Pseudomonas denitrificans

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Pseudomonas denitrificans
Scientific classification OOjs UI icon edit-ltr.svg
Domain: Bacteria
Phylum: Pseudomonadota
Class: Gammaproteobacteria
Order: Pseudomonadales
Family: Pseudomonadaceae
Genus: Pseudomonas
Species:
P. denitrificans
Binomial name
Pseudomonas denitrificans
Bergey, et al. 1961
Type strain
ATCC 19244

CCEB 525
IAM 12023
NCIMB 1656
NCTC 1656
NRRL B-1028

Pseudomonas denitrificans is a Gram-negative aerobic bacterium that performs denitrification. It was first isolated from garden soil in Vienna, Austria. It overproduces cobalamin (vitamin B12), which it uses for methionine synthesis [1] and it has been used for manufacture of the vitamin. [2] Scientists at Rhône-Poulenc Rorer took a genetically engineered strain of the bacteria, in which eight of the cob genes involved in the biosynthesis of the vitamin had been overexpressed, to establish the complete sequence of methylation and other steps in the cobalamin pathway. [3] [4]

Based on 16S rRNA analysis, P. denitrificans has been placed in the P. pertucinogena group. [5]

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<span class="mw-page-title-main">Cobalamin riboswitch</span>

Cobalamin riboswitch is a cis-regulatory element which is widely distributed in 5' untranslated regions of vitamin B12 (Cobalamin) related genes in bacteria.

<span class="mw-page-title-main">Precorrin-2 C20-methyltransferase</span>

In enzymology, a precorrin-2 C20-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Precorrin-3B C17-methyltransferase</span>

In enzymology, precorrin-3B C17-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a precorrin-4 C11-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Precorrin-6A synthase (deacetylating)</span>

In enzymology, precorrin-6A synthase (deacetylating) (EC 2.1.1.152) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Precorrin-6Y C5,15-methyltransferase (decarboxylating)</span>

In enzymology, a precorrin-6Y C5,15-methyltransferase (decarboxylating) (EC 2.1.1.132) is an enzyme that catalyzes the chemical reaction

In enzymology, a precorrin-6A reductase (EC 1.3.1.54) is an enzyme that catalyzes the chemical reaction

In enzymology, a precorrin-3B synthase (EC 1.14.13.83) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Precorrin-8X methylmutase</span>

In enzymology, a precorrin-8X methylmutase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cobalt chelatase</span> Enzyme

Cobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) (EC 6.3.5.9) is an enzyme that catalyzes the chemical reaction

Vitamin B<sub><small>12</small></sub> Vitamin used in animal cells metabolism

Vitamin B12, also known as cobalamin, is a water-soluble vitamin involved in metabolism. It is one of eight B vitamins. It is required by animals, which use it as a cofactor in DNA synthesis, and in both fatty acid and amino acid metabolism. It is important in the normal functioning of the nervous system via its role in the synthesis of myelin, and in the circulatory system in the maturation of red blood cells in the bone marrow. Plants do not need cobalamin and carry out the reactions with enzymes that are not dependent on it.

<span class="mw-page-title-main">Nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase</span>

In enzymology, a nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cob(I)yrinic acid a,c-diamide adenosyltransferase</span> Class of enzymes

In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.

<span class="mw-page-title-main">Cobalamin biosynthesis</span>

Cobalamin biosynthesis is the process by which bacteria and archea make cobalamin, vitamin B12. Many steps are involved in converting aminolevulinic acid via uroporphyrinogen III and adenosylcobyric acid to the final forms in which it is used by enzymes in both the producing organisms and other species, including humans who acquire it through their diet.

Adenosylcobinamide-GDP ribazoletransferase is an enzyme with systematic name adenosylcobinamide-GDP:alpha-ribazole ribazoletransferase. This enzyme catalyses the following chemical reaction

Shimwellia blattae is a species of bacterium, one of two in the genus Shimwellia. It is an aerobic enteric bacterium first isolated from the hindgut of cockroaches. Although it is related to human pathogens, including Escherichia coli, S. blattae is not pathogenic to humans. It is notable for its ability to synthesize vitamin B12 de novo.

References

  1. Lago BD, and Demain AL (1969). "Alternate requirement for vitamin B12 or methionine in mutants of Pseudomonas denitrificans, a vitamin B12-producing bacterium". J Bacteriol. 99 (1): 347–9. doi:10.1128/jb.99.1.347-349.1969. PMC   250011 . PMID   5802615.
  2. Fang, H; Kang, J; Zhang, D (30 January 2017). "Microbial production of vitamin B12: a review and future perspectives". Microbial Cell Factories. 16 (1): 15. doi: 10.1186/s12934-017-0631-y . PMC   5282855 . PMID   28137297.
  3. Debussche, L.; Thibaut, D.; Cameron, B.; Crouzet, J.; Blanche, F. (1993). "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans". Journal of Bacteriology. 175 (22): 7430–7440. doi:10.1128/jb.175.22.7430-7440.1993. PMC   206888 . PMID   8226690.
  4. R. Caspi (2013-09-25). "Pathway: adenosylcobalamin biosynthesis II (aerobic)". MetaCyc Metabolic Pathway Database. Retrieved 2020-04-24.
  5. Anzai, Y.; Kim, H.; Park, J. Y.; Wakabayashi, H.; Oyaizu, H. (2000). "Phylogenetic affiliation of the pseudomonads based on 16S rRNA sequence". International Journal of Systematic and Evolutionary Microbiology. 50 (4): 1563–1589. doi:10.1099/00207713-50-4-1563. PMID   10939664.