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A debranching enzyme is a molecule that helps facilitate the breakdown of glycogen, which serves as a store of glucose in the body, through glucosyltransferase and glucosidase activity. Together with phosphorylases, debranching enzymes mobilize glucose reserves from glycogen deposits in the muscles and liver. This constitutes a major source of energy reserves in most organisms. Glycogen breakdown is highly regulated in the body, especially in the liver, by various hormones including insulin and glucagon, to maintain a homeostatic balance of blood-glucose levels. When glycogen breakdown is compromised by mutations in the glycogen debranching enzyme, metabolic diseases such as Glycogen storage disease type III can result.
Paenarthrobacter ureafaciens KI72, popularly known as nylon-eating bacteria, is a strain of Paenarthrobacter ureafaciens that can digest certain by-products of nylon 6 manufacture. It uses a set of enzymes to digest nylon, popularly known as nylonase.
Pectinesterase (EC 3.1.1.11; systematic name pectin pectylhydrolase) is a ubiquitous cell-wall-associated enzyme that presents several isoforms that facilitate plant cell wall modification and subsequent breakdown. It catalyzes the following reaction:
Alteromonas is a genus of Pseudomonadota found in sea water, either in the open ocean or in the coast. It is Gram-negative. Its cells are curved rods with a single polar flagellum.
Atrazine Chlorohydrolase (AtzA) is an enzyme (E.C.3.8.1.8), which catalyzes the conversion of atrazine to hydroxyatrazine. Bacterial degradation determines the environmental impact and efficacy of an herbicide or pesticide. Initially, most pesticides are highly effective and show minimal bacterial degradation; however, bacteria can rapidly evolve and gain the ability to metabolize potential nutrients in the environment. Despite a remarkable structural similarity, degradation of atrazine by bacteria capable of melamine degradation was rare; however, since its introduction as a pesticide in the United States, bacteria capable of atrazine degradation have evolved. Currently, Pseudomonas sp. strain ADP seems to be the optimal bacterial strain for atrazine degradations, which appears to be the sole nitrogen source for the bacteria.
Fibrobacter succinogenes is a cellulolytic bacterium species in the genus Fibrobacter. It is present in the rumen of cattle. F. succinogenes is a gram negative, rod-shaped, obligate anaerobe that is a major contributor to cellulose digestion. Since its discovery in the 1950s, it has been studied for its role in herbivore digestion and cellulose fermentation, which can be utilized in biofuel production.
In enzymology, an alanine racemase is an enzyme that catalyzes the chemical reaction
Aryldialkylphosphatase is a metalloenzyme that hydrolyzes the triester linkage found in organophosphate insecticides:
In enzymology, a riboflavin kinase is an enzyme that catalyzes the chemical reaction
NUDIX hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x, hence their name. The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the NUDIX superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.
Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds. Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. Many types of glucanases share similar amino acid sequences but vastly different substrates. Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active.
Alteromonas macleodii is a species of widespread marine bacterium found in surface waters across temperate and tropical regions. First discovered in a survey of aerobic bacteria in 1972, A. macleodii has since been placed within the phylum Pseudomonadota and is recognised as a prominent component of surface waters between 0 and 50 metres. Alteromonas macleodii has a single circular DNA chromosome of 4.6 million base pairs. Variable regions in the genome of A. macleodii confer functional diversity to closely related strains and facilitate different lifestyles and strategies. Certain A. macleodii strains are currently being explored for their industrial uses, including in cosmetics, bioethanol production and rare earth mining.
Organophosphorus acid anhydrolase (OPAA) is an enzyme that been shown to be particularly effective in detoxifying organophosphorus-containing compounds, such as deadly nerve gas used in chemical warfare. The enzyme is found in a diverse range of organisms, including protozoa, squid and clams, mammals, and soil bacteria. A highly active form of the enzyme is typically isolated from the marine bacteria Alteromonas undina for laboratory study. This form is both halophilic and thermophilic, making it particularly useful for detoxification applications. A slightly less active variant of OPAA has also been isolated in mung beans and slime mold duckweed.
κ-Carrageenase is an enzyme with systematic name κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining). It catalyses the endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans
Iota-carrageenase is an enzyme with systematic name iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting). This enzyme catalyses the following chemical reaction
Beta porphyranase is an enzyme responsible for the degradation of porphyran, which composes the cell wall of red algae. So far only five β-porphyranases have been identified: PorA and PorB are found in the marine bacteria Zobellia galactinovirans. A wild-type porphyranase activity has been found in Pseudoalteromonas atlantica. BpGH16B and BpGH86A have been found in the human gut bacterium, Bacteroides plebeius, of Japanese individuals.
Alcanivorax pacificus is a pyrene-degrading marine gammaproteobacterium. It is of the genus Alcanivorax, a group of marine bacteria known for degrading hydrocarbons. When originally proposed, the genus Alcanivorax comprised six distinguishable species. However, A. pacificus, a seventh strain, was isolated from deep sea sediments in the West Pacific Ocean by Shanghai Majorbio Bio-pharm Technology Co., Ltd. in 2011. A. pacificus’s ability to degrade hydrocarbons can be employed for cleaning up oil-contaminated oceans through bioremediation. The genomic differences present in this strain of Alcanivorax that distinguish it from the original consortium are important to understand to better utilize this bacteria for bioremediation.
Oleispira antarctica is a hydrocarbonoclastic marine bacterium, the type species in its genus. It is psychrophilic, aerobic and Gram-negative, with polar flagellum. Its genome has been sequenced and from this information, it has been recognized as a potentially important organism capable of oil degradation in the deep sea.
Polaribacter is a genus in the family Flavobacteriaceae. They are gram-negative, aerobic bacteria that can be heterotrophic, psychrophilic or mesophilic. Most species are non-motile and species range from ovoid to rod-shaped. Polaribacter forms yellow- to orange-pigmented colonies. They have been mostly adapted to cool marine ecosystems, and their optimal growth range is at a temperature between 10 and 32 °C and at a pH of 7.0 to 8.0. They are oxidase and catalase-positive and are able to grow using carbohydrates, amino acids, and organic acids.
D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally-occurring amino acids, this carbon has the L-configuration. D-Amino acids are occasionally found in nature as residues in proteins. They are formed from ribosomally-derived D-amino acid residues.
References
- 1 2 3 4 5 Ohta Y, Hatada Y (October 2006). "A novel enzyme, lambda-carrageenase, isolated from a deep-sea bacterium". J. Biochem. 140 (4): 475–81. doi:10.1093/jb/mvj180. PMID 16926183.
- 1 2 3 4 Guibet M, Colin S, Barbeyron T, et al. (May 2007). "Degradation of lambda-carrageenan by Pseudoalteromonas carrageenovora lambda-carrageenase: a new family of glycoside hydrolases unrelated to kappa- and iota-carrageenases". Biochem. J. 404 (1): 105–14. doi:10.1042/BJ20061359. PMC 1868830 . PMID 17269933.
- ↑ "LGC Standards: Certified reference materials".
