Trans-2,3-dihydro-3-hydroxyanthranilate isomerase

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Trans-2,3-dihydro-3-hydroxyanthranilate isomerase
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EC no. 5.3.3.17
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Trans-2,3-dihydro-3-hydroxyanthranilate isomerase (EC 5.3.3.17, phzF (gene)) is an enzyme with systematic name (5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate isomerase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate

The enzyme is involved in phenazine biosynthesis.

Related Research Articles

<i>Pseudomonas fluorescens</i> Species of bacterium

Pseudomonas fluorescens is a common Gram-negative, rod-shaped bacterium. It belongs to the Pseudomonas genus; 16S rRNA analysis as well as phylogenomic analysis has placed P. fluorescens in the P. fluorescens group within the genus, to which it lends its name.

<i>Pseudomonas aeruginosa</i> Species of bacterium

Pseudomonas aeruginosa is a common encapsulated, Gram-negative, aerobic–facultatively anaerobic, rod-shaped bacterium that can cause disease in plants and animals, including humans. A species of considerable medical importance, P. aeruginosa is a multidrug resistant pathogen recognized for its ubiquity, its intrinsically advanced antibiotic resistance mechanisms, and its association with serious illnesses – hospital-acquired infections such as ventilator-associated pneumonia and various sepsis syndromes.

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Phenazine is an organic compound with the formula (C6H4)2N2. It is a dibenzo annulated pyrazine, and the parent substance of many dyestuffs, such as the toluylene red, indulines, and safranines (and the closely related eurhodines). Phenazine crystallizes in yellow needles, which are only sparingly soluble in alcohol. Sulfuric acid dissolves it, forming a deep-red solution.

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In enzymology, a steroid Δ5-isomerase is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Pyocyanin</span> Chemical compound

Pyocyanin (PCN) is one of the many toxic compounds produced and secreted by the Gram negative bacterium Pseudomonas aeruginosa. Pyocyanin is a blue secondary metabolite, turning red below pH 4.9, with the ability to oxidise and reduce other molecules and therefore kill microbes competing against P. aeruginosa as well as mammalian cells of the lungs which P. aeruginosa has infected during cystic fibrosis. Since pyocyanin is a zwitterion at blood pH, it is easily able to cross the cell membrane. There are three different states in which pyocyanin can exist: oxidized (blue), monovalently reduced (colourless) or divalently reduced (red). Mitochondria play an important role in the cycling of pyocyanin between its redox states. Due to its redox-active properties, pyocyanin generates reactive oxygen species.

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Tilivalline is a nonribosomal enterotoxin and was the first naturally occurring pyrrolobenzodiazepine (PBD) to be associated with disease in the human intestine. Previous work has shown that PBD tilivalline produced by Klebsiella oxytoca was linked to the pathogenesis of colitis in animal model of antibiotic-associated hemorrhagic colitis (AAHC). Since the enteric bacterium K. oxytoca is part of the intestinal microbiota and tilivalline causes the pathogenesis of colitis, it is important to understand the biosynthesis and regulation of tilivalline activity.

Mathurin-Joseph Fordos was a French pharmaceutical chemist who was the first to examine what he named as pyocyanin, the blue pigment in pus produced by Pseudomonas aeruginosa. This was the first natural phenazine to be described. He also collaborated with Louis Daguerre and is thought to have been involved in producing one of the first photographs in 1837 of the Pont Neuf in Paris.

References

  1. Parsons JF, Song F, Parsons L, Calabrese K, Eisenstein E, Ladner JE (October 2004). "Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79". Biochemistry. 43 (39): 12427–35. doi:10.1021/bi049059z. PMID   15449932.
  2. Blankenfeldt W, Kuzin AP, Skarina T, Korniyenko Y, Tong L, Bayer P, Janning P, Thomashow LS, Mavrodi DV (November 2004). "Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens". Proceedings of the National Academy of Sciences of the United States of America. 101 (47): 16431–6. doi: 10.1073/pnas.0407371101 . PMC   534541 . PMID   15545603.
  3. Parsons JF, Calabrese K, Eisenstein E, Ladner JE (November 2004). "Structure of the phenazine biosynthesis enzyme PhzG" (PDF). Acta Crystallographica Section D. 60 (Pt 11): 2110–3. doi: 10.1107/s0907444904022474 . PMID   15502343.
  4. Mavrodi DV, Bleimling N, Thomashow LS, Blankenfeldt W (January 2004). "The purification, crystallization and preliminary structural characterization of PhzF, a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79". Acta Crystallographica Section D. 60 (Pt 1): 184–6. doi:10.1107/s090744490302571x. PMID   14684924.
  5. Ahuja EG, Janning P, Mentel M, Graebsch A, Breinbauer R, Hiller W, Costisella B, Thomashow LS, Mavrodi DV, Blankenfeldt W (December 2008). "PhzA/B catalyzes the formation of the tricycle in phenazine biosynthesis". Journal of the American Chemical Society. 130 (50): 17053–61. doi:10.1021/ja806325k. PMID   19053436.