Glucose-6-phosphate dehydrogenase (coenzyme-F420)

Last updated
Glucose-6-phosphate dehydrogenase (coenzyme-F420)
Identifiers
EC no. 1.1.98.2
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

Glucose-6-phosphate dehydrogenase (coenzyme-F420) (EC 1.1.98.2, coenzyme F420-dependent glucose-6-phosphate dehydrogenase, F420-dependent glucose-6-phosphate dehydrogenase, FGD1, Rv0407, F420-dependent glucose-6-phosphate dehydrogenase 1) is an enzyme with systematic name D-glucose-6-phosphate:F420 1-oxidoreductase. [1] [2] [3] This enzyme catalyses the following chemical reaction

D-glucose 6-phosphate + oxidized coenzyme F420 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420

Thus enzyme is specific for D-glucose 6-phosphate.

Related Research Articles

<span class="mw-page-title-main">Citric acid cycle</span> Chemical reactions to release energy in cells

The citric acid cycle —also known as the Krebs cycle, Szent-Györgyi-Krebs cycle or the TCA cycle (tricarboxylic acid cycle)—is a series of chemical reactions to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism. Even though it is branded as a 'cycle', it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized.

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide</span> Chemical compound which is reduced and oxidized

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

<span class="mw-page-title-main">Glucose-6-phosphate dehydrogenase</span> Enzyme involved in the production of energy by cells

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glyceraldehyde 3-phosphate dehydrogenase</span> Enzyme of the glycolysis metabolic pathway

Glyceraldehyde 3-phosphate dehydrogenase is an enzyme of about 37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In addition to this long established metabolic function, GAPDH has recently been implicated in several non-metabolic processes, including transcription activation, initiation of apoptosis, ER to Golgi vesicle shuttling, and fast axonal, or axoplasmic transport. In sperm, a testis-specific isoenzyme GAPDHS is expressed.

<span class="mw-page-title-main">Aldose reductase</span> Enzyme

In enzymology, aldose reductase is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. It is primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism.

<span class="mw-page-title-main">UTP—glucose-1-phosphate uridylyltransferase</span> Class of enzymes

UTP—glucose-1-phosphate uridylyltransferase also known as glucose-1-phosphate uridylyltransferase is an enzyme involved in carbohydrate metabolism. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e.,

<span class="mw-page-title-main">6-phosphogluconolactonase</span> Cytosolic enzyme

6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway:

D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.

<span class="mw-page-title-main">Phosphogluconate dehydrogenase (decarboxylating)</span>

In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">3-Hydroxybutyryl-CoA dehydrogenase</span> Class of enzymes

In enzymology, a 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) is an enzyme that catalyzes the chemical reaction

In enzymology, a coenzyme F420 hydrogenase (EC 1.12.98.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a 5,10-methylenetetrahydromethanopterin reductase (EC 1.5.98.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a methylenetetrahydromethanopterin dehydrogenase (EC 1.5.98.1) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Inositol-3-phosphate synthase</span>

In enzymology, an inositol-3-phosphate synthase is an enzyme that catalyzes the chemical reaction

Coenzyme F<sub>420</sub> Chemical compound

Coenzyme F420 or 8-hydroxy-5-deazaflavin is a coenzyme (sometimes called a cofactor) involved in redox reactions in methanogens, in many Actinomycetota, and sporadically in other bacterial lineages. It is a flavin derivative with an absorption maximum at 420 nm—hence its name. The coenzyme is a substrate for coenzyme F420 hydrogenase, 5,10-methylenetetrahydromethanopterin reductase and methylenetetrahydromethanopterin dehydrogenase.

<span class="mw-page-title-main">Glycerol-3-phosphate dehydrogenase (quinone)</span>

Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3 is an enzyme with systematic name sn-glycerol 3-phosphate:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase is an enzyme with systematic name L-cysteine:1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol ligase (AMP-forming). This enzyme catalyses the following chemical reaction

Coenzyme F420-0:L-glutamate ligase (EC 6.3.2.31, CofE-AF, MJ0768, CofE) is an enzyme with systematic name L-glutamate:coenzyme F420-0 ligase (GDP-forming). This enzyme catalyses the following chemical reaction

Mycofactocin (MFT) is a family of small molecules derived from a peptide of the type known as RiPP (ribosomally synthesized and post-translationally modified peptides), naturally occurring in many types of Mycobacterium. It was discovered in a bioinformatics study in 2011. All mycofactocins share a precursor in the form of premycofactocin (PMFT); they differ by the cellulose tail added. Being redox active, both PMFT and MFT have an oxidized dione (mycofactocinone) form and a reduced diol (mycofactocinol) form, respectively termed PMFTH2 and MFTH2.

References

  1. Purwantini E, Daniels L (May 1996). "Purification of a novel coenzyme F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis". Journal of Bacteriology. 178 (10): 2861–6. PMC   178021 . PMID   8631674.
  2. Bashiri G, Squire CJ, Baker EN, Moreland NJ (July 2007). "Expression, purification and crystallization of native and selenomethionine labeled Mycobacterium tuberculosis FGD1 (Rv0407) using a Mycobacterium smegmatis expression system". Protein Expression and Purification. 54 (1): 38–44. doi:10.1016/j.pep.2007.01.014. PMID   17376702.
  3. Purwantini E, Gillis TP, Daniels L (January 1997). "Presence of F420-dependent glucose-6-phosphate dehydrogenase in Mycobacterium and Nocardia species, but absence from Streptomyces and Corynebacterium species and methanogenic Archaea". FEMS Microbiology Letters. 146 (1): 129–34. doi: 10.1111/j.1574-6968.1997.tb10182.x . PMID   8997717.