mononucleotide

The loss of MSH6 function results in instability at mononucleotide repeats.

Flavodoxin is a bacterial protein that includes flavin mononucleotide.

Thus, the two substrates of this enzyme are dinucleotide and HO, whereas its product is mononucleotide.

This enzyme requires the presence of a cofactor, FMN (flavin mononucleotide).

Flavin mononucleotide is also used as an orange-red food colour additive, designated in Europe as E number E101a.

Luciferase produces blue/green light through the oxidation of reduced flavin mononucleotide and a long-chain aldehyde by diatomic oxygen.

The mutated region contains two associated genes: nicotinamide mononucleotide adenlyl transferase 1 (Nmnat-1) and ubiquitination factor e4b (Ube4b).

The electrons enter complex I via a prosthetic group attached to the complex, flavin mononucleotide (FMN).

Nicotinamide mononucleotide adenylyltransferase 1 is an enzyme that in humans is encoded by the NMNAT1 gene.

In the reaction, a reduced flavin mononucleotide oxidizes a long-chain aliphatic aldehyde to an aliphatic carboxylic acid.

The chain of reactions is initiated by a blue light photon, which excites the flavin mononucleotide (FMN) photosensitizer to the singlet excited state.

The quinolinic acid is converted to nicotinic acid mononucleotide (NaMN) by transfer of a phosphoribose moiety.

The RNA-editing system seen in the animal may have evolved from mononucleotide deaminases, which have led to larger gene families that include the apobec-1 and adar genes.

Chorismate synthase requires the presence of a reduced flavin mononucleotide (FMNH2 or FADH2) for its activity.

Flavin mononucleotide is a prosthetic group found in, among other proteins, NADH dehydrogenase, E.coli nitroreductase and old yellow enzyme.

Both DNA and RNA are built from nucleoside phosphates, also known as mononucleotide monomers, which are thermodynamically less likely to combine than amino acids.

Riboflavin carrier proteins (RFCPs) together with human serum albumin transport flavin mononucleotide (FMN) in the blood circuit.

NADH is oxidized to NAD, by reducing Flavin mononucleotide to FMNH in one two-electron step.

A flavoprotein is a protein that contains a flavin moiety, this may be in the form of FAD or FMN (Flavin mononucleotide) .

It also contributes to the chemical structure of riboflavin and Flavin mononucleotide (FMN), which is a nucleotide coenzyme, present in the enzyme Glycolate Oxidase.

FMN riboswitch (also RFN-element) binds flavin mononucleotide (FMN) to regulate riboflavin biosynthesis and transport.

NAmPRTase catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, one step in the biosynthesis of nicotinamide adenine dinucleotide.

Other names in common use include NMN deamidase, nicotinamide mononucleotide deamidase, and nicotinamide mononucleotide amidohydrolase.

Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).

Other names in common use include niacin ribonucleotidase, nicotinic acid mononucleotide glycohydrolase, nicotinic acid mononucleotide pyrophosphorylase, and nicotinic acid phosphoribosyltransferase.