Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.333 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase (EC 1.1.1.333, decaprenylphospho-beta-D-ribofuranose 2'-epimerase, Rv3791, DprE2) is an enzyme with systematic name trans,octacis-decaprenylphospho-beta-D-arabinofuranose:NAD+ 2-oxidoreductase. [1] This enzyme catalyses the following chemical reaction
The reaction is catalysed in the reverse direction.
Nitrate reductase (NAD(P)H) (EC 1.7.1.2, assimilatory nitrate reductase, assimilatory NAD(P)H-nitrate reductase, NAD(P)H bispecific nitrate reductase, nitrate reductase (reduced nicotinamide adenine dinucleotide (phosphate)), nitrate reductase NAD(P)H, NAD(P)H-nitrate reductase, nitrate reductase [NAD(P)H2], NAD(P)H2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NAD(P)+ oxidoreductase. This enzyme catalises the following chemical reaction
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 dTDP-4-dehydro-6-deoxyglucose reductase (EC 1.1.1.266) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a trans-2-enoyl-CoA reductase (NAD+) (EC 1.3.1.44) 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
Diacetyl reductase ((S)-acetoin forming) (EC 1.1.1.304, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
D-xylose reductase (EC 1.1.1.307, XylR, XyrA, msXR, dsXR, monospecific xylose reductase, dual specific xylose reductase, NAD(P)H-dependent xylose reductase, xylose reductase) is an enzyme with systematic name xylitol: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
Decaprenylphospho-beta-D-ribofuranose 2-oxidase (EC 1.1.98.3, decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase, Rv3790, DprE1) is an enzyme with systematic name trans,octacis-decaprenylphospho-beta-D-ribofuranose:FAD 2-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
Rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,3/1,4-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-beta/4-beta-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction
Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-beta/5-beta-D-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase is an enzyme with systematic name dTDP-6-deoxy-beta-L-mannose:N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-alpha-L-rhamnosyltransferase. This enzyme catalyses the following chemical reaction
Decaprenyl-phosphate phosphoribosyltransferase is an enzyme with systematic name trans,octacis-decaprenylphospho-beta-D-ribofuranose 5-phosphate:diphosphate phospho-alpha-D-ribosyltransferase. This enzyme catalyses the following chemical reaction
Galactan 5-O-arabinofuranosyltransferase is an enzyme with systematic name galactofuranan:trans,octacis-decaprenylphospho-beta-D-arabinofuranose 5-O-alpha-D-arabinofuranosyltransferase. This enzyme catalyses the following chemical reaction
Arabinofuranan 3-O-arabinosyltransferase is an enzyme with systematic name alpha-(1->5)-arabinofuranan:trans,octacis-decaprenylphospho-beta-D-arabinofuranose 3-O-alpha-D-arabinofuranosyltransferase. This enzyme catalyses the following chemical reaction:
UDP-arabinopyranose mutase is an enzyme with systematic name UDP-arabinopyranose pyranomutase. This enzyme catalyses the following chemical reaction
Biliverdin reductase B is a protein that in humans is encoded by the BLVRB gene.
Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.