CDP-abequose synthase

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CDP-abequose synthase
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EC no. 1.1.1.341
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CDP-abequose synthase (EC 1.1.1.341, rfbJ (gene)) is an enzyme with systematic name CDP-alpha-D-abequose:NADP+ 4-oxidoreductase. [1] [2] [3] This enzyme catalyses the following chemical reaction

CDP-alpha-D-abequose + NADP+ CDP-4-dehydro-3,6-dideoxy-alpha-D-glucose + NADPH + H+

This enzyme is from Yersinia pseudotuberculosis and Salmonella enterica .

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Yersinia pestis is a gram-negative, non-motile, coccobacillus bacterium without spores that is related to both Yersinia enterocolitica and Yersinia pseudotuberculosis, the pathogen from which Y. pestis evolved and responsible for the Far East scarlet-like fever. It is a facultative anaerobic organism that can infect humans via the Oriental rat flea. It causes the disease plague, which caused the Plague of Justinian and the Black Death, the deadliest pandemic in recorded history. Plague takes three main forms: pneumonic, septicemic, and bubonic. Yersinia pestis is a parasite of its host, the rat flea, which is also a parasite of rats, hence Y. pestis is a hyperparasite.

<i>Yersinia enterocolitica</i> Species of bacterium

Yersinia enterocolitica is a Gram-negative, bacillus-shaped bacterium, belonging to the family Yersiniaceae. It is motile at temperatures of 22–29°C (72–84°F), but becomes nonmotile at normal human body temperature. Y. enterocolitica infection causes the disease yersiniosis, which is an animal-borne disease occurring in humans, as well as in a wide array of animals such as cattle, deer, pigs, and birds. Many of these animals recover from the disease and become carriers; these are potential sources of contagion despite showing no signs of disease. The bacterium infects the host by sticking to its cells using trimeric autotransporter adhesins.

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Yersinia pseudotuberculosis is a Gram-negative bacterium that causes Far East scarlet-like fever in humans, who occasionally get infected zoonotically, most often through the food-borne route. Animals are also infected by Y. pseudotuberculosis. The bacterium is urease positive.

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CDP-4-dehydro-6-deoxyglucose reductase (EC 1.17.1.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a CDP-paratose 2-epimerase is an enzyme that catalyzes the chemical reaction

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Alpha-aminoadipic semialdehyde synthase is an enzyme encoded by the AASS gene in humans and is involved in their major lysine degradation pathway. It is similar to the separate enzymes coded for by the LYS1 and LYS9 genes in yeast, and related to, although not similar in structure, the bifunctional enzyme found in plants. In humans, mutations in the AASS gene, and the corresponding alpha-aminoadipic semialdehyde synthase enzyme are associated with familial hyperlysinemia. This condition is inherited in an autosomal recessive pattern and is not considered a particularly negative condition, thus making it a rare disease.

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Yersiniabactin (Ybt) is a siderophore found in the pathogenic bacteria Yersinia pestis, Yersinia pseudotuberculosis, and Yersinia enterocolitica, as well as several strains of enterobacteria including enteropathogenic Escherichia coli and Salmonella enterica. Siderophores, compounds of low molecular mass with high affinities for ferric iron, are important virulence factors in pathogenic bacteria. Iron—an essential element for life used for such cellular processes as respiration and DNA replication—is extensively chelated by host proteins like lactoferrin and ferritin; thus, the pathogen produces molecules with an even higher affinity for Fe3+ than these proteins in order to acquire sufficient iron for growth. As a part of such an iron-uptake system, yersiniabactin plays an important role in pathogenicity of Y. pestis, Y. pseudotuberculosis, and Y. entercolitica.

CDP-paratose synthase (EC 1.1.1.342, rfbS (gene)) is an enzyme with systematic name CDP-alpha-D-paratose:NADP+ 4-oxidoreductase. This enzyme catalyses the following chemical reaction

Succinate-semialdehyde dehydrogenase (NADP+) (EC 1.2.1.79, succinic semialdehyde dehydrogenase (NADP+), succinyl semialdehyde dehydrogenase (NADP+), succinate semialdehyde:NADP+ oxidoreductase, NADP-dependent succinate-semialdehyde dehydrogenase, GabD) is an enzyme with systematic name succinate-semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction

(2,2,3-Trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase (EC 1.14.13.160, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase, OTEMO) is an enzyme with systematic name ((1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA,NADPH:oxygen oxidoreductase (1,5-lactonizing). This enzyme catalyses the following chemical reaction

Ditrans,polycis-polyprenyl diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase . This enzyme catalyses the following chemical reaction

The alpha-D-phosphohexomutases are a large superfamily of enzymes, with members in all three domains of life. Enzymes from this superfamily are ubiquitous in organisms from E. Coli to humans, and catalyze a phosphoryl transfer reaction on a phosphosugar substrate. Four well studied subgroups in the superfamily are:

  1. Phosphoglucomutase (PGM)
  2. Phosphoglucomutase/Phosphomannomutase (PGM/PMM)
  3. Phosphoglucosamine mutase (PNGM)
  4. Phosphoaceytlglucosamine mutase (PAGM)

References

  1. Kessler AC, Brown PK, Romana LK, Reeves PR (December 1991). "Molecular cloning and genetic characterization of the rfb region from Yersinia pseudotuberculosis serogroup IIA, which determines the formation of the 3,6-dideoxyhexose abequose". Journal of General Microbiology. 137 (12): 2689–95. doi: 10.1099/00221287-137-12-2689 . PMID   1724263.
  2. Wyk P, Reeves P (October 1989). "Identification and sequence of the gene for abequose synthase, which confers antigenic specificity on group B salmonellae: homology with galactose epimerase". Journal of Bacteriology. 171 (10): 5687–93. PMC   210415 . PMID   2793832.
  3. Thorson JS, Lo SF, Ploux O, He X, Liu HW (September 1994). "Studies of the biosynthesis of 3,6-dideoxyhexoses: molecular cloning and characterization of the asc (ascarylose) region from Yersinia pseudotuberculosis serogroup VA". Journal of Bacteriology. 176 (17): 5483–93. PMC   196737 . PMID   8071227.