نتایج جستجو برای: oxidoreductases

تعداد نتایج: 1064  

2012
Veronica Sanda Chedea Mitsuo Jisaka

Lipoxygenases (EC 1.13.11.12, linoleate:oxygen, oxidoreductases, LOXs) which are widely found in plants, fungi, and animals, are a large monomeric protein family with non-heme, non-sulphur, iron cofactor containing dioxygenases that catalyze the oxidation of polyunsaturated fatty acids (PUFA) as substrate with at least one 1Z, 4Z-pentadiene moiety such as linoleic, linolenic and arachidonic aci...

2007
Richard Cammack

The conventional assay method for the majority of enzymes envisages a reaction between substrates in aqueous solution. A measurable concentration of product is accumulated over time. This paradigm has served well for the characterization of many enzymes. Variations of the method, often using chromogenic or fluorogenic substrates, have been developed and are widely used for purposes such as clin...

2017
Blair Ney Carlo R. Carere Richard Sparling Thanavit Jirapanjawat Matthew B. Stott Colin J. Jackson John G. Oakeshott Andrew C. Warden Chris Greening

F420 is a microbial cofactor that mediates a wide range of physiologically important and industrially relevant redox reactions, including in methanogenesis and tetracycline biosynthesis. This deazaflavin comprises a redox-active isoalloxazine headgroup conjugated to a lactyloligoglutamyl tail. Here we studied the catalytic significance of the oligoglutamate chain, which differs in length betwee...

Journal: :Integrative biology : quantitative biosciences from nano to macro 2012
Arye Harel Paul Falkowski Yana Bromberg

Non-equilibrium catalysis of electron transfer reactions (i.e. redox) regulates the flux of key elements found in biological macromolecules. The enzymes responsible, oxidoreductases, contain specific transition metals in poorly sequence-conserved domains. These domains evolved ∼2.4 billion years ago in microbes and spread across the tree of life. We lack understanding of how oxidoreductases evo...

2009
Lawrence P. Wackett

Biocat collection http://www.biocatcollection.net/cms/ The Biocat collection is a repository of organisms and enzymes that are available for screening or other uses in biocatalysis. The collection includes oxidoreductases, hydrolases, lyases and polymerases. BRENDA http://www.brenda-enzymes.info/ BRENDA is a comprehensive database of enzymes organized with practical usage in mind. There is exte...

Journal: :Journal of bacteriology 1995
N K Heinzinger S Y Fujimoto M A Clark M S Moreno E L Barrett

The phs chromosomal locus of Salmonella typhimurium is essential for the dissimilatory anaerobic reduction of thiosulfate to hydrogen sulfide. Sequence analysis of the phs region revealed a functional operon with three open reading frames, designated phsA, phsB, and phsC, which encode peptides of 82.7, 21.3, and 28.5 kDa, respectively. The predicted products of phsA and phsB exhibited significa...

2004
James C. A. Bardwell

In Escherichia coli, a family of periplasmic disulfide oxidoreductases catalyzes correct disulfide bond formation in periplasmic and secreted proteins. Despite the importance of native disulfide bonds in the folding and function of many proteins, a systematic investigation of the in vivo substrates of E. coli periplasmic disulfide oxidoreductases, including the well characterized oxidase DsbA, ...

Journal: :Applied and environmental microbiology 2012
Xuan Wang Elliot N Miller Lorraine P Yomano K T Shanmugam Lonnie O Ingram

Expression arrays were used to identify 4 putative oxidoreductases that were upregulated (>3-fold) by furfural (15 mM, 15 min). Plasmid expression of one (ucpA) increased furan tolerance in ethanologenic strain LY180 and wild-type strain W. Deleting ucpA decreased furfural tolerance. Although the mechanism remains unknown, the cryptic ucpA gene is now associated with a phenotype: furan resistance.

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