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Mevalonate pathway

The mevalonate pathway is a key anabolic in eukaryotes, , and some that synthesizes isoprenoid precursors from , enabling the production of , non-sterol isoprenoids, and other vital biomolecules essential for cellular function. This pathway begins with the condensation of three molecules of to form 3-hydroxy-3-methylglutaryl-CoA () via HMG-CoA synthase, followed by the rate-limiting reduction of to mevalonate catalyzed by (), an targeted by statins for cholesterol-lowering therapy. Mevalonate is then sequentially phosphorylated and decarboxylated to yield isopentenyl pyrophosphate (), the universal five-carbon building block of isoprenoids, through the actions of mevalonate kinase, phosphomevalonate kinase, and mevalonate diphosphate decarboxylase. IPP isomerizes to dimethylallyl pyrophosphate (DMAPP), which condenses stepwise—first to and then to (FPP)—via farnesyl pyrophosphate synthase, marking the entry into branched downstream routes. serves as a : two molecules condense to form via squalene synthase, initiating cholesterol biosynthesis through epoxidation and cyclization steps that produce lanosterol and ultimately ; alternatively, FPP extends to geranylgeranyl pyrophosphate (GGPP) for non-sterol isoprenoid synthesis. Key products include for membrane fluidity and precursor to steroid hormones, bile acids, and ; GGPP and FPP for prenylation of proteins like and Rho , crucial for ; and other isoprenoids such as ubiquinone (for electron transport), (for ), and A. The pathway's regulation is tightly controlled, primarily at the HMGCR step through sterol regulatory element-binding protein 2 (SREBP2) transcription and feedback inhibition by s and isoprenoids, ensuring in . Dysregulation of the mevalonate pathway contributes to diseases like and cancer, where upregulated activity supports tumor growth via enhanced and membrane synthesis, highlighting its therapeutic targeting potential beyond cardiovascular applications. Evolutionarily, it contrasts with the non-mevalonate () pathway in and many , underscoring its essential role in eukaryotic and archaeal .

Introduction

Definition and overview

The mevalonate pathway is an anabolic metabolic pathway that converts acetyl-CoA into isopentenyl pyrophosphate (IPP) and its isomer dimethylallyl pyrophosphate (DMAPP), utilizing mevalonate as a key intermediate. These five-carbon isoprenoid units serve as building blocks for a diverse array of biomolecules, including sterols, dolichols, and prenyl groups essential for cellular functions. The pathway was identified in the 1950s through pioneering work by Feodor Lynen and Konrad Bloch, who elucidated the mechanisms of biosynthesis from precursors, earning them the 1964 in Physiology or Medicine for discoveries concerning the metabolism of and fatty acids. Lynen's group in particular demonstrated the role of mevalonate as a critical intermediate in this process using extracts. In outline, the pathway proceeds from the condensation of two molecules of to form acetoacetyl-CoA, followed by its reaction with another to yield 3-hydroxy-3-methylglutaryl-CoA (), which is then reduced to mevalonate; subsequent and steps produce IPP and DMAPP. This route serves as the primary means of isoprenoid in eukaryotes—including , fungi, and the cytosol of , and certain bacteria, while many bacteria and the plastids of employ an alternative non-mevalonate () pathway.

Biological significance

The mevalonate pathway serves as the primary biosynthetic route for isoprenoids in animals, fungi, the of plants, , and some bacteria, generating over 30,000 distinct compounds that fulfill diverse cellular roles. These include sterols such as , which maintain and integrity; prenyl groups like farnesyl and that enable of proteins, including small involved in signaling; dolichols essential for N-linked of proteins in the ; ubiquinones (coenzyme Q) that function as electron carriers in the mitochondrial respiratory chain; and the polyprenyl component of A, a key in for . This vast array of products underscores the pathway's centrality in supporting membrane structure, protein function, and energy production across cellular compartments. Evolutionarily, the mevalonate pathway represents an ancient metabolic innovation conserved across the three domains of life, likely originating in the and adapting to specialized roles in eukaryotes. Its persistence highlights its indispensable contributions to fundamental processes: sterols and ensure membrane adaptability in varying environments, prenylation of proteins like facilitates intracellular signaling cascades critical for growth and differentiation, and isoprenoid-derived cofactors such as ubiquinone and heme A sustain aerobic respiration and . In modern organisms, particularly mammals, the pathway's flux intensifies during , as seen in rapidly dividing tissues and cancer cells, where heightened demand for isoprenoids supports biomass accumulation and survival signaling. The pathway draws substantially from the cellular pool, integrating it into broader and consuming a notable fraction under basal conditions to fuel isoprenoid demands. This interconnects the mevalonate route with , as both compete for the same cytosolic substrate derived from mitochondrial export via citrate. Furthermore, it ties into upstream catabolic networks, with originating from and the tricarboxylic acid (Krebs) cycle, enabling coordinated responses to nutrient availability and energy status that balance with cellular needs.

Biosynthetic pathway

Upper mevalonate pathway

The upper mevalonate pathway comprises the initial three enzymatic steps that convert three molecules of into mevalonate, the committed precursor for downstream isoprenoid biosynthesis in eukaryotes. This segment of the pathway is highly conserved across species and serves as the entry point for derived from or into isoprenoid production. The first step involves the reversible Claisen-type condensation catalyzed by acetoacetyl-CoA thiolase (EC 2.3.1.9), where two molecules of acetyl-CoA form acetoacetyl-CoA:
$2 \text{ acetyl-CoA} \rightleftharpoons \text{acetoacetyl-CoA} + \text{CoA}
This reaction establishes the four-carbon β-ketoacyl intermediate essential for chain elongation.
In the second step, HMG-CoA synthase (EC 2.3.3.10) catalyzes the irreversible aldol addition of a third acetyl-CoA to acetoacetyl-CoA, incorporating water to yield 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA), a six-carbon branched-chain thioester:
\text{acetoacetyl-CoA} + \text{acetyl-CoA} + \text{H}_2\text{O} \rightarrow \text{HMG-CoA} + \text{CoA} + \text{H}^+
This condensation introduces the hydroxyl and methyl groups characteristic of HMG-CoA.
The third and rate-limiting step is the reduction of HMG-CoA to (R)-mevalonate, mediated by HMG-CoA reductase (EC 1.1.1.34), which requires two equivalents of NADPH and proceeds via a sequential two-step reduction mechanism:
\text{HMG-CoA} + 2 \text{ NADPH} + 2 \text{ H}^+ \rightarrow \text{mevalonate} + \text{CoA} + 2 \text{ NADP}^+
This enzyme represents the primary regulatory point in the pathway.
Overall, the upper pathway stoichiometry balances as follows:
$3 \text{ acetyl-CoA} + 2 \text{ NADPH} + 2 \text{ H}^+ + \text{H}_2\text{O} \rightarrow \text{mevalonate} + 3 \text{ CoA} + 2 \text{ NADP}^+
In animal cells, the synthesis of acetoacetyl-CoA and HMG-CoA occurs in the cytosol, while the reduction to mevalonate takes place in the endoplasmic reticulum membrane.

Lower mevalonate pathway

The lower mevalonate pathway encompasses the conversion of mevalonate to the isoprenoid precursors isopentenyl diphosphate () and dimethylallyl diphosphate (DMAPP), involving sequential , , and steps that activate the C6 mevalonate unit into reactive building blocks for downstream . This segment of the pathway is energy-intensive, consuming three molecules of ATP to drive the transformations, and contrasts with the upper pathway by focusing on the activation and fragmentation of mevalonate rather than its initial formation. The first step is catalyzed by mevalonate (EC 2.7.1.36), which phosphorylates mevalonate at the position using ATP to yield mevalonate 5- and . This ATP-dependent reaction is the initial activation, with the conserved across eukaryotes, , and some , featuring key catalytic residues such as and aspartate that facilitate substrate binding and transfer. In the subsequent step, phosphomevalonate (EC 2.7.4.2) further phosphorylates mevalonate 5- at the same hydroxyl group, again utilizing ATP to produce mevalonate 5-diphosphate (also known as diphosphomevalonate) and . This exhibits structural variations by , adopting an NMP kinase fold in animals but a GHMP kinase domain in , underscoring evolutionary adaptations while maintaining the core function. The third step involves diphosphomevalonate decarboxylase (also termed mevalonate diphosphate decarboxylase, 4.1.1.33), which catalyzes the ATP-dependent of mevalonate 5-diphosphate to form , releasing CO₂ and producing and inorganic . This reaction incorporates a third at the position prior to , effectively rearranging the carbon skeleton; in some organisms, such as certain , the decarboxylase also possesses phosphomevalonate activity, integrating the second and third steps into a bifunctional . The overall for the conversion of mevalonate to is: \text{Mevalonate} + 3 \text{ ATP} \rightarrow \text{IPP} + 3 \text{ ADP} + \text{ P}_i + \text{ CO}_2 This process generates the allylic C5 unit IPP, which serves as the primary precursor. IPP is then isomerized to DMAPP by isopentenyl-diphosphate Δ-isomerase (EC 5.3.3.2), a reversible reaction involving a 1,3-proton shift that converts the homoallylic IPP to the more electrophilic allylic DMAPP. This isomerization, often represented as: \text{IPP} \rightleftharpoons \text{DMAPP} is essential for providing both isomers as substrates for prenyltransferase enzymes in isoprenoid chain elongation, with the enzyme existing in type I (NAD(P)H-dependent, found in eukaryotes and some bacteria) and type II (FMN-dependent, prevalent in archaea) variants to accommodate diverse cellular environments. In some archaea, such as Thermoplasma acidophilum, the lower pathway features variations with additional phosphorylation steps to produce modified isoprenoids: mevalonate is first phosphorylated at C3 by mevalonate-3-kinase to mevalonate 3-phosphate, followed by mevalonate-3-phosphate-5-kinase adding a second phosphate to yield mevalonate 3,5-bisphosphate, which undergoes ATP-independent decarboxylation to isopentenyl phosphate and subsequent phosphorylation to IPP. These modifications support the synthesis of archaeal-specific ether-linked lipids, diverging from the canonical eukaryotic and bacterial routes while converging on IPP as the output.

Enzymes and reactions

Upper pathway enzymes

The upper pathway of the mevalonate pathway in mammals involves three key enzymes that convert to mevalonate: acetoacetyl-CoA (ACAT), 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) , and (HMGR). These enzymes operate primarily in the , with the exception of a mitochondrial isoform of HMG-CoA that functions in rather than . No specific cofactors beyond substrates and are required for ACAT and HMG-CoA , while HMGR utilizes NADPH as a cofactor for its reductive step. Acetoacetyl-CoA thiolase (ACAT), also known as acetyl-CoA acetyltransferase (EC 2.3.1.9), catalyzes the initial Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA and free CoA, a reversible reaction that initiates the carbon chain elongation in the mevalonate pathway. In mammals, ACAT exists as cytosolic and mitochondrial isoforms, with the cytosolic form dedicated to cholesterol and isoprenoid biosynthesis. The enzyme functions as a homodimer, with each subunit approximately 40 kDa, featuring two distinct active sites: a cysteine-directed site for the degradative thiolytic cleavage and a histidine-directed site for the biosynthetic condensation. The catalytic mechanism proceeds via enolate formation on one acetyl-CoA molecule, followed by nucleophilic attack on the carbonyl of the second acetyl-CoA, facilitated by a conserved His348-Asn319 pair in the active site. ACAT activity is inhibited by high levels of free CoA, which competes with acetyl-CoA for binding and exerts product inhibition on the condensation reaction, helping to regulate flux through the pathway. HMG-CoA synthase, or 3-hydroxy-3-methylglutaryl-CoA synthase (EC 2.3.3.10), catalyzes the subsequent condensation of acetoacetyl-CoA with another to produce and free , committing the pathway to mevalonate production. Mammals express two isoforms: the cytosolic HMGCS1 (encoded by the HMGCS1 gene), which supports the mevalonate pathway for isoprenoid synthesis, and the mitochondrial HMGCS2 (encoded by HMGCS2), involved in during . The cytosolic isoform localizes exclusively to the , while the mitochondrial form is targeted to the via an N-terminal . Structurally, both isoforms are homodimers of about 50 kDa subunits, with a TIM barrel-like fold in the . The mechanism involves three steps: initial of a catalytic (Cys129 in human HMGCS1) by to form an acetyl-enzyme , enolization of the bound acetoacetyl-CoA to generate a nucleophilic , and Claisen of the enolate with the acetyl group, followed by to release . This enolization step is rate-limiting and is promoted by a conserved glutamate residue that abstracts the alpha-proton from acetoacetyl-CoA. HMG-CoA reductase (HMGR), or 3-hydroxy-3-methylglutaryl-CoA reductase (EC 1.1.1.34), catalyzes the irreversible reduction of HMG-CoA to mevalonate using two molecules of NADPH, serving as the rate-limiting and committed step of the mevalonate pathway. In humans, HMGR is encoded by the HMGCR gene on chromosome 5 and localizes to the endoplasmic reticulum (ER) membrane, where its N-terminal domain anchors the enzyme. The full-length human HMGR is a 97 kDa glycoprotein that forms tetramers, with the membrane domain comprising eight transmembrane helices spanning the ER bilayer, while the C-terminal catalytic domain (residues 463–887) protrudes into the cytosol. The catalytic mechanism is zinc-independent and proceeds via an ordered sequential bi-bi mechanism, with the pro-R hydride from the 4-position of NADPH transferred directly to the C5 position of HMG-CoA, followed by protonation at C3 and a second NADPH-dependent reduction. This hydride transfer is facilitated by a conserved arginine (Arg590) that polarizes the substrate carbonyl, enabling the four-electron reduction without metal ion assistance, and the reaction releases CoA as a product.

Lower pathway enzymes

The lower mevalonate pathway involves a series of enzymatic steps that convert mevalonate into the isoprenoid precursors isopentenyl diphosphate () and dimethylallyl diphosphate (DMAPP), primarily through , , and reactions. These enzymes operate in the of eukaryotic cells and are essential for channeling intermediates toward downstream isoprenoid biosynthesis. Mevalonate kinase (MVK), encoded by the MVK , catalyzes the first committed step by phosphorylating the C5 hydroxyl group of mevalonate using ATP as the donor, yielding 5-phosphomevalonate and ; this enzyme is classified as ATP:mevalonate 5-phosphotransferase (EC 2.7.1.36). MVK is subject to feedback inhibition by downstream isoprenoid products such as (GPP) and (FPP), which bind competitively at the ATP site with low micromolar affinities (Ki ≈ 0.4–0.6 μM), thereby regulating flux through the pathway to prevent overaccumulation of intermediates. This regulatory mechanism helps maintain cellular in and non-sterol isoprenoid production. Phosphomevalonate kinase (PMK), less extensively characterized than other pathway enzymes, transfers a second phosphate group from ATP to the C3 hydroxyl of 5-phosphomevalonate, producing (3R)-mevalonate 5-diphosphate and (EC 2.7.4.2). This cytosolic enzyme follows an ordered bi-bi kinetic , with 5-phosphomevalonate first, followed by ATP, and exhibits a preference for Mg²⁺ as a cofactor to facilitate phosphoryl transfer. Structural studies reveal substrate-induced conformational changes that position the C3 hydroxyl for nucleophilic attack on the ATP γ-phosphate, underscoring its role in preparing the substrate for subsequent . Mevalonate diphosphate decarboxylase (MDD), also known as diphosphomevalonate decarboxylase (EC 4.1.1.34), performs a multifunctional role by first phosphorylating the position of mevalonate 5-diphosphate using ATP to form a transient 3,5-bisphosphate intermediate, followed by Mg²⁺-dependent to generate , CO₂, , and inorganic . This ATP hydrolysis-driven process requires Mg²⁺ for nucleotide coordination and proceeds via a β-elimination , where the C3 acts as a after of the C3 hydroxyl by a catalytic aspartate residue (e.g., Asp283 in MDD), facilitating elimination of the C1 and formation of the C2–C3 double bond. Crystal structures of MDD highlight a funnel-shaped that accommodates sequential substrate and binding, with key residues like Arg144 stabilizing the for departure. Isopentenyl diphosphate:dimethylallyl diphosphate isomerase (IDI, 5.3.3.2) catalyzes the reversible of to DMAPP by shifting the from the C2–C3 position in to the C3–C4 position in DMAPP, providing the allylic starter unit for prenyl chain elongation. Two distinct types exist: type 1 IDI, predominant in eukaryotes and some , is a metal-dependent (requiring Mg²⁺ or Mn²⁺) that operates via a mechanism involving direct addition/abstraction at the without cofactors; type 2 IDI, found mainly in prokaryotes and , is a (FMN)-dependent that uses NADPH to generate a reduced flavin for stereospecific proton transfer through a carbocation-like pathway. This ensures a balanced pool of and DMAPP for efficient isoprenoid assembly.

Regulation

Transcriptional and translational control

The mevalonate pathway is primarily regulated at the transcriptional level through sterol regulatory element-binding proteins (SREBPs), which are membrane-bound transcription factors that sense cellular levels and control the expression of genes involved in and isoprenoid biosynthesis. When sterol levels are low, SREBP-2 is cleaved and translocated to the , where it binds to sterol regulatory elements (SREs) in the promoters of target genes, including (HMGCR), the rate-limiting enzyme of the pathway, thereby activating their transcription. This process is facilitated by the SREBP cleavage-activating protein (SCAP), which escorts SREBP from the (ER) to the Golgi for proteolytic processing; however, when sterols are abundant, the SCAP-Insig complex retains SREBP in the ER, preventing its activation and thus repressing transcription of pathway enzymes like HMGCR. Isoforms such as SREBP-1a, SREBP-1c, and SREBP-2 exhibit tissue-specific roles, with SREBP-2 predominantly regulating cholesterol synthesis genes in the liver and other tissues. Other nuclear receptors also modulate mevalonate pathway in response to lipid signals. The liver X receptor (LXR), activated by oxysterols derived from or pathway intermediates like desmosterol, promotes cholesterol efflux to maintain sterol ; oxysterols also inhibit SREBP processing by binding Insig and retaining SREBP in the , thereby indirectly repressing HMGCR and other SREBP-2 targets during high-oxysterol conditions. proliferator-activated receptors (PPARs), particularly PPARγ, are activated by mevalonate-derived intermediates such as (FPP), which binds directly to the receptor and enhances transcription of genes involved in lipid storage and metabolism, including those supporting and uptake. This activation promotes the expression of PPAR target genes like adipocyte protein 2 (aP2) and (LPL), linking mevalonate flux to broader lipid regulatory networks. At the translational level, HMGCR expression is fine-tuned by elements in its mRNA, particularly the complex (UTR), which forms secondary structures that inhibit ribosome scanning and reduce efficiency. Nonsterol isoprenoids, products of the mevalonate pathway, mediate this repression when their levels rise, ensuring control to prevent excess enzyme production; depletion of these isoprenoids, as occurs with inhibition, relieves translational suppression. While Rho require prenylation by mevalonate-derived for activation and contribute to cytoskeletal and signaling regulation, their role in directly modulating HMGCR remains linked through broader pathway rather than specific mechanistic activation. Studies have shown that increased acetylation at the HMGCR promoter enhances chromatin accessibility and , promoting mevalonate pathway upregulation to support tumor growth and survival in cancer cells; this modification is vulnerable to inhibitors targeting histone deacetylases, suggesting therapeutic potential. These insights underscore how epigenetic alterations integrate with transcriptional controls to dysregulate the pathway in disease states.

Post-translational mechanisms

Post-translational mechanisms in the mevalonate pathway primarily involve reversible modifications and protein degradation that rapidly adjust enzyme activity in response to cellular needs, such as sterol levels or energy status, without altering gene expression. These processes ensure tight control over isoprenoid biosynthesis, preventing overaccumulation of pathway intermediates. Key enzymes like 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR), mevalonate kinase (MVK), and phosphomevalonate kinase (PMK) are regulated through phosphorylation, ubiquitination, and allosteric inhibition. HMGR, the rate-limiting enzyme, undergoes primarily at serine residues by (AMPK), which inactivates the enzyme under conditions of low energy, such as high AMP/ATP ratios. This occurs at Ser-872 in the rat enzyme, reducing catalytic activity and thereby downregulating synthesis. Conversely, by protein phosphatase 2A (PP2A) activates HMGR, restoring its function when energy levels are sufficient. PP2A, a heterotrimeric complex, targets the phosphorylated sites to promote rapid reactivation, highlighting a dynamic balance in HMGR regulation. Another critical mechanism is the -induced ubiquitination and proteasomal of HMGR via the endoplasmic reticulum-associated (ERAD) pathway. When levels rise, HMGR binds to Insig proteins in the ER membrane, recruiting the E3 ubiquitin ligase gp78, which polyubiquitinates the enzyme's cytosolic domain. This marks HMGR for dislocation from the ER and subsequent degradation by the 26S , effectively reducing pathway . , an early intermediate, potently enhances this Insig-mediated ubiquitination, providing a loop sensitive to precursors. Downstream enzymes MVK and are subject to direct feedback inhibition by pathway end-products (FPP) and (GGPP), which bind allosterically to inhibit activity and prevent excessive isoprenoid buildup. In humans, FPP analogs like farnesyl thiodiphosphate competitively inhibit MVK by overlapping with the ATP-binding site, with inhibition constants in the nanomolar range. Similarly, GGPP inhibits both MVK and , modulating the phosphorylation steps to balance non-sterol isoprenoid production. Allosteric regulation also involves cofactor availability, particularly NADPH, which influences HMGR kinetics through sigmoidal response curves indicative of cooperative binding. Reduced NADPH levels shift HMGR to a less active, allosteric form, linking pathway activity to cellular redox state. In archaea, recent studies reveal redox-sensitive elements in the pathway, such as a [4Fe-4S] cluster in phosphomevalonate dehydratase from Aeropyrum pernix, enabling the enzyme to sense oxidative stress and adjust isoprenoid synthesis accordingly. This cluster's redox activity underscores evolutionary adaptations for environmental redox fluctuations in archaeal membranes.

Products and functions

Major isoprenoid products

The major isoprenoid products of the mevalonate pathway originate from the C5 units (IPP) and its (DMAPP), which condense head-to-tail to form longer prenyl intermediates that branch into diverse structural classes. Polyprenols represent extended polyisoprenoid chains, typically ranging from C80 to C100 units, assembled by cis-prenyltransferases through sequential additions of IPP to FPP or GGPP; exemplifies this class as a long-chain α-saturated polyprenol. Steroids emerge from the C30 intermediate , formed via the head-to-head condensation of two FPP molecules, which undergoes cyclization to and subsequent modifications yielding . Quinones such as (coenzyme Q10) incorporate a polyprenyl tail derived from FPP, extended by trans-prenyltransferase to form the 10-isoprene unit chain attached to a ring; menaquinones (forms of ) similarly feature isoprenoid tails built from mevalonate-derived prenyl units linked to a core.

Cellular and physiological roles

The mevalonate pathway produces isoprenoids that are indispensable for maintaining cellular structure, signaling, energy production, and physiological in eukaryotic cells. These molecules, including sterols, polyprenols, and prenyl groups, integrate into , facilitate protein modifications, and serve as cofactors in vital metabolic processes. In animals and fungi, the pathway's outputs primarily support membrane dynamics and , while in , they contribute to specialized functions like pigmentation and stress response, though the focus here remains on broader eukaryotic contexts. Cholesterol, a key derived from the mevalonate pathway, is essential for membrane integrity by modulating fluidity and enabling the formation of lipid rafts—specialized microdomains that organize signaling proteins and maintain membrane asymmetry. These rafts facilitate efficient cellular communication and , with cholesterol's rigid ring structure intercalating between phospholipids to prevent excessive fluidity at physiological temperatures. Additionally, dolichols, long-chain polyisoprenoids synthesized via the pathway, are enriched in the (ER) and Golgi membranes, where they act as anchors for assembly during N-linked protein , thereby supporting membrane stability and secretory pathway function. Protein prenylation, involving the attachment of farnesyl (15-carbon) or geranylgeranyl (20-carbon) groups from mevalonate-derived intermediates, is crucial for anchoring small like and Rho to cellular membranes, enabling their roles in , cytoskeletal dynamics, and vesicular trafficking. Farnesylation of proteins, for instance, targets them to the plasma membrane for activation in pathways, while geranylgeranylation of Rho regulates actin reorganization and . This ensures proper localization and activation of these proteins, which are pivotal for cellular and . In mitochondria, mevalonate pathway products support respiratory function: ubiquinone (coenzyme Q), an isoprenoid , shuttles electrons between complexes I/II and III in the (), facilitating ATP production and mitigating through its antioxidant properties. A, incorporating a farnesyl isoprenoid side chain from , serves as the prosthetic group in (complex IV), enabling the final reduction of oxygen to water and completing the . These contributions are vital for cellular and preventing accumulation. Cholesterol also functions as a precursor for biosynthesis in endocrine tissues, where it is converted to intermediates like for producing such as , which regulates stress responses and , and androgens like testosterone, essential for reproductive and muscle maintenance. Furthermore, from the pathway serves as the immediate precursor for synthesis upon UVB exposure, supporting calcium and immune function. These roles underscore the pathway's influence on organismal , linking to hormonal signaling.

Clinical aspects

Associated diseases

Mevalonate kinase deficiency (MKD) is an autosomal recessive autoinflammatory caused by biallelic pathogenic variants in the MVK , which encodes the enzyme mevalonate , leading to impaired isoprenoid biosynthesis and accumulation of mevalonic acid. This condition manifests as a spectrum of phenotypes, ranging from the milder hyper-IgD syndrome (HIDS), characterized by recurrent fevers, elevated serum IgD levels, and autoinflammatory episodes starting in infancy, to the severe mevalonic aciduria, which includes neurological impairment, developmental delay, dysmorphic features, and elevated urinary mevalonic acid. The deficiency disrupts protein and downstream isoprenoid production, triggering activation and release, such as interleukin-1β. Smith-Lemli-Opitz syndrome (SLOS) arises from mutations in the DHCR7 gene, encoding 7-dehydrocholesterol reductase, an enzyme in the post-squalene segment of the mevalonate pathway that catalyzes the final step in biosynthesis. This defect results in reduced levels and accumulation of the precursor , contributing to a multiple malformation syndrome with congenital anomalies, , and behavioral issues. The shortage impairs hedgehog signaling and membrane integrity, exacerbating developmental malformations, while elevated may exert toxic effects on neural tissues. Familial hypercholesterolemia (FH) involves defects in the low-density lipoprotein receptor (LDLR), indirectly dysregulating the mevalonate pathway by reducing cellular uptake and triggering compensatory upregulation of (HMGCR) and other pathway enzymes to increase endogenous synthesis. This leads to elevated plasma LDL-cholesterol levels and premature , with the pathway's hyperactivity sustaining through enhanced production. Dysregulation of the mevalonate pathway is implicated in cancer progression, where tumors often exhibit upregulated HMGCR expression to fuel via increased isoprenoid intermediates essential for protein of oncogenes like . This enables membrane localization and signaling of small , promoting and survival in various malignancies, including ovarian and pancreatic cancers. Recent studies (2022–2025) have linked mevalonate pathway alterations to neurodegeneration, particularly , where impaired of proteins involved in amyloid-beta processing contributes to plaque formation and synaptic dysfunction. More recent 2025 studies further implicate dysregulation in biosynthesis and protein in AD , including impaired ApoE and TDP-43 . Inhibition of the pathway reduces amyloid-beta production by disrupting , suggesting a role in neuroinflammatory cascades underlying cognitive decline.

Pharmacological interventions

Statins are competitive inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), the rate-limiting in the mevalonate pathway, which blocks the conversion of to mevalonate and thereby reduces downstream synthesis. Examples include , the first approved in 1987, and , a widely used synthetic analog that potently lowers levels by up to 50% in clinical use. By depleting mevalonate pathway intermediates, statins prevent through reduction and exhibit pleiotropic effects, such as anti-inflammatory actions via inhibition of isoprenoid-dependent protein . Nitrogen-containing bisphosphonates, such as alendronate, act as inhibitors of synthase (FPPS), a key enzyme in the mevalonate pathway that converts isopentenyl pyrophosphate and into . This inhibition disrupts geranylgeranylation of small like Rho and , impairing osteoclast function and , which forms the basis for their use in treating . In , bisphosphonates like zoledronate are applied to manage bone metastases in cancers such as and , where they reduce skeletal-related events by blocking tumor-induced osteolysis through the same prenylation-dependent mechanisms. Other inhibitors target additional steps in the pathway. Lapaquistat acetate, a synthase inhibitor, was developed to block the conversion of to presqualene diphosphate, aiming to lower without affecting upstream isoprenoids; however, phase III trials revealed concerns, leading to its discontinuation in 2008. Bempedoic acid inhibits ATP-citrate lyase (ACL), an enzyme upstream of HMGCR that provides for mevalonate synthesis, offering a alternative that activates primarily in the liver via ACSVL1-mediated conversion to its CoA form. Therapeutic monitoring of mevalonate pathway modulators includes attention to statin-induced , which arises from depletion of (GGPP) and subsequent impairment of Rho prenylation, leading to atrophy and weakness in susceptible patients. Proprotein convertase subtilisin/kexin type 9 () inhibitors, such as , indirectly influence pathway flux by enhancing low-density lipoprotein receptor recycling and increasing hepatic uptake, which upregulates HMGCR expression but reduces overall circulating levels without directly inhibiting mevalonate synthesis. In mevalonate kinase deficiency (MKD), an autoinflammatory disorder caused by pathway enzyme defects, the phase III CLUSTER trial demonstrated efficacy of the interleukin-1 (IL-1) blocker to mitigate from accumulated mevalonate intermediates, with 35% of MKD patients achieving complete response at week 16. Long-term data from trial extensions and real-world studies up to 2024 support its sustained efficacy and safety.

Alternative pathways

Non-mevalonate (MEP/DXP) pathway

The , also known as the methylerythritol 4-phosphate () pathway or 1-deoxy-D-xylulose 5-phosphate (DXP) pathway, represents an alternative route for the of the universal isoprenoid precursors isopentenyl diphosphate () and dimethylallyl diphosphate (DMAPP), distinct from the classical mevalonate-dependent pathway. Unlike the mevalonate pathway, it does not involve the intermediate mevalonate and instead utilizes carbohydrate-derived precursors from central metabolism. This pathway is essential for producing isoprenoids such as , , and prenyl groups in organisms where it operates. The pathway commences with the condensation of and pyruvate to form 1-deoxy-D-xylulose 5-phosphate (DXP), catalyzed by the DXP (DXS). This is followed by the reduction and isomerization of DXP to 2C-methyl-D-erythritol 4-phosphate (), mediated by DXP reductoisomerase (DXR or IspC), which requires NADPH and Mg²⁺ as cofactors. Subsequent transformations proceed through a series of five dedicated : cytidylyltransferase (IspD), which attaches a cytidylyl group to ; 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol (IspE), which phosphorylates the hydroxyl group; 2C-methyl-D-erythritol 2,4-cyclodiphosphate (IspF), a unique cyclase that forms a cyclic ; (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (IspG), an iron-sulfur cluster that generates the key (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP); and finally, HMBPP reductase (IspH), which reduces HMBPP to and DMAPP in the presence of . These steps highlight the pathway's mechanistic novelty, including metal-dependent rearrangements and radical-based reductions not found in the mevalonate route. Notable inhibitors target early enzymes, such as fosmidomycin, a from species that specifically inhibits DXR by acting as an analog of its substrate DXP, thereby disrupting isoprenoid production and serving as a lead for antibacterial and antimalarial agents. The pathway is absent in animals, which rely solely on the mevalonate pathway, but it predominates in the plastids of plants, , most eubacteria (including ), and apicomplexan parasites like , the causative agent of . This distribution underscores its potential as a selective therapeutic target, as inhibiting MEP enzymes affects pathogens without impacting human cells.

Evolutionary and organismal comparisons

The mevalonate (MVA) pathway is distributed across the of , fungi, and , where it serves as the primary route for , while the methylerythritol phosphate (MEP) pathway predominates in and the plastids of and algae. In higher , which possess both pathways, the MEP route operates within chloroplasts to support photosynthetic pigments and hormones, whereas the MVA pathway functions in the for and production; metabolic cross-talk between these compartments occurs through transporters that exchange intermediates like isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), enabling coordinated isoprenoid flux. This dual-pathway architecture in reflects an evolutionary for compartmentalized specialization, contrasting with the singular reliance on MVA in and fungi or MEP in most . Recent phylogenetic analyses suggest that the MVA pathway originated in the archaeal lineage after the Bacteria-Archaea divergence, while the MEP pathway emerged in the last bacterial common ancestor, indicating independent origins rather than presence in the (). In eukaryotes, gene duplications following endosymbiotic events—such as the acquisition of plastids from —facilitated the retention of both pathways in plants and , allowing for functional diversification. Recent phylogenomic studies (2021–2024) have uncovered evidence of (HGT) influencing pathway distribution, particularly in ; for instance, MEP pathway genes in plastid-bearing eukaryotes show contributions from both cyanobacterial ancestors and bacterial donors like Chlamydiae, suggesting HGT events that enhanced MEP functionality in algal lineages. Organismal variations highlight adaptive modifications of the MVA pathway. In , the pathway is altered to produce ether-linked lipids, which confer membrane stability in extreme environments; key enzymes, such as mevalonate diphosphate decarboxylase variants, direct toward glycerol-based backbones rather than linkages found in and eukaryotes. Conversely, certain pathogens like , which reside in apicomplexan parasites with plastid-derived organelles, depend exclusively on the pathway for isoprenoid precursors essential to their , making it a validated target for antimalarial antibiotics such as fosmidomycin that inhibit MEP enzymes without affecting MVA-dependent processes. These differences underscore the pathway's role in domain-specific lipid biochemistry and its exploitation for selective therapeutic interventions.

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