Methylacidiphilum infernorum

Last updated

Methylacidiphilum infernorum
Scientific classification
Domain:
Phylum:
Class:
Unclassified
Order:
Family:
Genus:
Species:
M. infernorum
Binomial name
Methylacidiphilum infernorum
Hou et al. 2008
Type strain
Isolate V4
Synonyms

Methylokorus infernorumDunfield et al. 2007
Strain V4Dunfield et al. 2007
Candidatus Methylacidiphilum infernorumHou et al.

Contents

Methylacidiphilum infernorum is an extremely acidophilic methanotrophic aerobic bacteria first isolated and described in 2007 growing on soil and sediment on Hell's Gate, New Zealand. [1] [2] [3] Similar organisms have also been isolated from geothermal sites on Italy and Russia.

A polyextremophile, these non-motile rods grows optimally at pH between 2.0 and 2.5 and temperature of 60 °C. It is a methanotrophic obligated bacteria that grows at 25% (v/v) of methane in air. It is also very dependent on carbon dioxide concentrations to grow, optimally at 8% (v/v) CO2 in air. [1]

Due to its classification in the phylum Verrucomicrobiota and its extreme acidophilic phenotype M. infernorum is unique between all known methanotrophs. [1]

Biology

Genome

It has a single circular chromosome of 2,287,145 base pairs. Under genome analysis it was found that M. infernorum may use a novel methylotrophic pathway because it encodes methane monooxygenase enzymes but lacks known genetic modules for methanol and formaldehyde oxidation. [1] [4]

All the enzymes required for the Calvin Benson Bassham cycle were identify by genetic analysis. [5]

Metabolism

It has been predicted that M. infernorum possess most of the key metabolic pathways for the biosynthesis of all amino acids, nucleotides and cofactors, with the sole exception of the cobalamin cofactor. [5]

Genetic studies have shown that the enzymes it uses in several metabolic pathways differs to the ones used by other methylotrophs like for example in the biosynthesis of aromatic amino acids, lipoic acid biosynthesis, urea cycle and in the number and diversity of transporters encoded. [5]

The bacteria is able to counteract extreme acidic environments thanks to the presence of various enzymes like glutamate decarboxylase, glutamate/γ-aminobutyrate antiporter, arginine decarboxylase and an arginine/agmatine antiporter. [5]

Related Research Articles

α-Ketoglutaric acid Chemical compound

α-Ketoglutaric acid is a keto acid.

<span class="mw-page-title-main">Methionine</span> Sulfur-containing amino acid

Methionine is an essential amino acid in humans.

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

Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl.

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

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

Pterin is a heterocyclic compound composed of a pteridine ring system, with a "keto group" and an amino group on positions 4 and 2 respectively. It is structurally related to the parent bicyclic heterocycle called pteridine. Pterins, as a group, are compounds related to pterin with additional substituents. Pterin itself is of no biological significance.

Methanotrophs are prokaryotes that metabolize methane as their source of carbon and chemical energy. They are bacteria or archaea, can grow aerobically or anaerobically, and require single-carbon compounds to survive.

Methylotrophs are a diverse group of microorganisms that can use reduced one-carbon compounds, such as methanol or methane, as the carbon source for their growth; and multi-carbon compounds that contain no carbon-carbon bonds, such as dimethyl ether and dimethylamine. This group of microorganisms also includes those capable of assimilating reduced one-carbon compounds by way of carbon dioxide using the ribulose bisphosphate pathway. These organisms should not be confused with methanogens which on the contrary produce methane as a by-product from various one-carbon compounds such as carbon dioxide. Some methylotrophs can degrade the greenhouse gas methane, and in this case they are called methanotrophs. The abundance, purity, and low price of methanol compared to commonly used sugars make methylotrophs competent organisms for production of amino acids, vitamins, recombinant proteins, single-cell proteins, co-enzymes and cytochromes.

Shikimic acid, more commonly known as its anionic form shikimate, is a cyclohexene, a cyclitol and a cyclohexanecarboxylic acid. It is an important biochemical metabolite in plants and microorganisms. Its name comes from the Japanese flower shikimi, from which it was first isolated in 1885 by Johan Fredrik Eykman. The elucidation of its structure was made nearly 50 years later.

<i>N</i>-Acetylglutamate synthase Class of enzymes

N-Acetylglutamate synthase (NAGS) is an enzyme that catalyses the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA.

<span class="mw-page-title-main">Amino acid synthesis</span> The set of biochemical processes by which amino acids are produced

Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).

Methylobacillus flagellatus is a species of aerobic bacteria.

In enzymology, an amino-acid racemase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Diaminopimelate epimerase</span>

In enzymology, a diaminopimelate epimerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Arginine decarboxylase</span>

The enzyme Acid-Induced Arginine Decarboxylase (AdiA), also commonly referred to as arginine decarboxylase, catalyzes the conversion of L-arginine into agmatine and carbon dioxide. The process consumes a proton in the decarboxylation and employs a pyridoxal-5'-phosphate (PLP) cofactor, similar to other enzymes involved in amino acid metabolism, such as ornithine decarboxylase and glutamine decarboxylase. It is found in bacteria and virus, though most research has so far focused on forms of the enzyme in bacteria. During the AdiA catalyzed decarboxylation of arginine, the necessary proton is consumed from the cell cytoplasm which helps to prevent the over-accumulation of protons inside the cell and serves to increase the intracellular pH. Arginine decarboxylase is part of an enzymatic system in Escherichia coli, Salmonella Typhimurium, and methane-producing bacteria Methanococcus jannaschii that makes these organisms acid resistant and allows them to survive under highly acidic medium.

<span class="mw-page-title-main">Diaminopimelate decarboxylase</span>

The enzyme diaminopimelate decarboxylase (EC 4.1.1.20) catalyzes the cleavage of carbon-carbon bonds in meso 2,6 diaminoheptanedioate to produce CO2 and L-lysine, the essential amino acid. It employs the cofactor pyridoxal phosphate, also known as PLP, which participates in numerous enzymatic transamination, decarboxylation and deamination reactions.

In enzymology, an aromatic-amino-acid transaminase is an enzyme that catalyzes the chemical reaction

In enzymology, a D-amino-acid transaminase is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">Cofactor engineering</span> Modification of use and function of cofactors in an organism’s metabolic pathways

Cofactor engineering, a subset of metabolic engineering, is defined as the manipulation of the use of cofactors in an organism’s metabolic pathways. In cofactor engineering, the concentrations of cofactors are changed in order to maximize or minimize metabolic fluxes. This type of engineering can be used to optimize the production of a metabolite product or to increase the efficiency of a metabolic network. The use of engineering single celled organisms to create lucrative chemicals from cheap raw materials is growing, and cofactor engineering can play a crucial role in maximizing production. The field has gained more popularity in the past decade and has several practical applications in chemical manufacturing, bioengineering and pharmaceutical industries.

Methylacidiphilum fumariolicum is an autotrophic bacterium first described in 2007 growing on volcanic pools near Naples, Italy. It grows in mud at temperatures between 50 °C and 60 °C and an acidic pH of 2–5. It is able to oxidize methane gas. It uses ammonium, nitrate or atmospheric nitrogen as a nitrogen source and fixes carbon dioxide.

References

  1. 1 2 3 4 Peter D, et al. (2007). "Methane oxidation by an extremely acidophilic bacterium of the phylum Verrucomicrobia". Nature. 450 (7171): 879–882. Bibcode:2007Natur.450..879D. doi:10.1038/nature06411. PMID   18004300. S2CID   4305258.
  2. Noel R. Krieg; Wolfgang Ludwig; William Whitman; Brian P. Hedlund; Bruce J. Paster; James T. Staley; Naomi Ward; Daniel Brown, eds. (2011). Bergey's Manual of Systematic Bacteriology: Volume 4: The Bacteroidetes, Spirochaetes, Tenericutes (Mollicutes), Acidobacteria, Fibrobacteres, Fusobacteria, Dictyoglomi, Gemmatimonadetes, Lentisphaerae, Verrucomicrobia, Chlamydiae, and Planctomycetes. Springer Science & Business Media. pp. 795–6. ISBN   978-0-387-68572-4.
  3. Malgorzata Pawlowska (22 April 2014). Mitigation of Landfill Gas Emissions. CRC Press. p. 64. ISBN   978-0-415-63077-1.
  4. Hanson R, Hanson T. (1996). "Methanotrophic bacteria". Microbiol. Rev. 60 (2): 439–471. doi:10.1128/MMBR.60.2.439-471.1996. PMC   239451 . PMID   8801441.
  5. 1 2 3 4 Hou S, et al. (2008). "Complete genome sequence of the extremely acidophilic methanotroph isolate V4, Methylacidiphilum infernorum, a representative of the bacterial phylum Verrucomicrobia". Biol. Direct. 3 (26): 26. doi: 10.1186/1745-6150-3-26 . PMC   2474590 . PMID   18593465.