Introduction to Enzymes - Protocatechuate 4,5-dioxygenase of Enzymes

Protocatechuate 4,5-dioxygenase of enzymes

In enzymology, a protocatechuate 4,5-dioxygenase (EC 1.13.11.8) is an enzyme that catalyzes the chemical reaction

protocatechuate O2 displaystyle rightleftharpoons 4-carboxy-2-hydroxymuconate semialdehydeThus, the two substrates of this enzyme are protocatechuate and O2, whereas its product is 4-carboxy-2-hydroxymuconate semialdehyde.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is protocatechuate:oxygen 4,5-oxidoreductase (decyclizing). Other names in common use include protocatechuate 4,5-oxygenase, protocatechuic 4,5-dioxygenase, and protocatechuic 4,5-oxygenase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron.

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Methylenetetrahydrofolate dehydrogenase (NADP) of enzymes

In enzymology, a methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydrofolate NADP displaystyle rightleftharpoons 5,10-methenyltetrahydrofolate NADPH HThus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NADP, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADPH, and H.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NADP oxidoreductase. Other names in common use include N5,N10-methylenetetrahydrofolate dehydrogenase, 5,10-methylenetetrahydrofolate:NADP oxidoreductase, 5,10-methylenetetrahydrofolate dehydrogenase, methylenetetrahydrofolate dehydrogenase, and methylenetetrahydrofolate dehydrogenase (NADP). This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.

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Pyruvate dehydrogenase (cytochrome) of enzymes

In enzymology, a pyruvate dehydrogenase (cytochrome) (EC 1.2.2.2) is an enzyme that catalyzes the chemical reaction

pyruvate ferricytochrome b1 H2O displaystyle rightleftharpoons acetate CO2 ferrocytochrome b1The 3 substrates of this enzyme are pyruvate, ferricytochrome b1, and H2O, whereas its 3 products are acetate, CO2, and ferrocytochrome b1.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and pyruvate oxidase (ambiguous). This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

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Mannose-6-phosphate 6-reductase of enzymes

In enzymology, a mannose-6-phosphate 6-reductase (EC 1.1.1.224) is an enzyme that catalyzes the chemical reaction

D-mannitol 1-phosphate NADP displaystyle rightleftharpoons D-mannose 6-phosphate NADPH HThus, the two substrates of this enzyme are D-mannitol 1-phosphate and NADP, whereas its 3 products are D-mannose 6-phosphate, NADPH, and H.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is D-mannitol-1-phosphate:NADP 6-oxidoreductase. Other names in common use include NADPH-dependent mannose 6-phosphate reductase, mannose-6-phosphate reductase, 6-phosphomannose reductase, NADP-dependent mannose-6-P:mannitol-1-P oxidoreductase, NADPH-dependent M6P reductase, and NADPH-mannose-6-P reductase.

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Glycerol-3-phosphate oxidase of enzymes

In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction

sn-glycerol 3-phosphate O2 displaystyle rightleftharpoons glycerone phosphate H2O2Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:oxygen 2-oxidoreductase. Other names in common use include glycerol phosphate oxidase, glycerol-1-phosphate oxidase, glycerol phosphate oxidase, L-alpha-glycerophosphate oxidase, alpha-glycerophosphate oxidase, and L-alpha-glycerol-3-phosphate oxidase. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD.

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ALG6 (enzyme class) of enzymes

Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase (EC 2.4.1.267, ALG6, Dol-P-Glc:Man9GlcNAc2-PP-Dol alpha-1,3-glucosyltransferase) is an enzyme with systematic name dolichyl beta-D-glucosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-glucosyltransferase.

This enzyme catalyses the following chemical reaction

which is:

dolichyl beta-D-glucosyl phosphate D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->6)-D-Man-alpha-(1->6)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol displaystyle rightleftharpoons D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->6)-D-Man-alpha-(1->6)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol dolichyl phosphate

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Isoflavone 3'-hydroxylase of enzymes

In enzymology, an isoflavone 3'-hydroxylase (EC 1.14.13.52) is an enzyme that catalyzes the chemical reaction

formononetin NADPH H O2 displaystyle rightleftharpoons calycosin NADP H2OThe 4 substrates of this enzyme are formononetin, NADPH, H, and O2, whereas its 3 products are calycosin, NADP, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is formononetin,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called isoflavone 3'-monooxygenase. This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.

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Names of enzymes

It is marketed under many brand names worldwide, including:

Xiva, An Li Nuo Er, An Sai Ma, Ansimar, Asima, Bestofyline, Chuan Ning, D-Fyal, Dilatair, Doxiba, Doxobid, Doxobron, Doxofilina, Doxofillina, Doxofyllin, Doxoll, Doxophylline, Doxovent, Doxyjohn, Fei Te Ai Si, Jian Fang Neng, Lang Ming, Lv Meng, Mai Ping Xi, Maxivent, Mucosma, Na De Lai, Phylex, Phyllin, Puroxan, Rexipin, Shu Zhi, Shuai An, Shuweixin, Suo Di, Suo Ji, Suo Li An, Xi Si Nuo, Xin Qian Ping, Xin Xi Ping, Yi Suo, and Yili.

It is also marketed as a combination drug with terbutaline as Doxoll-TL, Mucosma-T and Phylex-TR.

It is also marketed as a combination drug with montelukast as Doxoll-ML, Doxomont, Doxoril-M, Doxovent-M, Lunair-M, and Venidox-M.

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UDP-N-acetylglucosaminedolichyl-phosphate N-acetylglucosaminephosphotransferase of enzymes

In enzymology, an UDP-N-acetylglucosaminedolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) is an enzyme that catalyzes the chemical reaction

UDP-N-acetyl-D-glucosamine dolichyl phosphate displaystyle rightleftharpoons UMP N-acetyl-D-glucosaminyl-diphosphodolicholThus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and dolichyl phosphate, whereas its two products are UMP and N-acetyl-D-glucosaminyl-diphosphodolichol.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase. Other names in common use include UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase, UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase, UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase, uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase, chitobiosylpyrophosphoryldolichol synthase, dolichol phosphate N-acetylglucosamine-1-phosphotransferase, UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase, and UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase. This enzyme participates in the biosynthesis of N-glycan and glycan structures.

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Coenzyme F420 hydrogenase of enzymes

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

H2 coenzyme F420 displaystyle rightleftharpoons reduced coenzyme F420Thus, the two substrates of this enzyme are H2 and coenzyme F420, whereas its product is reduced coenzyme F420.

This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with other, known, acceptors. The systematic name of this enzyme class is hydrogen:coenzyme F420 oxidoreductase. Other names in common use include 8-hydroxy-5-deazaflavin-reducing hydrogenase, F420-reducing hydrogenase, and coenzyme F420-dependent hydrogenase. This enzyme participates in folate biosynthesis and is a critical part of energy conservation in some methanogens such as Methanosarcina barkeri. It has 3 cofactors: iron, nickel, and deazaflavin.

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-alpha,7-alpha-dihydroxy-5-beta-cholestanateCoA ligase of enzymes

In enzymology, a 3alpha,7alpha-dihydroxy-5beta-cholestanate-CoA ligase (EC 6.2.1.28) is an enzyme that catalyzes the chemical reaction

ATP (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate CoA displaystyle rightleftharpoons AMP diphosphate (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoAThe 3 substrates of this enzyme are ATP, (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate, and CoA, whereas its 3 products are AMP, diphosphate, and (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA.

This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate:CoA ligase (AMP-forming). Other names in common use include 3alpha,7alpha-dihydroxy-5beta-cholestanoyl coenzyme A synthetase, DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid biosynthesis.

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Methylmalonyl-CoA carboxytransferase of enzymes

In enzymology, a methylmalonyl-CoA carboxytransferase (EC 2.1.3.1) is an enzyme that catalyzes the chemical reaction

(S)-methylmalonyl-CoA pyruvate displaystyle rightleftharpoons propanoyl-CoA oxaloacetateThus, the two substrates of this enzyme are (S)-methylmalonyl-CoA and pyruvate, whereas its two products are propanoyl-CoA and oxaloacetate.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is (S)-methylmalonyl-CoA:pyruvate carboxytransferase. Other names in common use include transcarboxylase, methylmalonyl coenzyme A carboxyltransferase, methylmalonyl-CoA transcarboxylase, oxalacetic transcarboxylase, methylmalonyl-CoA carboxyltransferase, methylmalonyl-CoA carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase, and carboxytransferase incorrect. This enzyme participates in propanoate metabolism. It has 3 cofactors: zinc, Biotin, and Cobalt.

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S9 fraction of enzymes

The S9 fraction is the product of an organ tissue homogenate used in biological assays. The S9 fraction is most frequently used in assays that measure the metabolism of drugs and other xenobiotics. It is defined by the U.S. National Library of Medicine's "IUPAC Glossary of Terms Used in Toxicology" as the "Supernatant fraction obtained from an organ (usually liver) homogenate by centrifuging at 9000 g for 20 minutes in a suitable medium; this fraction contains cytosol and microsomes.

" The microsomes component of the S9 fraction contain cytochrome P450 isoforms (phase I metabolism) and other enzyme activities. The cytosolic portion contains the major part of the activities of transferases (phase II metabolism). The S9 fraction is easier to prepare than purified microsomes.

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Amiflamine of enzymes

Amiflamine (FLA-336) is a reversible inhibitor of monoamine oxidase A (MAO-A), thereby being a RIMA, and, to a lesser extent, semicarbazide-sensitive amine oxidase (SSAO), as well as a serotonin releasing agent (SRA). It is a derivative of the phenethylamine and amphetamine chemical classes. The ()-enantiomer is the active stereoisomer.

Amiflamine shows preference for inhibiting MAO-A in serotonergic relative to noradrenergic and dopaminergic neurons. In other words, at low doses, it can be used to selectively inhibit MAO-A enzymes in serotonin cells, whereas at higher doses it loses its selectivity. This property is attributed to amiflamine's higher affinity for the serotonin transporter over the norepinephrine and dopamine transporters, as transporter-mediated carriage is required for amiflamine to enter monoaminergic neurons.

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Pathophysiology of enzymes

Fumarase deficiency is caused by a mutation in the fumarate hydratase (FH) gene in humans, which encodes the enzyme that converts fumarate to malate in the mitochondria. Other mutant alleles of the FH gene, located on human Chromosome 1 at position 1q42.1, cause multiple cutaneous and uterine leiomyomata, hereditary leiomyomatosis and renal cell cancer. Fumarase deficiency is one of the few known deficiencies of the Krebs cycle or tricarboxylic acid cycle, the main enzymatic pathway of cellular aerobic respiration.

The condition is an autosomal recessive disorder, and it is therefore usually necessary for an affected individual to receive the mutant allele from both parents. A number of children diagnosed with the disorder have been born to parents who were first cousins. It can also be associated with uniparental isodisomy.

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Flavone synthase of enzymes

In enzymology, a flavone synthase (EC 1.14.11.22) is an enzyme that catalyzes the chemical reaction

a flavanone 2-oxoglutarate O2 displaystyle rightleftharpoons a flavone succinate CO2 H2OThe 3 substrates of this enzyme are flavanone, 2-oxoglutarate, and O2, whereas its 4 products are flavone, succinate, CO2, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating). This enzyme participates in flavonoid biosynthesis and isoflavonoid biosynthesis.

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Neddylation process of enzymes

NEDD8 links itself to a protein through an isopeptide linkage between its carboxy-terminal glycine and the lysine of the substrate.

The neddylation of the substrate causes in a structural change, and there are three main biochemical effects that result. First, neddylation can cause a conformational change in the substrate which may restrict molecular movement and the positioning of different binding partners. Second, it can cause the target protein to become incompatible with other proteins that it usually binds with. For example, CAND1 does not bind to neddylated proteins. In addition, neddylation can recruit NEDD8-interacting proteins. When NEDD8 binds to the ubiquitin E2 Ubc4, the interaction stimulates cullin-based ubiquitin ligases, although the exact mechanism is unclear.

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