Phosphonoacetaldehyde reductase (NADH)

Last updated
Phosphonoacetaldehyde reductase (NADH)
Identifiers
EC no. 1.1.1.309
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

Phosphonoacetaldehyde reductase (NADH) (EC 1.1.1.309, PhpC) is an enzyme with systematic name 2-hydroxyethylphosphonate:NAD+ oxidoreductase. [1] This enzyme catalyses the following chemical reaction

2-hydroxyethylphosphonate + NAD+ phosphonoacetaldehyde + NADH + H+

The enzyme from Streptomyces viridochromogenes catalyses a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate.

Related Research Articles

Nitrate reductase (NADH) (EC 1.7.1.1, assimilatory nitrate reductase, NADH-nitrate reductase, NADH-dependent nitrate reductase, assimilatory NADH: nitrate reductase, nitrate reductase (NADH2), NADH2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NAD+ oxidoreductase. This enzyme catalyzes the following chemical reaction

<span class="mw-page-title-main">Saccharopine dehydrogenase</span>

In molecular biology, the protein domain Saccharopine dehydrogenase (SDH), also named Saccharopine reductase, is an enzyme involved in the metabolism of the amino acid lysine, via an intermediate substance called saccharopine. The Saccharopine dehydrogenase enzyme can be classified under EC 1.5.1.7, EC 1.5.1.8, EC 1.5.1.9, and EC 1.5.1.10. It has an important function in lysine metabolism and catalyses a reaction in the alpha-Aminoadipic acid pathway. This pathway is unique to fungal organisms therefore, this molecule could be useful in the search for new antibiotics. This protein family also includes saccharopine dehydrogenase and homospermidine synthase. It is found in prokaryotes, eukaryotes and archaea.

In enzymology, a hydroxyphenylpyruvate reductase (EC 1.1.1.237) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">3alpha(or 20beta)-hydroxysteroid dehydrogenase</span> Class of enzymes

In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) is an enzyme that catalyzes the chemical reaction

In enzymology, an anthocyanidin reductase (EC 1.3.1.77) is an enzyme that catalyzes the chemical reaction

In enzymology, a dihydrouracil dehydrogenase (NAD+) (EC 1.3.1.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">6,7-dihydropteridine reductase</span> Class of enzymes

In enzymology, 6,7-dihydropteridine reductase (EC 1.5.1.34, also Dihydrobiopterin reductase) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NAD(P)H dehydrogenase (quinone)</span>

In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Saccharopine dehydrogenase (NAD+, L-lysine-forming)</span>

In enzymology, a saccharopine dehydrogenase (NAD+, L-lysine-forming) (EC 1.5.1.7) is an enzyme that catalyzes the chemical reaction

2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate reductase (EC 1.1.1.302, 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase, MjaRED, MJ0671 (gene)) is an enzyme with systematic name 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction

DTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+) (EC 1.1.1.339, tll (gene name)) is an enzyme with systematic name dTDP-6-deoxy-beta-L-talose:NAD+ 4-oxidoreductase. This enzyme catalyses the following chemical reaction

Long-chain acyl-(acyl-carrier-protein) reductase (EC 1.2.1.80, long-chain acyl-[acp] reductase, fatty acyl-[acyl-carrier-protein] reductase, acyl-[acp] reductase) is an enzyme with systematic name long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-(acyl-carrier protein)-forming). This enzyme catalyses the following chemical reaction

Acrylyl-CoA reductase (NADH) (EC 1.3.1.95) is an enzyme with systematic name propanoyl-CoA:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

Flavin reductase (NADH) (EC 1.5.1.36, NADH-dependent flavin reductase, flavin:NADH oxidoreductase) is an enzyme with systematic name flavin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

FAD reductase (NADH) (EC 1.5.1.37, NADH-FAD reductase, NADH-dependent FAD reductase) is an enzyme with systematic name FADH2:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

FMN reductase (NADH) (EC 1.5.1.42, NADH-FMN reductase) is an enzyme with systematic name FMNH2:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">NADH:ubiquinone reductase (non-electrogenic)</span> Class of enzymes

NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reaction:

Nitric oxide reductase (NAD(P), nitrous oxide-forming) (EC 1.7.1.14, fungal nitric oxide reductase, cytochrome P450nor, NOR (ambiguous)) is an enzyme with systematic name nitrous oxide:NAD(P) oxidoreductase. 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

References

  1. Blodgett JA, Thomas PM, Li G, Velasquez JE, van der Donk WA, Kelleher NL, Metcalf WW (August 2007). "Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide". Nature Chemical Biology. 3 (8): 480–5. doi:10.1038/nchembio.2007.9. PMC   4313788 . PMID   17632514.