Sadiqua Noor

Amylase is an enzyme that aids in the conversion of starch to sugars. There is a detailed description of amylase enzyme example provided.

Amylase is an enzyme that catalyzes the hydrolysis (breaking of a substance by adding a water molecule) of starch into smaller carbohydrate molecules like maltose (a molecule composed of two glucose molecules). Amylases are classified as alpha, beta, or gamma depending on how they attack the bonds between starch molecules.

1. Alpha amylase
2. Beta amylase
3. γ-Amylase
4. α-glucosidase
5. CGTase
6. Gluco amylase
7. Salivary amylase
8. Pancreatic amylase
9. Fungal amylases
10. Ptyalin
11. Pullulanase
12. Amylopullulanase
13. Cyclomaltodextrinase
14. Dextran glucosidase
15. Sucrose phosphorylase
16. Debranching enzyme
17. Alternansucrase
18. Maltooligosyl trehalose synthase
19. Trehalose synthase
20. Amylosucrase
21. Amylomaltase
22. Oligo-1,6-glucosidase
23. Isoamylase
24. Glucodextranase
25. Maltogenic amylase
26. Neopullulanase

Alpha amylase

Alpha-amylase (-amylase) is an enzyme with the EC number 3.2.1.1 that breaks down alpha bonds in big, alpha-linked polysaccharides like starch and glycogen to produce shorter chains, dextrins, and maltose. It’s the most common type of amylase in humans and other mammals.

Many fungi secrete it, and it is found in seeds containing starch as a food reserve. It belongs to the glycoside hydrolase 13 family. Saliva contains the digesting enzyme alpha amylase. It breaks down starch’s -1,4 glycosidic bonds. Mastication efficiency is critical for salivary amylase to permeate the meal bolus.

Beta amylase

The enzyme beta-amylase (EC 3.2.1.2, -amylase, saccharogen amylase, glycogenase) is also known as 4-alpha-D-glucan maltohydrolase. The most essential enzyme is beta-amylase, which cleaves two bonded glucose molecules from the reducing end of the chain.

The ability of beta-amylase to create enough maltose, the most significant fermentable sugar, is critical during the first stage of brewing.

γ-Amylase

γ-Amylase is a less commonly utilised enzyme in the food business. It hydrolyzes the final (1-4)glycosidic bond to breakdown starch from the non-reducing end, giving one glucose unit. It can also hydrolyze glycosidic bonds (1-6). In comparison to other amylases, the enzyme has a lower ph optimum. A type of amylase that produces glucose by cleaving the final alpha-1,4-glycosidic connections at the nonreducing end of amylase and amylopectin. It also breaks down alpha-1-6 glycosidic bonds. In acidic conditions, -amylase is most effective (optimum pH of 3).

α-glucosidase

Alpha-glucosidase is a glucosidase that acts on α(1-4) bonds and is found in the brush edge of the small intestine. Starch and disaccharides are converted to glucose by the enzyme alpha-glucosidase.

CGTase

CGTases (cyclodextrin glycosyltransferases) are enzymes that can create cyclodextrins (σ(1->4) connected circular oligoglucosides) from starch.

Gluco amylase

Glucoamylase is a fungal enzyme with 45 carbohydrate side chains, including single mannose residues and mannose, glucose, and galactose oligosaccharide chains.

Salivary amylase

Salivary amylase may be a cleavage enzyme for glucose polymers generated by the salivary glands. It only accounts for a minor a part of total amylase excreted, which is usually produced by the pancreas.

Pancreatic amylase

Pancreatic amylase completes carbohydrate digestion, leading to glucose, a small molecule taken into the bloodstream and transported throughout the body.

Fungal amylases

Aspergillus oryzae produces a kind of alpha amylase called fungal Amylase. There are two types of it: liquid and powder.This fast-acting hydrolase works in the acidic, neutral, and mildly alkaline pH ranges.

Ptyalin

Human salivary glands generate ptyalin, a starch hydrolyzing enzyme. It’s a specific type of salivary amylase. Ptyalin, a salivary molecule, helps the tongue digest starch.

Pullulanase

Pullulanase is a type of glucanase that degrades pullulan. It is an amylolytic exoenzyme. Gram-negative bacteria of the genus Klebsiella generate it as an extracellular, cell surface-anchored lipoprotein.

Amylopullulanase

Amylopullulanases are a type of debranching enzyme that belongs to the glycoside hydrolases (GHs) family of carbohydrate-active enzymes, which is classified by sequence.

Cyclomaltodextrinase

The enzyme cyclomaltodextrinase (CDase) hydrolyzes cyclodextrin to generate linear oligosaccharides with (1,4)-linkages.

Dextran glucosidase

Streptococcus mutans Dextran Glucosidase (SMDG), an exo-type glycoside hydrolase (GH) family 13 glucosidase, hydrolyzes a -1,6-glucosidic linkage at the non-reducing ends of isomaltooligosaccharides and dextran.

Sucrose phosphorylase

Sucrose phosphorylase is a key enzyme in sucrose metabolism and the control of other metabolic intermediates.Sucrose phosphorylases are carbohydrate-active enzymes with exceptional biocatalytic potential for converting regular table sugar into compounds with desirable characteristics.

Debranching enzyme

A debranching enzyme helps the breakdown of glycogen, which serves as a glucose storage in the body, by glucosyltransferase and glucosidase activity. Debranching enzymes, in conjunction with phosphorylases, mobilise glucose stores from glycogen deposits in the muscles and liver.

Alternansucrase

Alternansucrase catalyses the transfer of an alpha-D-glucosyl residue from sucrose to the 6- and 3-positions of the terminal residue of an alpha-D-non-reducing glucan, resulting in a glucan with alternating alpha-1,6- and alpha-1,3-bonds.

Maltooligosyl trehalose synthase

Intramolecular transglycosylation of maltooligosaccharide to maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) is catalysed by this enzyme.

Trehalose synthase

Trehalose synthase (TreS) is a catalytic enzyme that catalyses the reversible conversion of maltose to trehalose. Bacteria are the principal producers of TreS. Because of the inexpensive cost of the substrate, the simplicity of the reaction, and the high conversion yield, the TreS route is appealing for the synthesis of trehalose.

Amylosucrase

Amylosucrase (EC 2.4.1.4) belongs to the glycoside hydrolases (-amylases) Family 13, but its biological purpose is to synthesise amylose-like polymers from sucrose.

Amylomaltase

Amylomaltase (AM) catalyses the transglycosylation of starch to get linear or cyclic oligosaccharides, which has biotechnological and industrial applications.

Oligo-1,6-glucosidase

The isomaltase–maltase component is in charge of breaking down isomaltose and maltose into two glucose molecules.

Isoamylase

Glycogen 6-alpha-D-glucanohydrolase is the scientific name for isoamylase . Glycogen, amylopectin, and its beta-limit dextrins undergo hydrolysis of alpha-D-glucosidic branch connections. Amylopectin is easily hydrolyzed by this enzyme.

Glucodextranase(GDase)

The enzyme glucodextranase catalyses the hydrolysis of dextran’s glucosidic bonds. N, A, B, and C are the four domains that make up the structure of GDase. Domain A has a six-barrel structure, while domain N has seventeen antiparallel strands. Both domains appear to be concerned with catalytic activity in bacterial glucoamylases (GAs).

Maltogenic amylase

Maltogenic amylase is a type of amylase that breaks down starch into maltose. It may break down starch into smaller molecules in settings where it has lots of substrates to deal with. It’s an endo-amylase, which means it functions at the end of a molecule string.

Neopullulanase

Neopullulanase (EC 3.2.1.135, pullulanase II) is a pullulan 4-D-glucanohydrolase (panose-forming) enzyme of the alpha-amylase family.Neopullulanase, a glycosyl hydrolase isolated from Bacillus stearothermophilus (bsNpl), could be used in the starch and detergent sectors.

Also Read:

• How is adenine formed
• Eukaryotic chromosome structure
• Do plant cells have mitochondria
• Types of eukaryotic chromosomes
• Are protists heterotrophs
• Ecosyetm examples
• Structure of cytosine
• Do all cells have cytoplasm
• Are algae autotrophs
• Do cytoplasm have mitochondria

Anabolism refers to a group of metabolic mechanisms that build compounds from smaller components.There is a detailed description of anabolic enzyme example provided.

Anabolic enzymes facilitate metabolic events involving the construction of bigger complex compounds from simpler ones. These anabolic reactions need a significant amount of energy. Endergonic processes are another name for them.

1. DNA polymerase.
2. ATP synthase
3. Ribulose-1,5-bisphosphate carboxylase-oxygenase,
4. Glycogen synthase.
5. Glycogen synthase kinase 3
6. Glucokinase
7. Hexokinases
8. Phosphoglucomutase
9. RNA polymerase
10. Glutamine synthetase
11. Methionine synthase
12. Asparagine synthetase
13. Aminoacyl-tRNA-synthetase
14. Glycosyltransferase
15. DNA ligase
16. Citrate synthase
17. Pseudouridine synthase
18. Fatty acid synthase
19. Cellulose synthase
20. Succinyl coenzyme A synthetase
21. Anabolic Ornithine Carbamoyltransferase

DNA polymerase

DNA polymerase is a well-known example of an anabolic enzyme. The DNA molecule is rebuilt by this enzyme. DNA polymerase assembles nucleotides to form DNA molecules.

DNA’s building units are nucleotides. It is required for DNA replication, and it usually works in pairs to produce two identical DNA strands from a single DNA molecule (template).

ATP synthase

The ATP synthase is a mitochondrial enzyme that catalyzes the synthesis of ATP from ADP and phosphate. It is driven by a flux of protons over a gradient created by electron transfer from the proton’s chemically positive to negative side.

Ribulose-1,5-bisphosphate carboxylase-oxygenase,

The enzyme ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCo) is engaged in the first major phase of carbon fixation, which is the conversion of atmospheric carbon dioxide to energy-rich compounds like glucose by plants and other photosynthetic organisms.

RubisCO is essential for the survival of life on Earth because it catalyzes the conversion of atmospheric CO(2) to organic matter.

Glycogen synthase

Glycogen synthase (UDP-glucose-glycogen glucosyltransferase) is a crucial enzyme in glycogenesis, the process of converting glucose to glycogen. Glycogen synthase (GS) is a skeletal muscle enzyme that catalyzes the conversion of uridine diphosphate-glucose to glycogen. GS activity is assumed to be rate-limiting in the disposal of glucose as muscle glycogen in conjunction with the glucose transport stage.

Glycogen synthase kinase 3

Glycogen synthase kinase 3 (GSK-3) is a serine/threonine protein kinase that allows phosphate molecules to be added to serine and threonine amino acid residues.

Glucokinase

The enzyme glucosekinase aids in the phosphorylation of glucose to glucose-6-phosphate. Humans and most other animals have glucokinase in their liver and pancreas cells. It acts as a glucose sensor in each of these organs, causing changes in metabolism or cell function in response to changes in glucose levels.

Hexokinases

Hexokinase is a phosphorylating enzyme that converts hexoses (six-carbon sugars) to hexose phosphate.Hexokinase can take an inorganic phosphate group from ATP and transfer it to a substrate.

Phosphoglucomutase

Phosphoglucomutase is an enzyme that moves a phosphate group from the 1 to the 6 position on a -D-glucose monomer in one direction or from the 6 to the 1 position in the other.

RNA polymerase

RNA polymerase (green) follows a strand of DNA to make RNA.

The enzyme RNA polymerase is responsible for transcribing a DNA sequence into an RNA sequence during the transcription process.

Glutamine synthetase

Glutamine synthetase is an enzyme that catalyses the condensation of glutamate and ammonia to create glutamine, which is an important step in nitrogen metabolism.

Methionine synthase

The enzyme aids in the digestion of amino acids, which are the building blocks of proteins. Methionine synthase, in particular, performs a chemical reaction that transforms the amino acid homocysteine to the amino acid methionine. Methionine is used by the body to create proteins and other essential chemicals.

Asparagine synthetase

Asparagine Synthetase is a cytoplasmic enzyme that catalyses the ATP-dependent amidotransferase process that produces the non-essential amino acid asparagine from aspartate and glutamine.

Aminoacyl-tRNA-synthetase

The enzyme aminoacyl-tRNA synthetase (aaRS or ARS), also known as tRNA-ligase, binds the proper amino acid to its associated tRNA. It accomplishes this by catalysing the transesterification of a cognate amino acid or its precursor to one of the cognate tRNAs that are compatible with it, resulting in an aminoacyl-tRNA. Twenty separate aminoacyl-tRNA synthetases, one for each amino acid in the genetic code, produce the 20 different forms of aa-tRNA in humans.

Glycosyltransferase

Glycosyltransferases are enzymes that initiate and lengthen glycan chains on mucins by transferring active sugar residues to the correct acceptor.

DNA ligase

DNA ligase is a type of ligase that catalyses the formation of a phosphodiester bond between DNA strands, making it easier to bind them together. In living creatures, it helps to repair single-strand breaks in duplex DNA, although some forms may also help to repair double-strand breaks.

Citrate synthase

Citrate synthase is a pace-making enzyme in the first step of the citric acid cycle that is found in practically all living cells (or Krebs cycle).

Citrate synthase is found in the mitochondrial matrix of eukaryotic cells, however it is encoded by nuclear DNA rather than mitochondrial DNA. It is produced in the cytoplasm and subsequently transferred to the mitochondrial matrix.

Pseudouridine synthase

Pseudouridine synthases are the enzymes responsible for the majority of biological RNA posttranslational modifications. These enzymes appear to use both sequence and structural information to achieve site specificity in the isomerization of uridine residues that are already part of an RNA chain.

Fatty acid synthase

Fatty acid synthase, which catalyses the formation of long-chain fatty acids from acetyl-CoA and malonyl-CoAAs, is the rate-limiting enzyme in the fatty acid synthesis pathway.

Cellulose synthase

Cellulose synthase is a huge protein complex that builds cellulose strands and fibrils in the plant plasma membrane. The complex is a huge rosette with about 6-fold symmetry, made up of six trimers containing three slightly different enzyme types.To make cellulose, cellulose synthase employs an active form of glucose linked to a UDP nucleotide.

Succinyl coenzyme A synthetase

Succinyl coenzyme A synthetase catalyses the reversible conversion of succinyl-CoA to succinate. The enzyme aids in the creation of a nucleoside triphosphate molecule (GTP or ATP) from an inorganic phosphate molecule and a nucleoside diphosphate molecule from this process (either GDP or ADP). It is found within the mitochondrial matrix of a cell and serves as one of the catalysts in the citric acid cycle, which is a critical step in cellular metabolism.

Anabolic Ornithine Carbamoyltransferase

Ornithine transcarbamylase (OTC) (also known as ornithine carbamoyltransferase) is an enzyme that catalyses the conversion of carbamoyl phosphate (CP) to citrulline (Cit) and phosphate (Pi).In prokaryotes, anabolic OTC aids the sixth step in the production of the amino acid arginine. [5] Mammalian OTC, on the other hand, is critical to the urea cycle, which captures poisonous ammonia and converts it to urea, a less toxic nitrogen source, for excretion.

Also Read:

• Plant cell structure
• Do animal cells have chloroplasts
• Are globular proteins soluble
• Example of eukaryotic cell
• Centipede characteristics
• Arachnid characteristics
• Why chromosomes are in pairs
• Do protists move
• Are algae multicellular
• Digestive enzymes in lysosomes

Allosteric enzymes change their conformational ensemble when an effector binds to them, resulting in a change in binding affinity at a new ligand binding site. There is a detailed description of allosteric enzyme examples provided.

Allosteric enzymes are a class of biocatalysts that share many of the same properties as enzymes but don’t follow the Michaelis-Menten kinetic model. Their dynamics, on the other hand, are sigmoid.

1. Phosphofructokinase (PFK)
2. Isocitrate dehydrogenase (IDH)
3. Aspartate transcarbamoylase (ATCase)
4. Glycogen phosphorylase
5. AGPase
6. Acetyl-CoA carboxylase
7. Pyruvate Kinase
8. Ribonucleotide reductase
9. glutamine synthetase
10. glyceraldehyde-3 phosphate dehydrogenase
11. Hexokinase
12. glucokinase
13. fructose 1,6-bisphosphatase
14. pyruvate carboxylase
15. Citrate synthase
16.  Succinate dehydrogenase 
17. α-Ketoglutarate dehydrogenase
18. carbonic anhydrase
19. xanthine oxidase
20. choline esterase
21. nucleoside triphosphates
22. methionine synthase
23. carnitine palmitoyltransferase 1
24. fatty acid synthase,
25. Fatty acid amide hydrolase

Phosphofructokinase (PFK)

One of the most significant glycolysis regulating enzymes (EC 2.7.1.11) is phosphofructokinase-1 (PFK-1).

It’s an allosteric enzyme with four subunits that’s regulated by a variety of activators and inhibitors.

Isocitrate dehydrogenase (IDH)

The key control point of the citric acid cycle is catalysed by isocitrate dehydrogenase (IDH). Human IDH is made up of two heterodimers, one of which acts as a catalytic component and the other as a regulatory subunit.

Aspartate transcarbamoylase (ATCase)

The enzyme aspartate transcarbamoylase (ATCase) aids in the flow limit and committed step of pyrimidine biosynthesis.

ATCase is made up of a large catalytic and a smaller regulatory subunit.

Glycogen phosphorylase

In the metabolism of glucose, the enzyme glycogen phosphorylase is crucial. It is responsible for the release of glucose monomers from the glycogen polymer stored in the liver (glycogenolysis). In a process that does not require ATP, GP breaks down glucose to form glucose-1-phosphate (G-1-P).

AGPase

In amyloplasts, AGPase catalyzes the limiting reaction by converting glucose 1-phosphate (Glc-1-P) and ATP to ADP-Glc and inorganic pyrophosphate (PPi) as the first enzyme in the starch production pathway. 3-phosphoglyceric acid (3-PGA) stimulates the enzyme’s catalytic activity, while inorganic phosphate inhibits it (Pi).

Acetyl-CoA carboxylase

Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, a key intermediate substrate in fatty acid metabolic control.

Pyruvate Kinase

The enzyme pyruvate kinase is involved in the final phase of glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate to adenosine diphosphate, resulting in one pyruvate molecule and one ATP molecule.

Ribonucleotide reductase

E. coli’s ribonucleotide reductase is an allosteric enzyme whose activity and specificity are controlled by a complex system of nucleoside triphosphates. Such effectors were found to alter both the Michaelis constant and Vmax values for particular substrates; when multiple effectors were used, the ensuing patterns of activation and inhibition revealed that catalytic activity regulation was extremely intricate.

Glutamine synthetase

In E. coli, glutamine synthetase activity is inhibited by seven different glutamine metabolic end products, including tryptophan, histidine, carbamyl-phosphate, CTP, AMP, glucose-6-phosphate, and NAD+, as well as serine, alanine, and glycine..

Glyceraldehyde-3 phosphate dehydrogenase

Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) is a 37-kDa enzyme that catalyzes the sixth step of glycolysis, allowing glucose to be broken down for energy and carbon molecules. Ferredoxin-NADP reductase regulates glyceraldehyde-3-phosphate dehydrogenase.

Hexokinase

When glucose binds to hexokinase, it causes an induced fit conformational change. Physiological amounts of glucose-6-phosphate the product allosterically restrict this conformational change, which precludes ATP hydrolysis.

Glucokinase

Glucokinase (GK) is a monomeric allosteric enzyme that is essential for maintaining blood glucose homeostasis. GK is regulated both directly and indirectly by GK regulatory protein (GKRP) allosteric effectors.

Fructose 1,6-bisphosphatase

A number of tiny molecules, including AMP and fructose-2,6-phosphate, which are negative regulators, and ATP, which is a positive regulator, allosterically regulate the enzyme.

Pyruvate carboxylase

PC is a biotin-containing enzyme that catalyzes the synthesis of oxaloacetate from pyruvate in the presence of an allosteric activator, acetyl CoA. The allosteric activator acetyl-CoA controls the activity of the biotin-dependent enzyme pyruvate carboxylase in numerous species.

Citrate synthase

Escherichia coli’s citrate synthase (CS) is an allosteric hexameric enzyme that is inhibited by NADH. Because the end product of the citric acid cycle, ATP, inhibits citrate synthase, ADP (adenosine diphosphate) acts as an allosteric activator of the enzyme because ATP is produced from ADP. As a result, when the cell has a lot of ATP, the rate of the cycle slows down.

 Succinate dehydrogenase 

Succinate dehydrogenase (SDH) or succinate-coenzyme Q reductase (SQR) or respiratory complex II is an enzyme complex found in the inner mitochondrial membrane of eukaryotic and many bacterial cells. It’s the only enzyme in the citric acid cycle and the electron transport chain.

α-Ketoglutarate dehydrogenase

The citric acid cycle’s major regulatory point is ketoglutarate dehydrogenase. Its products, succinyl CoA and NADH, block it. A cell with a strong energy charge will also be inhibitive. Allosteric activators of the enzyme include ADP and calcium ions.

Carbonic anhydrase

Carbonic anhydrases are a family of enzymes that can change intracellular and extracellular pH, influencing proliferation, migration, and invasion, as well as contributing to pH gradient inversion.

Xanthine oxidase

Xanthine oxidase is a kind of xanthine oxidoreductase, which produces reactive oxygen species. These enzymes catalyze the conversion of hypoxanthine to xanthine, and they can also convert xanthine to uric acid. In several animals, including humans, these enzymes play a key role in purine catabolism.

Choline esterase

Choline esterase is a member of the esterase family that lyses choline-based esters, some of which are neurotransmitters. [1] As a result, one of two enzymes catalyzes the hydrolysis of these cholinergic neurotransmitters, such as converting acetylcholine to choline and acetic acid.

Nucleoside triphosphates

A nucleoside triphosphate is a molecule with a nitrogenous base attached to a 5-carbon sugar (either ribose or deoxyribose) and three phosphate groups attached to the sugar. A nucleotide is an example of a molecule. They are the molecular progenitors of DNA and RNA, which are nucleotide chains formed during the replication and transcription of DNA. Nucleoside triphosphates are also engaged in signaling pathways and serve as a source of energy for cellular activities.

Methionine synthase

The final step in the regeneration of methionine from homocysteine is catalyzed by methionine synthase. The transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine, yielding tetrahydrofolate and methionine, is carried out by both cobalamin-dependent and cobalamin-independent versions of the enzyme.

Carnitine palmitoyltransferase 1

Carnitine palmitoyltransferase 1 is a protein that facilitates fatty acid transport from the cytosol to the mitochondrial matrix.

Fatty acid synthase

The multi-enzyme protein fatty acid synthase catalyzes the production of fatty acids. It’s not a single enzyme, but rather an entire enzymatic system made up of two identical 272 kDa multifunctional polypeptides that pass substrates from one functional domain to the next.

Fatty acid amide hydrolase

The fatty acid amide hydrolase (FAAH) enzyme is a serine hydrolase that degrades the fatty acid amide family of signaling lipids, which includes anandamide, an endocannabinoid. FAAH’s role in pain and nervous system problems has made it an appealing molecular imaging target.

Also Read:

• Genetic diversity types
• Saprophytic bacteria examples
• Tundra biome examples
• Pathogenic bacteria examples
• Protists cell walls and plant cell walls
• Water movement through cell wall
• Does cytoplasm contains all the organelles
• Monogenea characteristics
• Biome examples
• Is fatty acid polar

These are microorganisms that convert nitrates in the soil to nitrogen gas in the atmosphere .There is a detailed description of denitrifying bacteria examples provided.

The conversion of nitrate and nitrite to nitrous oxide and dinitrogen gas is known as denitrification . Many Bacteria and Archaea have the ability to denitrify , and a variety of organic and inorganic substances can be employed as electron donors.

1. Thiobacillus denitrificans
2. Micrococcus denitrificans
3. Pseudomonas denitrificans
4. Alcaligenes faecalis
5. Streptomycetes
6. Paracoccus denitrificans
7. Thiosphaera pantotropha
8. Prolixibacter denitrificans
9. Zobellella denitrificans
10. Steroidobacter denitrificans
11. Ferrovibrio denitrificans
12. Halobacterium denitrificans
13. Thiomicrospira denitrificans
14. Pseudomonas aeruginosa
15. Noviherbaspirillum denitrificans
16. Rhodanobacter denitrificans
17. Blastobacter denitrificans
18. Bradyrhizobium denitrificans
19. Kingella denitrificans
20. Jonesia denitrificans
21. Achromobacter denitrificans

Thiobacillus denitrificans

1. Thiobacillus denitrificansis a facultative anaerobe bacterium that is obligately chemolithoautotrophic. It is best known for its capacity to link inorganic sulphur compound oxidation to denitrification. Image credited by Wikipedia It’s a natural agent for nitrate-polluted groundwater intrisic bioremediation.

It’s also been used to remove nitrates in designed water treatment systems. Its ability to perform nitrate-dependent Fe(II) oxidation under anaerobic conditions could have an impact on metal and radionuclide transport in the subsurface, as ferric iron-containing minerals, particularly iron(III) oxides, are well-known for their ability to adsorb heavy metals and radionuclides like uranium.

Micrococcus denitrificans

Micrococcus denitrificans can do both assimilatory and dissimilatory nitrate reduction, but only the assimilatory mechanism works in both aerobic and anaerobic environments. Aeration has at least three effects on a growing culture’s dissimilatory activity (the conversion of nitrate to nitrogen): 1)It prevents the adaptive development of the system; 2) If the system is already existing, it partially represses any further synthesis; and ,3) It totally blocks the action of the preformed system.

These effects of oxygen are mirrored to some extent in the control it exerts on the content and activity of nitrate reductase (the enzyme responsible for the early reduction of nitrate to nitrite) in the organism throughout growth. The transformation of nitrate into cell nitrogen is slightly inhibited by ammonium ions, however the activity of nitrate reductase in crude extracts of this organism is undetectable.

Pseudomonas denitrificans

Pseudomonas denitrificans is a gram-negative, aerobic, heterotrophic bacteria that participates in the nitrogen cycle’s denitrification process, which converts nitrate to nitrogen gas (N2). It grows best at a temperature of 25°C. It’s important in medicine and the environment, and it’s used in industry to make vitamin B12.

It could also be used for nitrate toxicity or wastewater treatment. Commercial chemicals such as 3-hydroxypropionic acid are made with this bacteria. Its denitrification powers aid wastewater management in several ways.

Alcaligenes faecalis

Alcaligenes faecalisis a Gram-negative heterotrophic bacterium found in soil.The bacteria A. faecalis had the ability to denitrify because it had a copper-containing nitrite reductase that catalysed the conversion of nitrite (NO2) to nitric oxide (NO).

Streptomycetes

Streptomycetes are a type of gram-positive filamentous bacteria that can be found in soil all around the world.

Paracoccus denitrificans

Paracoccus denitrificans is a denitrifying (nitrate-reducing) bacterium. It is a gram-negative, non-motile, coccus bacteria. During the stationary phase, it changes shape from rod to spherical.

It possesses a double membrane and a cell wall, like all gram-negative bacteria.

Thiosphaera pantotropha

Thiosphaera pantotropha is a sulphur bacterium that can do both heterotrophic nitrification and aerobic denitrification at the same time. It is a facultative anaerobe that can thrive on a variety of substrates, both mixotrophically and heterotrophically.Regardless of ambient dissolved oxygen concentration, it can oxidise reduced sulphur compounds, nitrify ammonia heterotrophically to nitrite, and convert nitrate or nitrite to nitrogen gas.

Prolixibacter denitrificans

Prolixibacter denitrificans sp. nov. is a nitrate-reducing bacterium isolated from crude oil that is iron-corroding and facultatively aerobic.

Zobellella denitrificans

Zobellella denitrificans belongs to the genus Zobellella and is a Gram-negative, facultatively anaerobic, heterotrophic, and denitrifying bacterium.

Steroidobacter denitrificans

Steroidobacter denitrificans belongs to the genus Steroidobacter and is a Gram-negative, motile bacterium, Chemo-organotrophs; non-fermentative, respiratory metabolism. Demonstrate nitrate reduction to dinitrogen monoxide and then to dinitrogen without accumulating nitrite in the process.

Ferrovibrio denitrificans.

Ferrovibrio denitrificans are gram-negative, flagellated, and rod-shaped cells are present. Colonies are white, convex, and round.

Halobacterium denitrificans

Halobacterium denitrificans was one of several carbohydrate-consuming, denitrifying, and very halophilic bacteria identified by anaerobic enrichment in nitrate.

Thiomicrospira denitrificans

Thiomicrospira is a genus of sulfur-oxidizing bacteria that was once thought to encompass all marine spiral-shaped bacteria. Thiomicrospira members are distributed across the gamma and epsilon subgroups of the Proteobacteria, according to subsequent analysis of 16S rDNA sequences. To present, all Thiomicrospira species have been identified as obligate chemolithoautotrophic bacteria that rely on sulphide, thiosulfate, and elemental sulphur as electron donors and CO2 as a carbon source.

The oxidation of reduced sulphur compounds provides energy to Thiomicrospira denitrificans. Denitrification occurs as a result of oxidation. Reduced sulphur H2S, S2O32-, and S° are used as electron donors, whereas O2 and NO3- are used as electron acceptors. Microbial activities link the geochemical cycle of redox substrates to the carbon, nitrogen, and sulphur cycles by connecting the oxidation and reduction of inorganic molecules to the generation of biomass.

Pseudomonas aeruginosa

Pseudomonas aeruginosa is a Gram-negative bacterium that is found in almost every habitat. It’s an opportunistic human pathogen that can cause a variety of life-threatening acute and chronic infections, especially in people who have weakened immune systems.

Noviherbaspirillum denitrificans

Noviherbaspirillum denitrificans is a Gram-negative, facultative anaerobe Proteobacterium isolated from rice paddy soil under denitrification-inducing circumstances.

Rhodanobacter denitrificans

Rhodanobacter denitrificans is a rod-shaped bacterium that is yellow-pigmented, gram-negative, non-sporulating, motile, slow-growing, and facultatively anaerobic. The bacteria is capable of full denitrification.This procedure is only capable of two Rhodanobacter species, one of which being Rhodanobacter denitrificans. In the absence of oxygen, growth is powered by the utilisation of electron acceptors such as nitrate, nitrite, and nitrous oxide.

Blastobacter denitrificans

Blastobacter spp. are freshwater bacteria that attach to a common base to form rosette structures. B. denitrificans is a member of the Proteobacteria’s -subdivision, according to comparisons of ribosomal 16S rRNA gene and internally transcribed spacer region sequences.

Bradyrhizobium denitrificans

Bradyrhizobium denitrificans is a Bradyrhizobium bacterium that was discovered in surface lake water in Germany.Bradyrhizobium is a genus of Gram-negative soil bacteria that fix nitrogen in large numbers. The nitrogen cycle is incomplete without nitrogen fixation. Plants must rely on nitrogen molecules such as nitrates instead of atmospheric nitrogen (N2).

Kingella denitrificans

Kingella are gram-negative coccobacilli that are found in pairs or short chains and belong to the Neisseriaceae family. The creatures develop slowly and are picky eaters. Kingella is an uncommon cause of human sickness that is recovered from the human respiratory tract.

Jonesia denitrificans

Jonesia denitrificans is a mesophilic anaerobe Actinobacterium that forms an aerial mycelium and was discovered in boiled ox blood. J. denitrificans has a typical coryneform morphology and can produce irregular nonsporulating rods with branched and club-like structures. Older cultures include coccoid cells.

Achromobacter denitrificans

The Gram-negative, oxidase- and catalase-positive, strictly aerobic, ubiquitous, motile bacterium Achromobacter denitrificans was identified from soil and has the potential to cause human illnesses. Achromobacter agile was its previous name.

Also Read:

• Gamete
• Fungi cell wall and archaea cell wall
• Do eubacteria have a cell wall
• Atp synthesis in aerobic respiration
• Does glycolysis occur in the cytoplasm
• Silverfish characteristics
• How are mitochondria similar to chloroplasts
• Pome fruit examples
• Lysosomes and ribosomes
• Parenchyma cells in plants