Nutrition Guide

In enzymology, a stizolobinate synthase (EC 1.13.11.30) is an enzyme that catalyzes the chemical reaction
3,4-dihydroxy-L-phenylalanine + O2 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde

Thus, the two substrates of this enzyme are 3,4-dihydroxy-L-phenylalanine and O2, whereas its product is 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-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 3,4-dihydroxy-L-phenylalanine:oxygen 2,3-oxidoreductase (recyclizing). This enzyme participates in tyrosine metabolism. It employs one cofactor, zinc.

In enzymology, a stizolobate synthase (EC 1.13.11.29) is an enzyme that catalyzes the chemical reaction
3,4-dihydroxy-L-phenylalanine + O2 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde

Thus, the two substrates of this enzyme are 3,4-dihydroxy-L-phenylalanine and O2, whereas its product is 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-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 3,4-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase (recyclizing). This enzyme participates in tyrosine metabolism. It employs one cofactor, zinc.

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1EI6.

In enzymology, a phosphonoacetate hydrolase (EC 3.11.1.2) is an enzyme that catalyzes the chemical reaction
phosphonoacetate + H2O acetate + phosphate

Thus, the two substrates of this enzyme are phosphonoacetate and H2O, whereas its two products are acetate and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is phosphonoacetate phosphonohydrolase. This enzyme participates in aminophosphonate metabolism. It employs one cofactor, zinc.

In enzymology, a N-acyl-D-glutamate deacylase (EC 3.5.1.82) is an enzyme that catalyzes the chemical reaction
N-acyl-D-glutamate + H2O a carboxylate + D-glutamate

Thus, the two substrates of this enzyme are N-acyl-D-glutamate and H2O, whereas its two products are carboxylate and D-glutamate.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-glutamate amidohydrolase. It employs one cofactor, zinc.

In enzymology, a N-acyl-D-aspartate deacylase (EC 3.5.1.83) is an enzyme that catalyzes the chemical reaction
N-acyl-D-aspartate + H2O a carboxylate + D-aspartate

Thus, the two substrates of this enzyme are N-acyl-D-aspartate and H2O, whereas its two products are carboxylate and D-aspartate.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-aspartate amidohydrolase. It employs one cofactor, zinc.

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1M7J, 1RJP, 1RJQ, 1RJR, 1RK5, 1RK6, 1V4Y, and 1V51.

In enzymology, a N-acyl-D-amino-acid deacylase (EC 3.5.1.81) is an enzyme that catalyzes the chemical reaction
N-acyl-D-amino acid + H2O an acid + D-amino acid

Thus, the two substrates of this enzyme are N-acyl-D-amino acid and H2O, whereas its two products are acid and D-amino acid.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-amino acid amidohydrolase. It employs one cofactor, zinc.

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1DCZ, 1DD2, 1ON3, 1ON9, 1RQB, 1RQE, 1RQH, 1RR2, 1S3H, 1U5J, 2D5D, and 2EVB.

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

Thus, 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.