more sources

Substrate stereo‐specificity in tryptophan dioxygenase and indoleamine 2,3‐dioxygenase [PDF]

open access: yesProteins: Structure, Function, and Bioinformatics, 2010
AbstractThe first and rate‐limiting step of the kynurenine pathway, in which tryptophan (Trp) is converted to N‐formylkynurenine is catalyzed by two heme‐containing proteins, Indoleamine 2,3‐dioxygenase (IDO), and Tryptophan 2,3‐dioxygenase (TDO). In mammals, TDO is found exclusively in liver tissue, IDO is found ubiquitously in all tissues.
Luciana, Capece   +5 more
openaire   +2 more sources

Does abscisic acid affect strigolactone biosynthesis? [PDF]

open access: yes, 2010
Strigolactones are considered a novel class of plant hormones that, in addition to their endogenous signalling function, are exuded into the rhizosphere acting as a signal to stimulate hyphal branching of arbuscular mycorrhizal (AM) fungi and germination
Adie   +76 more
core   +4 more sources

A co-conserved gene pair supports Caulobacter iron homeostasis during chelation stress

open access: yesJournal of Bacteriology
Synthetic metal chelators are widely used in industrial, clinical, and agricultural settings, leading to their accumulation in the environment. We measured the growth of Caulobacter crescentus, a soil and aquatic bacterium, in the presence of the ...
Sergio Hernandez-Ortiz   +4 more
doaj   +1 more source

The nitric oxide response in plant-associated endosymbiotic bacteria [PDF]

open access: yes, 2011
Nitric oxide (NO) is a gaseous signalling molecule which becomes very toxic due to its ability to react with multiple cellular targets in biological systems. Bacterial cells protect against NO through the expression of enzymes that detoxify this molecule
Andrew J. Gates   +57 more
core   +1 more source

Structure of an aromatic-ring-hydroxylating dioxygenase – naphthalene 1,2-dioxygenase [PDF]

open access: yesStructure, 1998
Pseudomonas sp. NCIB 9816-4 utilizes a multicomponent enzyme system to oxidize naphthalene to (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The enzyme component catalyzing this reaction, naphthalene 1,2-dioxygenase (NDO), belongs to a family of aromatic-ring-hydroxylating dioxygenases that oxidize aromatic hydrocarbons and related compounds to cis ...
Kauppi, Björn   +6 more
openaire   +2 more sources

RNAi-mediated suppression of three carotenoid-cleavage dioxygenase genes, OsCCD1, 4a, and 4b, increases carotenoid content in rice

open access: yesJournal of Experimental Botany, 2018
Knock-down of the carotenoid-cleavage dioxygenase OsCCD4a in rice enhances the content of carotenoids in leaves and seeds.
Miyoshi Ko   +6 more
semanticscholar   +1 more source

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