Nutrition Guide

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1DZN, 1E0Y, and 1E8G.

In enzymology, a vanillyl-alcohol oxidase (EC 1.1.3.38) is an enzyme that catalyzes the chemical reaction
vanillyl alcohol + O2 vanillin + H2O2

Thus, the two substrates of this enzyme are vanillyl alcohol and O2, whereas its two products are vanillin 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 vanillyl alcohol:oxygen oxidoreductase. This enzyme is also called 4-hydroxy-2-methoxybenzyl alcohol oxidase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1HSK, 1MBB, 1MBT, 1UXY, 2GQT, 2GQU, 2MBR, and 2Q85.

In enzymology, an UDP-N-acetylmuramate dehydrogenase (EC 1.1.1.158) is an enzyme that catalyzes the chemical reaction
UDP-N-acetylmuramate + NADP+ UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+

Thus, the two substrates of this enzyme are UDP-N-acetylmuramate and NADP+, whereas its 3 products are UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine, 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 UDP-N-acetylmuramate:NADP+ oxidoreductase. Other names in common use include MurB reductase, UDP-N-acetylenolpyruvoylglucosamine reductase, UDP-N-acetylglucosamine-enoylpyruvate reductase, UDP-GlcNAc-enoylpyruvate reductase, uridine diphosphoacetylpyruvoylglucosamine reductase, uridine diphospho-N-acetylglucosamine-enolpyruvate reductase, uridine-5′-diphospho-N-acetyl-2-amino-2-deoxy-3-O-, and lactylglucose:NADP-oxidoreductase. This enzyme participates in aminosugars metabolism. It employs one cofactor, FAD.

In enzymology, a trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction
trypanothione + NADP+ trypanothione disulfide + NADPH + H+

Thus, the two substrates of this enzyme are trypanothione and NADP+, whereas its 3 products are trypanothione disulfide, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is trypanothione:NADP+ oxidoreductase. Other names in common use include trypanothione reductase, and NADPH2:trypanothione oxidoreductase. It employs one cofactor, FAD.

In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction
thiamine + 2 O2 + H2O thiamine acetic acid + 2 H2O2

The 3 substrates of this enzyme are thiamine, O2, and H2O, whereas its two products are thiamine acetic acid 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 thiamine:oxygen 5-oxidoreductase. Other names in common use include thiamin dehydrogenase, thiamine dehydrogenase, and thiamin:oxygen 5-oxidoreductase. This enzyme participates in thiamine metabolism. It employs one cofactor, FAD.

In enzymology, a taxifolin 8-monooxygenase (EC 1.14.13.19) is an enzyme that catalyzes the chemical reaction
taxifolin + NAD(P)H + H+ + O2 2,3-dihydrogossypetin + NAD(P)+ + H2O

The 5 substrates of this enzyme are taxifolin, NADH, NADPH, H+, and O2, whereas its 4 products are 2,3-dihydrogossypetin, NAD+, 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 taxifolin,NAD(P)H:oxygen oxidoreductase (8-hydroxylating). This enzyme is also called taxifolin hydroxylase. It has 2 cofactors: FAD, and Flavoprotein.

In enzymology, a tartronate-semialdehyde synthase (EC 4.1.1.47) is an enzyme that catalyzes the chemical reaction
2 glyoxylate tartronate semialdehyde + CO2

Hence, this enzyme has one substrate, glyoxylate, and two products, tartronate semialdehyde and CO2.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is glyoxylate carboxy-lyase (dimerizing tartronate-semialdehyde-forming). Other names in common use include tartronate semialdehyde carboxylase, glyoxylate carbo-ligase, glyoxylic carbo-ligase, hydroxymalonic semialdehyde carboxylase, tartronic semialdehyde carboxylase, glyoxalate carboligase, and glyoxylate carboxy-lyase (dimerizing). This enzyme participates in glyoxylate and dicarboxylate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

In enzymology, a steroid 9alpha-monooxygenase (EC 1.14.99.24) is an enzyme that catalyzes the chemical reaction
pregna-4,9(11)-diene-3,20-dione + AH2 + O2 9,11alpha-epoxypregn-4-ene-3,20-dione + A + H2O

The 3 substrates of this enzyme are pregna-4,9(11)-diene-3,20-dione, AH2, and O2, whereas its 3 products are 9,11alpha-epoxypregn-4-ene-3,20-dione, A, 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 derive from O miscellaneous. The systematic name of this enzyme class is steroid,hydrogen-donor:oxygen oxidoreductase (9-epoxidizing). This enzyme is also called steroid 9alpha-hydroxylase. It has 2 cofactors: FMN, and Iron-sulfur.

In enzymology, a salicylate 1-monooxygenase (EC 1.14.13.1) is an enzyme that catalyzes the chemical reaction
salicylate + NADH + 2 H+ + O2 catechol + NAD+ + H2O + CO2

The 4 substrates of this enzyme are salicylate, NADH, H+, and O2, whereas its 4 products are catechol, NAD+, H2O, and CO2.

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 salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating). Other names in common use include salicylate hydroxylase, salicylate 1-hydroxylase, salicylate monooxygenase, and salicylate hydroxylase (decarboxylating). This enzyme participates in 3 metabolic pathways: 1- and 2-methylnaphthalene degradation, naphthalene and anthracene degradation, and fluorene degradation. It employs one cofactor, FAD.