Methylphosphonate synthase

Last updated
Methylphosphonate synthase
Identifiers
EC no. 1.13.11.73
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Methylphosphonate synthase (EC 1.13.11.73, mpnS (gene)) is an enzyme with systematic name 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (methylphosphonate forming). [1] This enzyme catalyses the following chemical reaction

2-hydroxyethylphosphonate + O2 methylphosphonate + HCO3−

Methylphosphonate synthase is isolated from the marine archaeon Nitrosopumilus maritimus .

Related Research Articles

<span class="mw-page-title-main">Aerobic organism</span> Organism that thrives in an oxygenated environment

An aerobic organism or aerobe is an organism that can survive and grow in an oxygenated environment. The ability to exhibit aerobic respiration may yield benefits to the aerobic organism, as aerobic respiration yields more energy than anaerobic respiration. Energy production of the cell involves the synthesis of ATP by an enzyme called ATP synthase. In aerobic respiration, ATP synthase is coupled with an electron transport chain in which oxygen acts as a terminal electron acceptor. In July 2020, marine biologists reported that aerobic microorganisms (mainly), in "quasi-suspended animation", were found in organically poor sediments, up to 101.5 million years old, 250 feet below the seafloor in the South Pacific Gyre (SPG), and could be the longest-living life forms ever found.

<span class="mw-page-title-main">Nitric oxide synthase</span> Enzyme catalysing the formation of the gasotransmitter NO(nitric oxide)

Nitric oxide synthases (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS and nNOS. The inducible isoform, iNOS, involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free radical with an unpaired electron. It is the proximate cause of septic shock and may function in autoimmune disease.

In enzymology, a secologanin synthase (EC 1.14.19.62, was wrongly classified as EC 1.3.3.9 in the past) is an enzyme that catalyzes the chemical reaction

In enzymology, a columbamine oxidase (EC 1.21.3.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a berbamunine synthase (EC 1.14.19.66, Formerly EC 1.1.3.34 and EC 1.14.21.3) is an enzyme that catalyzes the chemical reaction

In enzymology, a deacetoxycephalosporin-C synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a leucocyanidin oxygenase (EC 1.14.11.19) is an enzyme that catalyzes the chemical reaction

In enzymology, a licodione synthase (EC 1.14.13.87) is an enzyme that catalyzes the chemical reaction

Carlactone synthase (EC 1.13.11.69, CCD8 (gene), MAX4 (gene), NCED8 (gene)) is an enzyme with systematic name 9-cis-10'-apo-beta-carotenal:O2 oxidoreductase (14,15-cleaving, carlactone-forming). This enzyme catalyses the following chemical reaction

2-hydroxyethylphosphonate dioxygenase (EC 1.13.11.72, HEPD, phpD (gene)) is an enzyme with systematic name 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming). This enzyme catalyses the following chemical reaction

2-hydroxyethylphosphonate:O2 1,2-oxidoreductase may refer to:

Clavaminate synthase (EC 1.14.11.21, clavaminate synthase 2, clavaminic acid synthase) is an enzyme with systematic name deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating). This enzyme catalyses the following chemical reaction

Angelicin synthase (EC 1.14.13.115, CYP71AJ4 (gene)) is an enzyme with systematic name (+)-columbianetin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction:

Nitric-oxide synthase (NAD(P)H-dependent) (EC 1.14.14.47, nitric oxide synthetase, NO synthase) is an enzyme with systematic name L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming). This enzyme catalyses the following chemical reaction

Pentalenic acid synthase (EC 1.14.15.11, CYP105D7, sav7469 (gene)) is an enzyme with systematic name 1-deoxypentalenate,reduced ferredoxin:O2 oxidoreductase. This enzyme catalyses the following chemical reaction

Biflaviolin synthase (EC 1.14.21.7, CYP158A2, CYP 158A2, cytochrome P450 158A2) is an enzyme with systematic name flaviolin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction

Aureusidin synthase is an enzyme with systematic name 2',4,4',6'-tetrahydroxychalcone 4'-O-beta-D-glucoside:oxygen oxidoreductase.

<span class="mw-page-title-main">Tetrahydrocannabinolic acid synthase</span> Enzyme

Tetrahydrocannabinolic acid (THCA) synthase is an enzyme responsible for catalyzing the formation of THCA from cannabigerolic acid (CBGA). THCA is the direct precursor of tetrahydrocannabinol (THC), the principal psychoactive component of cannabis, which is produced from various strains of Cannabis sativa. Therefore, THCA synthase is considered to be a key enzyme controlling cannabis psychoactivity. Polymorphisms of THCA synthase result in varying levels of THC in Cannabis plants, resulting in "drug-type" and "fiber-type" C. sativa varieties.

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase is an enzyme with systematic name ATP:methylphosphonate 5-triphosphoribosyltransferase. This enzyme catalyses the following chemical reaction

Dichlorochromopyrrolate synthase (EC 1.21.3.9, RebD, dichlorochromopyrrolic acid synthase) is an enzyme with systematic name 2-imino-3-(7-chloroindol-3-yl)propanoate ammonia-lyase (dichlorochromopyrrolate-forming). This enzyme catalyses the following chemical reaction

References

  1. Metcalf WW, Griffin BM, Cicchillo RM, Gao J, Janga SC, Cooke HA, Circello BT, Evans BS, Martens-Habbena W, Stahl DA, van der Donk WA (August 2012). "Synthesis of methylphosphonic acid by marine microbes: a source for methane in the aerobic ocean". Science. 337 (6098): 1104–7. doi:10.1126/science.1219875. PMC   3466329 . PMID   22936780.