Transketolase, discovered independently by Racker and Horecker in 1953 (and named by Racker) , did not receive much attention until 1992, when crystal X-ray structure analysis of the enzyme from Saccharomyces cerevisiae was performed . These data, together with the results of site-directed mutagenesis, made it possible to understand in detail the mechanism of thiamine diphosphate-dependent catalysis. Some progress was also made in studies of the functional properties of transketolase. The structure and mechanism of action of transketolase are reviewed, with the primary emphasis laid on the baker's yeast enzyme. The oligomeric structure of transketolase, the interaction of the coenzyme with the apoenzyme and the role of phosphate groups in the substrate interaction with the protein have been studied. The role of essential groups of apotransketolase in the binding of the coenzyme, substrates as well as in the catalytic act are described. The peculiarities of formation of. Transketolase (EC 184.108.40.206), Enzym, das die Transketolierung katalysiert, ein wichtiger Vorgang des Kohlenhydratstoffwechsels, insbesondere im Pentosephosphat-Zyklus und Calvin-Zyklus. Es kommt in verschiedenen Zell- und Gewebearten, wie Säugetierleber, in grünen Pflanzen, und in zahlreichen Bakterienspezies, vor. Das Enzym enthält Thiaminpyrophosphat als Coenzym und divalente Metallkationen. Bei der Transketolierung wird eine Transketolase, discovered independently by Racker and Horecker in 1953 (and named by Racker) , did not receive much attention until 1992, when crystal X-ray structure analysis of the enzyme from Saccharomyces cerevisiae was performed . These data, together with the results of site-directed mutagenesis, made it possible to understand in detail the mechanism of thiamine diphosphate-dependent catalysis. Some progress was also made in studies of the functional properties of transketolase. The. Structure and functioning mechanism of transketolase 1. Introduction. Transketolase (TK, EC 220.127.116.11) is the key rate-limiting enzyme of the non-oxidative branch of the... 2. General structure of transketolase. The molecule of TK from S. cerevisiae appears as a homodimer of structurally... 3..
Transketolase (TK) (Gen: TKT) ist der Name für Enzyme, die eine Ketogruppe von Xylulose-5-phosphat auf ein Aldol übertragen, meist Ribose-5-phosphat. Dieser Reaktionsschritt, zusammen mit dem der Transaldolase, verbindet die Glykolyse mit dem Pentosephosphatweg. Transketolasen kommen in Bakterien, Pflanzen und Tieren vor [Transketolase: structure and mechanism of action]. [Article in Russian] Kochetov GA. The structure and mechanism of action of transketolase are reviewed, with the primary emphasis laid on the baker's yeast enzyme. The oligomeric structure of transketolase, the interaction of the coenzyme with the apoenzyme and the role of phosphate groups in the substrate interaction with the protein have. TTPP is a competitive inhibitor, with respect to thiamin pyrophosphate, of bakers' yeast transketolase but it is neither a tight binding inhibitor nor a slow binding inhibitor. TTPP decreases the kinetically observed negative cooperativity seen for thiamin pyrophosphate and also decreases the rate constant for the hysteretic activation of the enzyme by thiamin pyrophosphate. We conclude that thiamin thiazolone pyrophosphate is not an effective transition state analogue for the.
Englisch: transketolase 1 Definition Als Transketolasen bezeichnet man die zur Gruppe II der EC-Klassifikation gehörigen Enzyme, die Aldosen meist unter Bildung anderer Aldosen in Ketosen umwandelt. Sie benötigen Thiamin -Pyrophosphat (Vitamin B1) als Cofaktor Transketolase. mit TPP-Effekt. Material. 2 ml EDTA-Blut (gekühlt, NICHT gefroren) Referenzbereiche < 20% TPP-Effekt und siehe Befundbericht Hinweis: Zur Ermittlung des Vitamin B1-Status als alleinige Bestimmung ungeeignet (siehe Anmerkungen). Verfahren. enzymatisch-fotometrisch. Sonstiges. Fremdlaborleistung. Diese Analyse fällt nicht in den Bereich der akkreditierten Untersuchungen. Transketolase (TK) is a ubiquitous enzyme operating in the non-oxidative branch of the pentose phosphate pathway (PPP) and in the Calvin-Benson cycle (CBC) in photosynthetic organisms. It catalyzes.. Transketolase is a thiamine-dependent enzyme and the catalytic mechanism invokes a series of proton transfer steps (Scheme 72). Initially, proton abstraction at C-2 of the thiazolium ring of thiamine occurs via Glu418. Following release of the first product, the αcarbanion intermediate serves as a nucleophile in an attack on an electrophilic aldehyde, facilitated by protonation of the aldehydic oxygen of the substrate. His30 and His263 are postulated to form hydrogen bonds to the negatively.
The laboratory synthesis of benzoin is interesting because it mimics the mechanism of TPP-dependant enzymatic reactions in biological systems. This reaction is not catalyzed by an enzyme - rather, the thiamine molecule acts on its own, playing a similar catalytic role to that played by its diphosphate ester cousin (TPP) in enzymatic reactions Mechanism of Transketolase - YouTube. Mechanism of Transketolase. Watch later. Share. Copy link. Info. Shopping. Tap to unmute. If playback doesn't begin shortly, try restarting your device
We have computationally determined the catalytic mechanism of human transketolase (hTK) using a cluster model approach and density functional theory calculations. We were able to determine all the relevant structures, bringing solid evidences to the proposed experimental mechanism, and to add important detail to the structure of the transition states and the energy profile associated with. The structure and mechanism of action of transketolase are reviewed, with the primary emphasis laid on the baker's yeast enzyme. The oligomeric structure of transketolase, the interaction of the coenzyme with the apoenzyme and the role of phosphate groups in the substrate interaction with the protein have been studied PDF | On Mar 1, 1961, Asoke G. Datta and others published Mechanism of Action of Transketolase | Find, read and cite all the research you need on ResearchGat Transketolase catalyzes the transfer of a glycolaldehyde residue from ketose (the donor substrate) to aldose (the acceptor substrate). In the absence of aldose, transketolase catalyzes a one-substrate reaction that involves only ketose. The mechanism of this reaction is unknown
Oxythiamine (OT), an analogue of anti-metabolite, can suppress the nonoxidative synthesis of ribose and induce cell apoptosis by causing a G1 phase arrest in vitro and in vivo. However, the molecular mechanism remains unclear yet. In the present study, a quantitative proteomic analysis using the modified SILAC method (mSILAC) was performed to determine the effect of metabolic inhibition on. We have computationally determined the catalytic mechanism of human transketolase (hTK) using a cluster model approach and density functional theory calculations. We were able to determine all the relevant structures, bringing solid evidences to the proposed experimental mechanism, and to add important detail to the structure of the transition states and the energy profile associated with catalysis. Furthermore, we have established the existence of a crucial intermediate of the. Transketolase, discovered independently by Racker and Horecker in 1953 (and named by Racker) , did not receive much attention until 1992, when crystal X-ray structure analysis of the enzyme from Saccharomyces cerevisiae was performed . These data, together with the results of site-directed mutagenesis, made it possible to understand in detail the mechanism of thiamine diphosphate.
Xylulose-5-phosphat wird unter dem Einfluss der Transketolase in Glycerinaldehyd-3-phosphat und einen Glykolaldehyd-Rest gespalten, der auf den Cofaktor des Enzyms, Thiaminpyrophosphat übertragen wird. Die so aktivierte C 2-Gruppe wird von der Transketolase auf Ribose-5-phosphat übertragen, wobei Sedoheptulose-7-phosphat entsteht. 2.5 Bildung von Erythrose-4-phosphat und Fructose-6-phosphat. We have determined the catalytic mechanism of human transketolase (hTK) computationally, using a cluster model approach and density functional theory calculations. We were able to determine all the relevant structures, bringing solid evidences to the proposed experimental mechanism, and to add important detail to the structure of the transition states and the energy profile associated with. TPP is an important cofactor that acts catalytically in the decarboxylation of α-keto acids and the transketolase reaction. In the mechanism of TPP-dependent enzymes, the cofactor is a carrier of hydroxyalkyl residues (also referred to as active aldehydes) Decarboxylation of α-keto acids
Ransfer can increase CD4Foxp3 Treg accumulation in transplant recipients as a attainable mechanism to prolong survival. To determine regardless of whether these CD4Foxp3 Treg cells have a regulatory ability, CD4CD25T cells had been purified from spleens of mice sacrificed on day 21. By this process 763 of those CD4CD25T cells ended up determined for being Foxp3, which have been then utilized. Although metabolic reprogramming is recognized as a hallmark of tumorigenesis and progression, little is known about metabolic enzymes and oncometabolites that regulate breast cancer metastasis, and very few metabolic molecules have been identified as potential therapeutic targets. In this study, the transketolase (TKT) expression correlated with tumor size in the 4T1/BALB/c syngeneic model . In animal experiments, hippocampal neurogenesis and the activity of thiamine-dependent transketolase decrease markedly under conditions of thiamine deficiency The mechanism of action of transketolase, mediated by its cofactor thiamine pyrophosphate (Figure 2), is well known by several studies [3,4], however, drugs targeting the active centre of transketolase, which act as cofactor analogs, have poor activity and low selectivity over other thiamine-dependent enzymes such as pyruvate dehydrogenase. Oxythiamine  and thiamine thiazolone diphosphate.
.jpg. From Wikimedia Commons, the free media repository. Jump to navigation Jump to search. File; File history; File usage on Commons; File usage on other wikis; Size of this preview: 568 × 599 pixels. Other resolutions: 227 × 240 pixels | 455 × 480 pixels | 569 × 600 pixels | 728 × 768 pixels | | . Original file image/jpeg) File information. Mechanism of Transketolase Mechanism TA Ali Jiwani 7.05 S03, Recitation #10, 4/25/03Based on a Handout Created by '01 TA Chris Allen Summary of reaction in pentose cycle CH2OH C C C CH2OP O HO OH H H + TK + Xylulose-5-
Information on EC 18.104.22.168 - transketolase. donor substrate, but not acceptor substrate, enhances affinity of cofactor to apoenzyme to a different degree for the two active centers, resulting in a negative cooperativity for cofactor binding Transketolase (TK) cofactor binding has been studied extensively over many years, yet certain mysteries remain, such as a lack of consensus on the cooperativity of thiamine pyrophosphate (TPP. Transketolase on the other hand simply cleaves off the ketone group from the substrate. It does not perform an aldol cleavage. Apart form this, the mechanisms of action of the two enzymes vary considerably. For instance transketolase requires thiamine pyrophosphate (TPP) as a cofactor but transaldolase does not
Transketolase catalyzes the transfer of a glycolaldehyde residue from ketose (the donor substrate) to aldose (the acceptor substrate). In the absence of aldose, transketolase catalyses the one-substrate reaction that involves only ketose. The mechanism of this reaction was unknown. Here we show that hydroxypyruvate serves as a substrate for one-substrate.. Transketolase is a prominent thiamin diphosphate-dependent enzyme in sugar metabolism that catalyzes the reversible transfer of a 2-carbon dihydroxyethyl fragment between a donor ketose and an acceptor aldose. The X-ray structures of transketolase from E. coli in a covalent complex with donor ketoses d-xylulose 5-phosphate (X5P) and d-fructose 6-phosphate (F6P) at 1.47 Å and 1.65 Å. both these enzymes utilise thiamine #=gf cc pyrophosphate as a cofactor, suggesting there may be common #=gf cc aspects in their mechanism of catalysis. #=gf sq 17602 #=gs a0a2v4xcw9_9flao/8-274 ac a0a2v4xcw9.1 #=gs a1r5z8_paeat/66-263 ac a1r5z8.1 #=gs a0a238whq0_9pseu/115-343 ac a0a238whq0.1 #=gs g8twr9_sulad/6-337 ac g8twr9.1 #=gs a0a1c5j1x5_9actn/16-362 ac a0a1c5j1x5.1 #=gs a1b2q0_pardp/12-336 ac a1b2q0.1 #=gs a0a319b5h4_asplb/24-361 ac a0a319b5h4.1 #=gs a0a3b3z9l6_9gobi/84-247 ac.
Transketolase participates in the pentose phosphate path-way, a pathway that produces reducing substances, such as reduced nicotinamide adenine dinucleotide phosphate (NADPH), for various cellular biosynthetic reactions, includ-ing for lipids, and for removal of oxygen radicals. Transketo- lase is critical for maintenance of the cellular redox state,37 thus thiamine deficiency results in the. The mechanism determining transketolase protein levels remains to be elucidated, but the data presented provide evidence that this may contribute to the complex regulatory mechanisms maintaining thiamine homeostasis in plants. INTRODUCTION. The Calvin Benson (C3) cycle is the primary pathway of atmospheric CO 2 uptake and fixation into organic molecules. The fixed carbon is used for sucrose. Our proteomic studies investigating the interactions between peritoneal (LP-9) and ovarian cancer (OVCAR-5) cells found transketolase (TKT) to be regulated in the co-culture system. This study characterized TKT expression in advanced stage (III/IV) serous ovarian cancers (n = 125 primary and n = 54 peritoneal metastases), normal ovaries (n = 6) and benign serous cystadenomas (n = 10) by immunohistochemistry. In addition, we also evaluated the function of TKT in ovarian cancer. The Catalytic Mechanism of Transketolase THIAMIN PYROPHOSPHATE-DERIVED TRANSITION STATES FOR TRANSKETOLASE AND PYRUVATE DEHYDROGENASE ARE NOT IDENTICAL* (Received for publication, February 17, 1983) David S. ShreveS, Michael P. Holloway, Jesse C. Haggerty, 1118, and Henry 2. Sable7 From the Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106 Thiamin thiazolone.
Short name: Transketolase-like_Pyr-bd. Overlapping homologous superfamilies . H Thiamin diphosphate-binding fold (IPR029061) H Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain superfamily (IPR042179) Description. Transketolase . 22.214.171.124 (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5. The metabolism of cancer cells is often reprogrammed by dysregulation of metabolic enzymes. Transketolase-like 1 (TKTL1) is a homodimeric transketolase linking the pentose-phosphate pathway with the glycolytic pathway. It is generally silenced at a transcriptional level in somatic tissues. However, in human cancers its expression is associated with the acquisition of a glycolytic phenotype. A transketolase reaction was catalyzed by cyanide ion under prebiotic conditions instead of its modern catalyst, thiamine pyrophosphate (TPP). Cyanide ion converted fructose plus glyceraldehyde to erythrose plus xylulose, the same products as are formed in modern biochemistry (but without the phosphate groups on the sugars). Cyanide was actually a better catalyst than was TPP in simple. In this work we present fundamental insights in multiple mechanistic aspects of ThDP-dependent enzymes using the Escherichia coli transketolase as model system. Studies on the control of cofactor dynamics and their impact on catalysis provided a model by which intrinsic cofactor movement facilitates bond strain reducing the energy barrier for C-C bond cleavage. Further, a core tenet of ThDP. Transketolase EC 126.96.36.199 (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor.
Es blockiert den Mechanismus des Transketolase-like-1 (TKTL1) Enzym, welches besonders bei schnell wachsenden bösartigen Tumorzellen für deren Wachstum durch Vergärung von Zucker (Glucose), deren häufig schwer ansprechende Therapie und meist schlechte Prognose bzw. hohe Rezidivrate sorgt. Enzyms, der Gärungsprozess wird gestoppt, die Mitochondrien beginnen wieder bei normalem Stoffwechsel. Transketolase encoded by the TKT gene is an enzyme of both the pentose phosphate pathway in all organisms and the Calvin cycle of photosynthesis. It catalyzes two important reactions, which operate in opposite directions in these two pathways. In the first reaction of the non-oxidative pentose phosphate pathway, the cofactor thiamine diphosphate accepts a 2-carbon fragment from a 5-carbon.
Here, we found that peroxisomal transketolase (known also as dihydroxyacetone synthase) and peroxisomal transaldolase (enzyme with unknown function) in the thermotolerant methylotrophic yeast, Ogataea (Hansenula) polymorpha, are required for xylose alcoholic fermentation, but not for growth on this pentose sugar. Mutants with knockout of DAS1 and TAL2 coding for peroxisomal transketolase and peroxisomal transaldolase, respectively, normally grow on xylose. However, these mutants. (wikipedia transketolase) (biochemistry) An enzyme of both the pentose phosphate pathway in animals and the Calvin cycle of photosynthesis, which catalyzes two important reactions. Text is available under the Creative Commons Attribution/Share-Alike License; additional terms may apply Transketolase (TKT) (EC 188.8.131.52) and transaldolase (TALDO) (EC 184.108.40.206) are key enzymes of non-oxidative branch of PPP determining its efficiency. TKT requires thiamine diphosphate (active vitamin B 1) as a co-factor. Processing large amounts of glucose automatically increases demand for dietary thiamine (the condition is called high calorie malnutrition), and thus, thiamine deficiency could have an inhibitory effect on PPP and increase the hyperglycaemia toxicity. Interestingly. In the oxidative phase of the pentose-phosphate pathway, transketolase serves to catalyze the transfer of a glycoaldehyde from xylulose-5-phosphate to ribose-5-phosphate, forming sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate in the process (Figure 1 and Figure 5) Transketolase is an ideal node for redox control within the cell. Its activation under oxidative conditions would be coherent with diversion of metabolic flux toward the PPP to provide reducing power for antioxidant defense systems. Moreover, the products of transketolase reaction form starting points for several other biosynthetic pathways, thus redistributing the fate of glucose derived metabolites towards macromolecular building blocks for cellular proliferation (see Figur
Transketolase is an important enzyme in a biochemical pathway called the pentose phosphate pathway. In this set of biochemical reactions, a molecule called glucose-6-phosphate, which is derived from the sugar glucose, is modified by transketolase, yielding two products—a sugar called ribose-5-phosphate and a molecule called reduced nicotinamide adenine dinucleotide phosphate (NADPH. Kinetic mechanism of active site non-equivalence in transketolase . By Marina V Kovina, Vitaliy A Selivanov, Natalia V Kochevova and German A Kochetov. Cite . BibTex; Full citation; Publisher: Wiley. Year: 2002. DOI identifier: 10.1016/s0014-5793(97)01331-8. OAI identifier: Provided by. While complete deﬁciency of glucose 6-phosphate dehy-drogenase (G6PD) or transketolase (TK) is lethal, TAL-deﬁcient mice developed normally with the Q. . Transketolase is an enzyme which requires thiamine and magnesium, and is involved in the regeneration of glutathione through the pentose phosphate pathway. This enzyme requires the coenzyme TPP to carry out this transformation. The thiamin diphosphate (ThDP)-dependent 1 enzyme transketolase (EC 220.127.116.11) catalyzes the cleavage of a carbon-carbon bond adjacent to a carbonyl group.
. Kovina, Vitaliy A. Selivanov, Natalia V. Kochevova, German A. Kochetov* A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899 Moscow, Russia Received 6 October 1997 Abstract The two-step mechanism of coenzyme (TDP) binding to apotransketolase has been examined by kinetic modeling, and. The enzyme requires the coenzyme thiamine pyrophosphate (TPP) in addition to Mg 2+ ions and the reaction mechanism is similar to that of pyruvate decarboxylase. A 2-carbon active glycol-aldehyde moiety bound to TPP is transferred from xylulose-5-P to ribose-5-P producing the 7-carbon ketose sedoheptulose-7-P and the aldose glyceraldehyde-3-P. Transketolase is the first enzyme characteristic of. transaldolase and transketolase. 26 de janeiro de 2021, às 3:1 ENCODES a protein that exhibits calcium ion binding (ortholog); carbohydrate binding (ortholog); magnesium ion binding (ortholog); INVOLVED IN glyceraldehyde-3-phosphate biosynthetic process (ortholog); pentose-phosphate shunt (ortholog); pentose-phosphate shunt, non-oxidative branch (ortholog); PARTICIPATES IN pentose phosphate pathway; pentose phosphate pathway - non-oxidative phase; ribose. International/Cummins Dealer Website: Links. 2017 Engines Single Module Aftertreatment CumminsEngines YouTube QuickServe® Online RAPIDSERVE™ Web Connected Diagnostics Genuine Cummins Parts Brochures Eaton Cummins JV. Previous Issue
The transketolase-like protein 1 (TKTL1) represents the enzymatic basis for an anaerobic glucose metabolism even in the presence of oxygen (aerobic glycolysis/Warburg effect), which is concomitant with a more malignant phenotype due to invasive growth/metastasis and resistance to radical and apoptosis inducing therapies. Expression of Apo10 and TKTL1 was analysed retrospectively in OSCC. Mechanism of EC 18.104.22.168 and EC 22.214.171.124 Transketolase. When cursor points to a box further details will be displayed in a tooltip window. If you click on the box you will change to appropriate reaction scheme or enzyme specification
Thiamine diphosphate (ThDP) dependent enzymes fulfill a number of indispensable functions in metabolism. Further, they are well-researched work-horses of biotechnology. Thus, deepening of our mechanistic and structural knowledge of these is imperative in improving biotechnological approaches, gain fundamental insight in enzymological principles and possibly develop antibiotics Novel Insights in Structure and Mechanism of Escherichia.
Information on EC 126.96.36.199 - formaldehyde transketolase for references in articles please use BRENDA:EC188.8.131.52 Please wait a moment until all data is loaded. This message will disappear when all data is loaded. EC Tree 2 Transferases 2.2 Transferring aldehyde or ketonic groups 2.2.1 Transketolases and transaldolases 184.108.40.206 formaldehyde transketolase. IUBMB Comments. A thiamine-diphosphate. ThDP is also a cofactor of cytosolic transketolase in the pentose phosphate pathway and of 2‐hydroxyacyl‐CoA lyase, a peroxisomal enzyme involved in α‐oxidation of phytanic acid. It seems that the α‐ketoglutarate dehydrogenase is most sensitive to thiamine deficiency, and reduced activity of this enzyme complex can quickly lead to reduced ATP synthesis, oxidative damage, and. . The novel transketolase-fluoropyruvate structure solved to a 1.60 Å resolution, it produced a snapshot image of the ketol donor prior to formation of the.
Transketolase is a universal amphibolic enzyme catalyzing reactions in the Calvin cycle and the oxidative pentose pathway producing erythrose-4-phosphate, leading to phenylpropanoid metabolism. Enhanced photosynthesis and carbon metabolism favor arsenic tolerance in Artemisia annua, a medicinal plant as revealed by homology-based proteomic Transketolase is widely used in organic synthesis. Enzyme Commission Number. EC 220.127.116.11. Activity > 0.1 units/mg. CAS No. 9014-48-6. Unit Definition. 1 U corresponds to the amount of enzyme which will produce 1 μmol of glyceraldehyde-3-phosphate from xylulose-5-phosphate per minute at pH 7.7 and 25°C, in the presence of ribose-5-phosphate, thiamine pyrophosphate and Mg2+ Storage. −20°C. Solution for Transketolase Transaldolase 1 FIGURE 12.34 Mechanism of CH,OH Lys-NH I the transketolase and transaldo- R-CH, CH, lase reactions. CH,OH N-CH, To illustrate the probable mechanism of the protein - ligand interaction, docking of compound 19 with P. falciparum transketolase is described in detail in Fig. 4b. Tight interaction between ligand and protein was observed as evident from several hydrogen bonds between polar atoms of compound 19 and those of active site residues Ala269, Gly30, Asp473 and Arg361
Nicht selten spielte dabei der Pentose-Phosphat-Weg und das Enzym Transketolase (TKT), bzw. ein verändertes Transketolase-Enzym (Transketolase-like 1, TKTL1), eine zentrale Rolle. US-Forscher konnten nun einen weiteren Mechanismus aufklären, der zu einer Resistenz von Pankreaskrebszellen gegenüber dem Chemomedikament Gemcitabin beiträgt.[note]Shukla SK et al. (2017): MUC1 and HIF-1alpha. This family includes transketolase enzymes EC 18.104.22.168 and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit P37941 EC 22.214.171.124. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis Transketolase (TKT) activity and nuclear localization promote hepatocellular carcinoma in a metabolic and a non-metabolic manner Zhaoyu Qin1†, Chan Xiang2†, Fan Zhong1, Yang Liu1, Qiongzhu Dong3, Kai Li4, Wenhao Shi4, Chen Ding1*, Lunxiu Qin3* and Fuchu He1,4* Abstract Background: Metabolic reprogramming is one of the hallmarks of cancer cells. The pentose phosphate pathway (PPP), a branch.