Glycolysis

Glycolysis (Graece γλυκύς glykys 'dulcis‘ + λύσις lysis 'dissolutio') est iter metabolicum in matrice cytoplasmatica percursum conversionum biochemicarum celerium a materia propulsoria externa glucoso C
₆H
₁₂O
₆ ad acidum pyruvicum CH
₃COCOO⁻
+ H⁺ intergradum ad nullum oxygenium consumentem formationem materiae propulsoriae internae ad usum mitochondriorum et organellarum cytoplasmatis et membranarum cellularium. Fructus secundus ad usum cellulae reactionum redoxidativarum multarum NADH + H⁺ est.

Cave: notitiae huius paginae nec praescriptiones nec consilia medica sunt.

Summarium glycolysis
$\Rightarrow$ +
Ex una molecula glucosi decem reactionibus biochemicis et duae moleculae acidi pyruvici et duae ATP et duae NADH nascuntur: α-D-glucosum + 2NAD⁺ + 2ADP + 2P_i ⟹ 2(pyruvatum) + 2NADH + 2ATP + 2H⁺ + 2H₂O

Varietates, quarum frequentissima et notissima (itaque in hoc loco descripta) est secundum Gustavum Embden et Otto Fritz Meyerhof (Via Embden-Meyerhof), notae sunt.

Quibusdam in cancrorum versio biochemica ab metabolismo mitochondriali ad glycolysem accidere videtur. Inhibitio enim glycolysis sit una diversis strategiis in cancris tractandis.

Glycolysis momentum glycaemiae maius habet.

Significatio et contextus

Glycolysis est pars catabolismi saccharidi in organismo plurimorum animalium. Ita magnus huius reactionum decursus est, ut non modo imminuantur moleculas monosaccharidi glucosi, sed recipiantur alia etiam commutantia antea monosaccharida, per exemplum fructosum. Sub intentione metabolica forti glycolyse celeriter energia prope locum indigentiae permitti possit, per exemplum prope vesiculas neurotransmissorum.^[1]

Usus proximus acidi pyruvici ex oxygenii praesentia pendet. Oxygenio praesente oxidatio in cyclo acidi citrici atque cursu phosphorylationis oxidativae ad aquam et dioxidum carbonii latior fit, absente invicem fermentatio (fermentatio homolactica) ad lactatum.

Ad summam, glycolysis a saccharidis nullo spatio interposito et celeriter energiam creat. Pro vita cottidiana equidem ad energiam efficiendum machinationes metabolismi supplentes necesse sunt. Oxygenio autem absente saccharomycetes glycolysem augebunt et consumptio glucosi aucta simul Effectus Pasteur nominatur.

Locus glycolysis

Reactiones biochemicae glycolysis in cellula, ibidem in matrice cytoplasmatica fiunt. Praesentia magnesii satis significationem habere videtur, quod dimidiae ( 1, 3, 7, 9, [[#Reactio biochemica 10: Pyruvati kinasis (PK)|10]] ^[2]) omnium reactionum hoc elemento egent.

Nonnullis protozois organella praecipua, glycosomata nominata, sunt, in quibus enzymi glycolysis inveniuntur. Exemplum protozoi cum glycosomatibus sunt trypanosomatidae, quae trypanosomiasem excitare possunt.

Cursus

Summarium graduum

In glycolysi ab una molecula glucosi effecto, duae acidi pyruvici fiunt:

D-Glucosum				Acidum pyruvicum
	+ 2 NAD⁺ + 2 ADP + 2 P_i		2		+ 2 NADH + 2 H⁺ + 2 ATP + 2 H₂O

Decem gradus accidunt, quorum primi quinque (reactiones biochemicae 1-5) pars praeparatoria et ultimi quinque gradus (reactiones biochemicae 6-10) pars quaestuosa nominantur.

Pars praeparatoria

Gradus	Substratum		Enzymum		Classis enzymarum	Annotationes
1	Glucosum	Glc	Hexokinasis	HK	Transferasis	Cofactor: Mg²⁺, Adenosinum triphosphoricum (ATP) (energia) consumitur
2	α-D-Glucoso-6-phosphatum	G6P	Phosphoglucosi isomerasis	PGI	Isomerasis
3	β-D-Fructoso-6-phosphatum	F6P	6-Phosphofructokinasis	PFK-1	Transferasis	Cofactor: Mg²⁺, Adenosinum triphosphoricum (ATP) (energia) consumitur
4	β-D-Fructoso-1,6-bisphosphatum	F1,6BP	Aldolasis	ALDO	Lyasis
5	Dihydroxyacetonophosphatum	DHAP	Triosophosphati Isomerasis	TPI	Isomerasis

Pars quaestuosa

Gradus	Substratum		Enzymum		Classis enzymarum	Annotationes
6	Glyceraldehydro-3-phosphatum	GADP	Glyceraldehydrophosphati dehydrogenasis	GAPDH	Oxidoreductasis	Nicotinamidum adeninum dinucleotidum (NADH, baiulus hydrogenii) formatur. Additio phosphati phosphorolysis vocatur.
7	1,3-Bisphosphoglyceratum	1,3BPG	Phosphoglycerati kinasis	PGK	Phosphoglycerati kinasis	Cofactor: Mg²⁺, Adenosinum triphosphoricum (ATP) (energia) formatur
8	3-Phosphoglyceratum	3PG	Phosphoglycerati mutasis	PGM, PGAM	Mutasis
9	2-Phosphoglyceratum	2PG	Enolasis	ENO	Lyasis	Cofactor: 2 Mg²⁺, una molecula aquae liberatur
10	Phosphoenolpyruvatum	PEP	Pyruvati kinasis	PK	Transferasis	Cofactor: Mg²⁺, Adenosinum triphosphoricum (ATP) (energia) formatur

Gradus glycolysis

Reactio biochemica 1: Hexokinasis (HK)

1. A glucoso ad glucoso-6-phosphatum

Hac in reactione prima phosphatum additur et in decima demum removebitur. Iste grex phosphati glucosum ex cellulam evadere prohibet, hexokinasis similem hauritorii glucosi laborans. Cofactor est Mg²⁺. Kation hydrogenii deponitur.

Haec reactio consumit energiam. ΔG° = -16,7 kJ/mol.

De biochemico Warburg effectus metabolismi maximi in cancro descriptus hac reactione hexokinasis molita est.

D-Glucosum

Hexokinasis

α-D-Glucoso-6-phosphatum

ATP

ADP

(Mg²⁺)

H⁺

Reactio biochemica 2: Phosphoglucosi isomerasis (PGI)

2. A glucoso-6-phosphato ad fructoso-6-phosphatum

Fructosi (cum phosphato) formatio.

α-D-Glucoso-6-phosphatum

Phosphoglucosi isomerasis

β-D-Fructoso-6-phosphatum

Reactio biochemica 3: Phosphofructokinasis (PFK-1)

3. A fructoso-6-phosphato ad fructoso-1,6-bisphosphatum

Cum energia phosphofructokinasis imponit alium phosphatum in moleculam - brevi bipartita ... Hic quoque Mg²⁺ cofactor est. Iterum kation hydrogenii deponitur.

Haec reactio consumit energiam. ΔG° = -14,2 kJ/mol.

β-D-Fructoso-6-phosphatum

Phosphofructokinasis

β-D-Fructoso-1,6-bisphosphatum

ATP

ADP

(Mg²⁺)

H⁺

Reactio biochemica 4: Aldolasis (ALDO)

4. A fructoso-1,6-bisphosphato ad glyceraldehydro-3-phosphatum et dihydroxyacetonophosphatum

Separatio ex uno pentoso uno ad duos triosos: aldolasis fructosum moleculis duabus phosphati gravidum in partes duas, quaeque unam moleculam phosphati portans, dividit. Solum dihydroxyacetonophosphatum in reactionem proximam (5) ingreditur. Altera substantia, glyceraldehydro-3-phosphatum, reactioni proximae deest, et statim in reactionem sextam (6) transit.

β-D-Fructoso-1,6-bisphosphatum

Aldolasis

D-Glyceraldehydro-3-phosphatum

Dihydroxyacetonophosphatum

+

Reactio biochemica 5: Triosophosphati isomerasis (TPI)

5. A dihydroxyacetonophosphato ad glyceraldehydro-3-phosphatum

Unitas: Post isomerasem secundam nihil restat aliud quam Glyceraldehydrum cum phosphato.

Dihydroxyacetonophosphatum

Triosophosphati isomerasis

D-Glyceraldehydro-3-phosphatum

Reactio biochemica 6: Glyceraldehydrophosphati dehydrogenasis (GAPDH)

6. A glyceraldehydro-3-phosphato ad 1,3-bisphosphoglyceratum

Oxidatio et phosphorylatio (phosphorolysis).

D-Glyceraldehydro-3-phosphatum

GAPDH

D-1,3-Bisphosphoglyceratum

NAD⁺

NADH⁺+H⁺

P_i

H⁺

Reactio biochemica 7: Phosphoglycerati kinasis (PGK)

7. A 1,3-bisphosphoglycerato ad 3-phosphoglyceratum

Cofactor: Mg²⁺

Haec reactio consumit energiam. ΔG° = -18,5 kJ/mol).

D-1,3-Bisphosphoglyceratum

Phosphoglycerati kinasis

D-3-Phosphoglyceratum

ADP

ATP

H⁺

(Mg²⁺)

Reactio biochemica 8: Phosphoglycerati mutasis (PGM, PGAM)

8. A 3-phosphoglycerato ad 2-phosphoglyceratum

D-3-Phosphoglyceratum

Phosphoglycerati mutasis

D-2-Phosphoglyceratum

Reactio biochemica 9: Enolasis (ENO)

9. A 2-phosphoglycerato ad phosphoenolpyruvatum

Cofactores: Duo ionta Mg²⁺, alterum ob causam phosphoglyceratorum conformationis appendicis carboxylici alterum ut socius dehydratationis.

D-2-Phosphoglyceratum

Enolasis

Phosphoenolpyruvatum

H₂O

(2 Mg²⁺)

Reactio biochemica 10: Pyruvati kinasis (PK)

10. A phosphoenolpyruvato ad acidum pyruvicum

Cofactor: Mg²⁺; PK-isoformae L, R, M1, et M2 notae sunt.

Haec reactio consumit energiam. ΔG° = -31,4 kJ/mol.

Phosphoenolpyruvatum

Pyruvati kinasis

Acidum pyruvicum

ADP

ATP

H⁺

(Mg²⁺)

Morbi et aegrotationes cum glycolysi coniunctae

Carcinogenesis et cancer

Conferatur pagina principalis cancer (morbus).

Intra formationem cancri (carcinogenesis) transformatio cellularum sanarum in cancrum observatur incrementum glycolysis^[3]. Quoque detrimentum mitochondriorum cum versio metabolica ad glycolysem disputatum est^[4]. Inhibitio ergo glycolysis est una diversis strategiis in cancris tractandis^[5].

Significatio carcinogensis

Cum glucosi oxidatio (aerobica) cellularum sanarum principalis fons energiae putetur, cancri cellulae autem glycolysem (anaerobicam) praecipue utuntur^[6] - etiam in oxygenii praesentia (effectus Warburgiensis^[7]). At mutationes programmarum cycli cellularis in carcinogenesi momentum maximum habere putatur. Isoforma M2 enzymi pyruvati kinasis (PKM2) tetramerus tumorigenesem impellere videtur^[8].

Nonnulli cancri cum adenoviris oncolyticis incrementum reactionum anapleroticarum ostendunt^[9].

Morbi neurodegenerativi

Conferatur pagina principalis Neurodegeneratio.

Commutationes itineris glycolysis mature in morbis neurodegenerativis appareant^[10].

Notae

↑ Jang S., Nelson J. C., Bend E. G., Rodríguez-Laureano L., Tueros F. G., Cartagenova L., Underwood K., Jorgensen E. M., Colón-Ramos D. A. (Apr 2016). "Glycolytic Enzymes Localize to Synapses under Energy Stress to Support Synaptic Function". Neuron 90 (2): 278-91
↑ Magnesio omnia kinasium enolasisque egent
↑ Shi Y., Liu S., Ahmad S., Gao Q. (2018). "Targeting Key Transporters in Tumor Glycolysis as a Novel Anticancer Strategy". Curr Top Med Chem: 10.2174/1568026618666180523105234
↑ Gonzalez C. D., Alvarez S., Ropolo A., Rosenzvit C., Bagnes M. F., Vaccaro M. I. (2014). "Autophagy, Warburg, and Warburg reverse effects in human cancer". BioMed research international: 2014:926729
↑ Sheng H., Tang W. (2016). "Glycolysis Inhibitors for Anticancer Therapy: A Review of Recent Patents". Recent Pat Anticancer Drug Discov 11 (3): 297-308
↑ Zhang X., Zhao H., Li Y., Xia D., Yang L., Ma Y., Li H. (2018). "The role of YAP/TAZ activity in cancer metabolic reprogramming". Mol Cancer 17 (1): 134
↑ Warburg O (1956). "On respiratory impairment in cancer cells". Science 124 (3215): 269-70
↑ Wong N., Ojo D., Yan J., Tang D. (2015). "PKM2 contributes to cancer metabolism". Cancer Lett 356 (2 Pt A): 184-91
↑ Dyer A., Schoeps B., Frost S., Jakeman P., Scott E. M., Freedman J., Jacobus E. J., Seymour L. W. (2019). "Antagonism of Glycolysis and Reductive Carboxylation of Glutamine Potentiates Activity of Oncolytic Adenoviruses in Cancer Cells". Cancer research 79 (2): 331-45
↑ Bell S. M., Burgess T., Lee J., Blackburn D. J., Allen S. P., Mortiboys H. (Nov 2020). "Peripheral Glycolysis in Neurodegenerative Diseases". International journal of molecular sciences 21 (23): 8924 doi:10.3390/ijms21238924

Nexus interni

Plura legere si cupis

Sigurd Lenzen, "A Fresh View of Glycolysis and Glucokinase Regulation: History and Current Status", Journal of Biological Chemistry, 2014ː 12189-12194
Marks: Basic Medical Biochemistry, Wolters Kluwer & Lippincott, Williams and Williams (sexta editioː 2023)

[1] Jang S., Nelson J. C., Bend E. G., Rodríguez-Laureano L., Tueros F. G., Cartagenova L., Underwood K., Jorgensen E. M., Colón-Ramos D. A. (Apr 2016). "Glycolytic Enzymes Localize to Synapses under Energy Stress to Support Synaptic Function". Neuron 90 (2): 278-91

[2] Magnesio omnia kinasium enolasisque egent

[3] Shi Y., Liu S., Ahmad S., Gao Q. (2018). "Targeting Key Transporters in Tumor Glycolysis as a Novel Anticancer Strategy". Curr Top Med Chem: 10.2174/1568026618666180523105234

[4] Gonzalez C. D., Alvarez S., Ropolo A., Rosenzvit C., Bagnes M. F., Vaccaro M. I. (2014). "Autophagy, Warburg, and Warburg reverse effects in human cancer". BioMed research international: 2014:926729

[5] Sheng H., Tang W. (2016). "Glycolysis Inhibitors for Anticancer Therapy: A Review of Recent Patents". Recent Pat Anticancer Drug Discov 11 (3): 297-308

[6] Zhang X., Zhao H., Li Y., Xia D., Yang L., Ma Y., Li H. (2018). "The role of YAP/TAZ activity in cancer metabolic reprogramming". Mol Cancer 17 (1): 134

[7] Warburg O (1956). "On respiratory impairment in cancer cells". Science 124 (3215): 269-70

[8] Wong N., Ojo D., Yan J., Tang D. (2015). "PKM2 contributes to cancer metabolism". Cancer Lett 356 (2 Pt A): 184-91

[9] Dyer A., Schoeps B., Frost S., Jakeman P., Scott E. M., Freedman J., Jacobus E. J., Seymour L. W. (2019). "Antagonism of Glycolysis and Reductive Carboxylation of Glutamine Potentiates Activity of Oncolytic Adenoviruses in Cancer Cells". Cancer research 79 (2): 331-45

[10] Bell S. M., Burgess T., Lee J., Blackburn D. J., Allen S. P., Mortiboys H. (Nov 2020). "Peripheral Glycolysis in Neurodegenerative Diseases". International journal of molecular sciences 21 (23): 8924 doi:10.3390/ijms21238924

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