Enzymes that catalyze decarboxylations. Medical search. Frequent questions

Pyruvate catalytic reaction catalyzed by pyruvate dehydrogenase system is a special decarboxylation method, namely oxidative decarboxylation, which is different from the common decarboxylation reaction, namely common decarboxylation. (wikipedia.org)
The oxidative decarboxylation reaction is catalyzed by pyruvate dehydrogenase system, which includes three different enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase (E3), six cofactors: thiamine pyrophosphate (TPP), lipoamide, coenzyme A (CoA), flavin adenine dinucleotide (FAD), magnesium ion, and one co-substrate: nicotinamide adenine dinucleotide (NAD+). (wikipedia.org)
At this time, the compound is acetyl dihydrolipoamide, which is then catalyzed by E2, and acetyl is transferred, to form acetyl CoA, all the above reactions only involve decarboxylation reaction, and do not involve the movement of H, while the real dehydrogenation effect of pyruvate dehydrogenase system will be reflected in the next step of reaction. (wikipedia.org)
For simple decarboxylation reaction, the enzyme involved in this reaction is pyruvate decarboxylase, which is different from oxidative decarboxylation. (wikipedia.org)
In fermentative organisms, pyruvate is non-oxidatively decarboxylated by the TPP-dependent enzyme pyruvate decarboxylase. (wikipedia.org)
As part of the PDH complex, TPP assists in oxidative decarboxylation of pyruvate. (wikipedia.org)
The enzymes catalyze decarboxylation of pyruvate and of ketoglutarate and the transketolation reaction in the pentose phosphate pathway. (medscape.com)
The α-subunits of the oxaloacetate and methylmalonyl-CoA decarboxylases are homologous to many biotin-containing enzymes including (1) pyruvate carboxylases, (2) homocitrate synthases, (3) biotin carboxyl carrier proteins, (4) isopropylmalate synthases and (5) acyl-CoA carboxylase. (tcdb.org)
Since both pyruvate and phosphoenolpyruvate(PEP) are three-carbon compounds, pyruvate must be carboxylated to a four-carbon compound, oxaloacetate (OAA), before such a decarboxylation can happen. (ufp.pt)
The enzyme responsible for pyruvate carboxylation (pyruvate carboxylase) is present inside the mithocondrial matrix, and contains biotin, a CO 2 -activating cofactor. (ufp.pt)
Pyruvate decarboxylase: It is an enzyme that catalyzes the decarboxylation of pyruvic acid to carbon dioxide and acetaldehyde. (blfilm.com)

Carbidopa, an inhibitor of aromatic amino acid decarboxylation, is a white, crystalline compound, slightly soluble in water, with a molecular weight of 244.3. (rxlist.com)
Stalevo, a combination drug consisting of levodopa (aromatic amino acid), carbidopa (aromatic amino acid decarboxylation inhibitor), and entacapone (catechol-O-methyltransferase (COMT) inhibitor) is indicated for the treatment of Parkinson's disease. (nih.gov)

To sum up, in the oxidative decarboxylation reaction, there is both an oxidation reaction and a decarboxylation. (wikipedia.org)
The intermediate product in this oxidative decarboxylation reaction is oxalosuccinate, whose formation is coupled with the production of NADH + H + . While still bound to the enzyme, oxalosuccinate loses CO2 to produce alpha-ketoglutarate. (encyclopedia.com)

In Rhizobium species, a PEPCK-deficient mutant fails to grow on minimal medium with succinate or other citric acid cycle intermediates but can grow on glucose and glycerol as a sole carbon source, suggesting that PEPCK functions here as a key gluconeogenic enzyme ( 30 ). (asm.org)
In order to overcome this thermodynamic barrier, the reaction will be coupled to a decarboxylation , a strategy often used by the cell to displace an equilibrium towards the formation of products, as it will also be observed in several reactions in the citric acid cycle . (ufp.pt)

Distinct enzymes catalyze decarboxylation of (1) oxaloacetate, (2) methylmalonyl-CoA, (3) glutaconyl-CoA and (4) malonate. (tcdb.org)
Phosphoenolpyruvate carboxykinase (PEPCK) catalyzes the decarboxylation and phosphorylation of oxaloacetate (OAA) to form phosphoenolpyruvate (PEP) in most organisms. (asm.org)
The enzyme catalyzes the oxidative decarboxylation of (S)-malate in CC the presence of NADP(+) and divalent metal ions, and decarboxylation CC of oxaloacetate, cf. (expasy.org)
Oxaloacetate decarboxylation releases the energy needed to enable C2 phosphorylation by GTP, yielding phosphoenolpyruvate (in a reaction catalyzed bynuma phosphoenolpyruvate carboxykinase - PEPCK). (ufp.pt)

histamine is produced exclusively by decarboxylation of histidine by histidine decarboxylase (HDC) and is catabolized by histamine N‐methyltransferase (HNMT) or by diamine oxidase 1 (DAO1). (medicinman.cz)
4-bromo-3-hydroxybenzoic acid is a potent inhibitor of the enzyme histidine decarboxylase. (targetmol.com)
Cell type-specific deletion of the Hdc gene, which encodes HDC (histidine decarboxylase), an enzyme essential for histamine synthesis, would shed light on the role of histamine synthesis and secretion by the minor histamine-producing cells. (healthjade.com)

An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity . (wikipedia.org)
enzyme (E) accelerates conversion of substrates (S) to products (P). Bottom: by binding to the enzyme, inhibitor (I) blocks binding of substrate. (wikipedia.org)
An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's catalysis of the reaction is blocked. (wikipedia.org)
Medicinal enzyme inhibitors often have low dissociation constants , meaning that only a minute amount of the inhibitor is required to inhibit the enzyme. (wikipedia.org)
A low concentration of the enzyme inhibitor reduces the risk for liver and kidney damage and other adverse drug reactions in humans. (wikipedia.org)
Mass spectral analysis of the enzyme-inhibitor complex confirms covalent attachment of the inhibitor to ODCase accompanied by the loss of two protons and the iodo moiety. (nih.gov)

Let us define a carboxylation reaction as the addition of a CO2 unit to a substrate molecule, and decarboxylation as loss of CO2. (wikipedia.org)
Enzymes are proteins that speed up chemical reactions necessary for life , in which substrate molecules are converted into products . (wikipedia.org)
[1] An enzyme facilitates a specific chemical reaction by binding the substrate to its active site , a specialized area on the enzyme that accelerates the most difficult step of the reaction . (wikipedia.org)
Reversible inhibitors produce different types of inhibition depending on whether they bind to the enzyme, the enzyme-substrate complex, or both. (wikipedia.org)
The binding site of inhibitors on enzymes is most commonly the same site that binds the substrate of the enzyme. (wikipedia.org)
Of note, the choice of RPs not only affect the substrate conversion rate but also the type and selectivity of reactions catalyzed by P450s 7 . (nature.com)
We propose that the specificity of XXT3, XXT4, and XXT5 is directed toward the prior synthesis of the acceptor substrate by the other two enzymes, XXT1 and XXT2. (bvsalud.org)
Thus, the broad range of metabolized substrates and the unprecedented variability of the chemical reactions catalyzed by cytochromes P450 can be attributed largely to the differences in substrate binding properties of different isozymes. (schoolbag.info)
Most reactions are catalyzed with narrow substrate specificity, and they afford products with high regioselectivity and stereoselectivity. (schoolbag.info)
Some enzymes may also bind simultaneously two or three substrate molecules, same or different, and various cases of the resulting activation or inhibition of the product turnover were documented both in vivo and in vitro (4, 7). (schoolbag.info)

The enzyme responsible for collagen maturation is prolyl 4-hydroxylase, making this enzyme a central activity in cuticle biosynthesis and a potentially important chemotherapeutic target. (embl.de)
Also, it requires well-coordinated expression of all genes encoding the enzymes that catalyze the biosynthesis pathway for the required cannabinoid and enzyme engineering to use specific starter molecules. (fortunahemp.com)
Nicotianamine synthase (NAS) catalyzes the biosynthesis of the low-molecular-mass metal chelator nicotianamine (NA) from the 2-aminobutyrate moieties of three SAM molecules. (bvsalud.org)
Although most xyloglucans (XyGs) biosynthesis enzymes have been identified, the molecular mechanism that defines XyG branching patterns is unclear. (bvsalud.org)
These heme enzymes are found in most organisms from all biological kingdoms and catalyze various oxidative chemical transformations important for the biosynthesis of steroid hormones, vitamins, signaling molecules, and many other compounds, as well as for the metabolism of xenobiotics. (schoolbag.info)

The main limiting factor is the efficiency, speed and quantity of the enzymes that build psilocybin and its genetics that codes for the proteins that build the enzymes that builds the magic. (shroomery.org)
Enzyme inhibitors are a chemically diverse set of substances that range in size from organic small molecules to macromolecular proteins . (wikipedia.org)
In addition to small molecules, some proteins act as enzyme inhibitors. (wikipedia.org)
Cytochrome P450 enzymes (P450s or CYPs) are a superfamily of heme-thiolate proteins widespread in all kingdoms of life 1 . (nature.com)
Studies in this area led to the identification of multiple bioluminescent proteins and enzyme systems, some of which have found direct applications in biological research (2). (neb.com)
Using a newly developed enzyme-coupled continuous activity assay, we compare differing NAS proteins identified through multiple sequence alignments and phylogenetic analyses. (bvsalud.org)
IDH proteins are homodimeric enzymes involved in diverse cellular processes, including adaptation to hypoxia, histone demethylation and DNA modification. (elsevierpure.com)
Both IDH2 and IDH1 (localized in the cytoplasm) proteins catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). (elsevierpure.com)

During the reaction, E1 participates in the decarboxylation of pyruvic acid, and then TPP connects the acetyl group after the reaction. (wikipedia.org)

Pyridoxal phosphate promotes decarboxylation of amino acids. (wikipedia.org)
GLuc is a monomeric enzyme of only 185 amino acids (19 kD), and is the smallest known luciferase. (neb.com)
These enzymes catalyze the decarboxylation of amino acids, beta-keto acids and alpha-keto acids. (targetmol.com)

We also consider the broader context of common carboxylation and decarboxylation reactions in biochemistry. (wikipedia.org)
The most prominent carboxylation reactions in biochemistry are catalyzed by biotin-dependent carboxylases and RuBisCO. (wikipedia.org)
It functions as a CO2 carrier in carboxylation and decarboxylation reactions catalyzed by a small family of enzymes, the biotin carboxylases. (pberghei.eu)

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme. (pberghei.eu)

In gluconeogenesis, the reactions catalyzed by phosphofructokinase and hexokinase are replaced by hydrolytic reactions. (ufp.pt)
Despite the unprecedented variability of chemical reactions catalyzed by cytochromes P450, all the important features of their mechanism can be attributed to the oxidative transformations driven by the main catalytic intermediate, which is a ferryl-oxo heme complex with the porphyrin pi-cation radical, or Compound I (3, 4, 8). (schoolbag.info)
Nonclassic reactions catalyzed by some cytochromes P450, which do not use oxygen, and thus deviate from the main P450 mechanism, include direct reductive processes driven by the heme iron (conversion of nitric oxide to nitrous oxide by CYP55, reductive dehalogenation, reduction of azo compounds and quinines, etc. (schoolbag.info)

O 2 using the decarboxylation of alpha-ketoglutarate as an electron donor. (wikipedia.org)
The next step is the oxidative decarboxylation of succinyl CoA from alpha-ketoglutarate. (encyclopedia.com)

Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO 2 ). (wikipedia.org)
This is conceptually the same as the more general term "decarboxylation" as defined above except that it specifically requires that the carboxyl group is, as expected, replaced by a hydrogen. (wikipedia.org)

The enzyme was purified 300‐fold to homogeneity, judged from the analysis of N‐terminal amino acid sequence, and found to be a monomeric enzyme of apparent 24 kDa. (elsevierpure.com)

Most are accompanied by α- Ketoglutarate α- Decarboxylation caused by dehydrogenation of hydroxyl carboxylic acids such as carbonyl carboxylic acid, malic acid, isocitric acid, etc. (wikipedia.org)
Usually, decarboxylation refers to a reaction of carboxylic acids , removing a carbon atom from a carbon chain. (wikipedia.org)
In ketonic decarboxylation a carboxylic acid is converted to a ketone. (wikipedia.org)

The active site of the dimeric enzyme lies at the interface between the two monomers. (tcdb.org)
HinfPDH is a dimeric enzyme, with each monomer consisting of an N-terminal α/β dinucleotide-binding domain and a C-terminal α-helical dimerization domain. (rcsb.org)

Decarboxylation reaction reactions are typically quite thermodynamically favorable due to the entropic contribution of cleaving a single molecule into two, one of which is a gas. (wikipedia.org)
Small molecule inhibitors include essential primary metabolites that inhibit upstream enzymes that produce those metabolites. (wikipedia.org)
[3] [2] Small molecule enzyme inhibitors also include secondary metabolites , which are not essential to the organism that produces them, but provide the organism with an evolutionary advantage, in that they can be used to repel predators or competing organisms or immobilize prey. (wikipedia.org)
Cytochromes P450 monooxygenases represent a large superfamily of heme enzymes, which require a dioxygen molecule and two electrons supplied by a NAD(P)H-dependent protein redox partner to form catalytically active high-valent ferryl-oxo intermediate. (schoolbag.info)
Cytochromes P450 represent a superfamily of heme enzymes with a common fold and mechanism that requires an atmospheric dioxygen molecule, two electrons from NAD(P)H, and one or two protons available from solvent water to form an active catalytic ferryl-oxo intermediate (1). (schoolbag.info)

Following the formation of isocitrate there are four oxidation-reduction reactions, the first of which, the oxidative decarboxylation of isocitrate, is catalyzed by isocitrate dehydrogenase. (encyclopedia.com)
1993). The next and irreversible part of BCAA catabolism is certainly catalyzed with the mitochondrial branched string -keto acidity dehydrogenase (BCKDC) enzyme complicated (Harris et al. (woofahs.com)
Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate. (cancer-research-network.com)
CH3COCOO− + H+ → CH3CHO + CO. This reaction is catalyzed by alcohol dehydrogenase (ADH1 in baker's yeast). (blfilm.com)
We found that the tricarboxylic acid cycle-associated enzyme α-ketoglutarate (α-KG) dehydrogenase (KGDH) entered the nucleus, where it interacted with various JMJs to regulate α-KG-dependent histone demethylations by JMJs, and thus controlled genome-wide gene expression in plants. (bvsalud.org)

Enzyme inhibitors may bind reversibly or irreversibly. (wikipedia.org)
Both BCAT enzymes reversibly transfer the -amino band of a BCAA for an amino group acceptor, -ketoglutarate generally. (woofahs.com)
It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. (doctorinternet.com)

These enzymes confer resistance to β-lactam antibiotics on bacteria that produce them. (cdc.gov)
PEPCKs have been generally classified according to their nucleotide specificities: enzymes from bacteria, yeast, and plants mainly use adenosine nucleotides, but enzymes from a variety of eukaryotes and mammals use guanosine or inosine phosphates ( 24 ). (asm.org)

The C-terminal domain of UMPS is orotidine-5'-monophosphate decarboxylase (OMPD), a cofactor-less yet extremely efficient enzyme. (rcsb.org)
Orotidine 5'-monophosphate decarboxylase (ODCase) has evolved to catalyze the decarboxylation of orotidine 5'-monophosphate without any covalent intermediates. (nih.gov)
It is formed via the decarboxylation of L-glutamate catalyzed by the enzyme, glutamic acid decarboxylase(GAD). (sigmaaldrich.com)
A novel decarboxylase which catalyzes an enantioselective decarboxylation of α‐aryl‐α‐methylmalonates to α‐arylpropionates has been purified from a soil bacterium Alcaligenes bronchisepticus KU 1201. (elsevierpure.com)
The decarboxylase is not a biotin containing enzyme because avidin have no influence on the enzyme activity. (elsevierpure.com)
Thus, the enzyme was tentatively named as arylmalonate decarboxylase. (elsevierpure.com)

In Escherichia coli , besides the PEPCK reaction, there is another pathway to form PEP from C 4 -dicarboxylic acid which involves the NAD- and NADP-dependent malic enzymes (MAEA and MAEB) and phosphoenolpyruvate synthase (PPS). (asm.org)
AN malic enzyme. (expasy.org)

The pckA gene, encoding the gluconeogenic enzyme phosphoenolpyruvate carboxykinase (PEPCK), was cloned by PCR amplification from the purple nonsulfur bacterium Rhodopseudomonas palustris No. 7. (asm.org)

HIV-1 protease), pyridoxal phosphate-catalyzed alpha decarboxylation, and acetolactate synthase. (umass.edu)

TPP is the key catalytic cofactor used by enzymes catalyzing non-oxidative and oxidative decarboxylation of α-keto acids. (wikipedia.org)
Thiamine mainly functions as thiamine pyrophosphate (TPP), which serves as a prosthetic group or cofactor for 3 enzymes essential to carbohydrate metabolism. (medscape.com)
Insect luciferases, including Photinus pyralis (firefly), catalyze the oxidation of a benzothiazol luciferin requiring ATP as a cofactor. (neb.com)
b) Name the cofactor(s) required by each enzyme reaction. (solvedlib.com)

The enzyme aconitase catalyzes both steps, since the intermediate is cis -aconitate. (encyclopedia.com)

With respect to their functional roles in living organisms, cytochromes P450 can be separated tentatively into the enzymes essential for biosynthetic pathways and the xenobiotic metabolizing enzymes (1). (schoolbag.info)

UMP synthase (UMPS) catalyzes the last two steps of de novo pyrimidine nucleotide synthesis and is a potential cancer drug target. (rcsb.org)
This creates a proton gradient that drives the synthesis of ATP by an enzyme called ATP synthase. (stemcelldaily.com)

Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. (novusbio.com)

[7] A special case of protein enzyme inhibitors are zymogens that contain an autoinhibitory N-terminal peptide that binds to the active site of enzyme that intramolecularly blocks its activity as a protective mechanism against uncontrolled catalysis. (wikipedia.org)
The enzyme transfers CO 2 from glutaconyl-CoA to a biotin carrier protein (the γ-subunit) that is subsequently decarboxylated by the carboxybiotin decarboxylation site within the Na + pumping beta subunit (Gcdβ). (tcdb.org)
Excessive Ca 2 + entry through glutamate receptors activates a large array of potential neurotoxic mechanisms, which include activation of enzymes such as phospholipases, calpains and other proteases, protein kinases, nitric oxide synthetase, endonucleases, as well as reactive oxygen species (for review, see Sattler and Tymianski, 2000 ). (jneurosci.org)
These enzymes, together with the four G‐protein‐coupled receptors H1R‐H4R, are ubiquitous in the CNS and mediate histaminergic signalling. (medicinman.cz)
Quantitative assessment of metabolite concentrations enables decoupling from genetic or environmental perturbations that may not affect gene transcription and/or protein translation, but may for example affect enzyme activity levels that could lead to correspondingly more or less metabolite. (biomedcentral.com)
MS = An 11-subunit enzyme complex that acts as an electron transferring protein in the mitochondrial respiratory chain. (doctorinternet.com)

How a single vitamin deficiency can have such diverse patterns of presentation is not fully understood, but genetic differences in the 3 enzymes that use thiamine are likely to play a large role. (medscape.com)

Studies of OMPDs from micro-organisms led to the proposal of several noncovalent decarboxylation mechanisms via high-energy intermediates. (rcsb.org)
Plasticity of catalytic residues and a covalent OMPD-UMP complex prompt a reevaluation of the prevailing decarboxylation mechanism in favor of covalent intermediates. (rcsb.org)
Some primary carbon metabolism-related enzymes were up-regulated by JA to provide sufficient metabolism intermediates and energy for tuber development. (biomedcentral.com)
Each step involves different enzymes and substrates, and produces different products and intermediates. (stemcelldaily.com)
Each step is a complex multistep enzymatic reaction process that involves different substrates, intermediates, products, enzymes, and coenzymes. (stemcelldaily.com)

a) Write a balanced equation for the reaction catalyzed by each enzyme. (solvedlib.com)

Decarboxylation in metabolism can be either non-oxidative or oxidative. (wikipedia.org)
MS = A necessary enzyme in the metabolism of galactose. (doctorinternet.com)

We also offer solutions for automation, site-directed mutagenesis, as well as your favorite restriction enzyme, ligase or competent cell products. (neb.com)

Regardless of how biotin is acquired, a dedicated ATP-dependent biotin ligase, or holocarboxylase synthetase (HCS), is required to catalyze the covalent attachment of biotin to a specific lysine in the target carboxylase. (pberghei.eu)

[2] Enzyme inhibitors also control essential enzymes such as proteases or nucleases that, if left unchecked, may damage a cell. (wikipedia.org)

Most reactions performed by cytochromes P450 can be catalyzed effectively by Compound I, which is formally the same high-valent intermediate in all isozymes (5, 6). (schoolbag.info)

Decarboxylation of aryl carboxylates can generate the equivalent of the corresponding aryl anion, which in turn can undergo cross coupling reactions . (wikipedia.org)
Comparing the relative activities, it is clear that the enzyme prefers α‐arylmalonates to α‐aryl‐α‐methylmalonates. (elsevierpure.com)

Hence the discovery and refinement of enzyme inhibitors is an active area of research in biochemistry and pharmacology . (wikipedia.org)

By contrast, reversible inhibitors bind non-covalently and may spontaneously leave the enzyme, allowing the enzyme to resume its function. (wikipedia.org)
2004). The first step in the catabolism from the BCAAs is certainly reversible transamination catalyzed with the branched string aminotransferase (BCAT) isozymes. (woofahs.com)
An enzyme that catalyzes the reversible reaction of α-d-glucose 1-phosphate UDPgalactose to produce UDPglucose and α-d-galactose 1-phosphate. (theodora.com)

These coenzymes are subsequently oxidized in the electron transport chain, where a series of enzymes transfers the electrons of NADH and FADH2 to oxygen, which is the final electron acceptor of cellular respiration in all eukaryotes. (encyclopedia.com)

Psilocin is a bit different as it it's not in the synthesis but from exposure of psilocybin to PsiK a dephosphorelating enzyme. (shroomery.org)

The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. (thermofisher.com)

These subunits catalyze different steps of the overall reaction. (wikipedia.org)

Phenethylamine can be biosynthesized from the amino acid phenylalanine by enzymatic decarboxylation. (hmdb.ca)

1990). BCKDC catalyzes oxidative decarboxylation from the BCKA items from the BCAT response, forming NADH as well as the particular branched-chain acyl CoA derivative of every BCAA. (woofahs.com)
Complejo enzimático que cataliza la DESCARBOXILACIÓN oxidativa y la DESAMINACIÓN de la GLICINA en DIÓXIDO DE CARBONO, AMONÍACO, NADH y N5N10-metilenotetrahidrofolato. (bvsalud.org)

These enzymes all use thiamine's thiazole ring to activate and transfer a 2-carbon unit (aldehyde), which provides precursors for other synthetic pathways and also provides energy for the cell. (medscape.com)
Strains deficient in all three enzymes cannot grow on C 4 -dicarboxylic acids as a sole carbon source, whereas strains retaining one of these enzymes are still able to grow ( 14 ). (asm.org)

Thus, depending on the organism, PEPCK may have different physiological roles as a gluconeogenic or an anaplerotic enzyme. (asm.org)

Irreversible inhibitors form a chemical bond with the enzyme such that the enzyme is inhibited until the chemical bond is broken. (wikipedia.org)
Enzyme inhibitors play an important role in all cells, since they are generally specific to one enzyme each and serve to control that enzyme's activity. (wikipedia.org)
Many poisons produced by animals or plants are enzyme inhibitors that block the activity of crucial enzymes in prey or predators . (wikipedia.org)
Many drug molecules are enzyme inhibitors that inhibit an aberrant human enzyme or an enzyme critical for the survival of a pathogen such as a virus , bacterium or parasite . (wikipedia.org)
Since anti-pathogen inhibitors generally target only one enzyme, such drugs are highly specific and generally produce few side effects in humans, provided that no analogous enzyme is found in humans. (wikipedia.org)
In vitro production of enzymatically active O. volvulus prolyl 4-hydroxylase should facilitate identification of specific inhibitors of the parasite enzyme. (embl.de)

They are often classified according to the cofactors that catalyze the transformations. (wikipedia.org)

Deficiency in this enzyme is the major cause of GALACTOSEMIA. (doctorinternet.com)
a deficiency or defect in this enzyme results in two forms of mucolipidoses, I-cell disease, and pseudo-Hurler polydystrophy. (theodora.com)
a deficiency of this enzyme is associated with one type of galactosemia. (theodora.com)

It is a multi-step, enzyme-catalyzed process that helps modify simple compounds into more complex compounds. (fortunahemp.com)
The enzyme complex catalyzes the oxidation of ubiquinol to ubiquinone and ferrocytochrome c in the presence of ferricytochrome c. (doctorinternet.com)

For example, enzymes in a metabolic pathway may be inhibited by molecules produced later in the pathway, thus curtailing the production of molecules that are no longer needed. (wikipedia.org)
It is generally assumed that unless they are genetically aberrant, normal cells are equipped with common metabolic machinery (i.e., transporters and enzymes) to cope with the changing nutritional environment. (wiley.com)

When this happens, one of the ways by which DNA is repaired is by base excision repair mechanism as initiated by the enzyme N-methylpurine glycosylase . (biologyonline.com)

Anatomy1

Organisms5

Diseases2

Chemicals and Drugs73

Analytical, Diagnostic and Therapeutic Techniques and Equipment1

Phenomena and Processes10

Technology, Industry, Agriculture1

Information Science1

Pyruvate11

Aromatic amino acid decarbox2

Oxidative decarboxylation reaction2

Citric acid2

Oxaloacetate4

Histidine decarboxylase3

Inhibitor6

Substrate10

Biosynthesis5

Proteins8

Pyruvic acid1

Amino acids3

Carboxylation3

Biotin-dependent1

Reactions catalyzed3

Alpha-ketoglutarate2

Carboxyl group2

Monomeric enzyme1

Carboxylic3

Dimeric enzyme2

Molecule5

Dehydrogenase5

Reversibly3

Bacteria2

Decarboxylase6

Malic2

Phosphoenolpyruvate carboxykinase1

Pyridoxal1

Cofactor4

Aconitase1

Biosynthetic1

Synthase2

Dehydrogenases1

Protein6

Thiamine1

Intermediates5

Reaction catalyzed1

Metabolism2

Site-directed mu1

Covalent attachment1

Proteases1

Compound1

Aryl2

Biochemistry1

Reversible3

Coenzymes1

Synthesis1

Hydroxylation1

Subunits1

Enzymatic1

NADH2

Carbon2

PEPCK1

Inhibitors6

Transformations1

Deficiency3

Complex2

Metabolic2

Mechanism1