EC Explorer

[browse EC tree] - [search]

EC 4.1.1.118 Details

show Brenda entry

EC number

4.1.1.118

Accepted name

isophthalyl-CoA decarboxylase

Reaction

isophthalyl-CoA = benzoyl-CoA + CO₂

Other name(s)

IPCD

Systematic name

isophthalyl-CoA carboxy-lyase

Comment

The enzyme, characterized from the bacterium Syntrophorhabdus aromaticivorans, participates in an anaerobic isophthalate degradation pathway. The enzyme requires a prenylated flavin mononucleotide cofactor.

History

created 2019

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.2 With a cytochrome as acceptor

1.1.3 With oxygen as acceptor

1.1.4 With a disulfide as acceptor

1.1.5 With a quinone or similar compound as acceptor

1.1.7 With an iron-sulfur protein as acceptor

1.1.9 With a copper protein as acceptor

1.1.98 With other, known, physiological acceptors

1.1.99 With unknown physiological acceptors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.2 With a cytochrome as acceptor

1.8.3 With oxygen as acceptor

1.8.4 With a disulfide as acceptor

1.8.4.1 glutathione—homocystine transhydrogenase

1.8.4.2 protein-disulfide reductase (glutathione)

1.8.4.3 glutathione—CoA-glutathione transhydrogenase

1.8.4.4 glutathione—cystine transhydrogenase

1.8.4.5 methionine-S-oxide reductase

1.8.4.6 protein-methionine-S-oxide reductase

1.8.4.7 enzyme-thiol transhydrogenase (glutathione-disulfide)

1.8.4.8 phosphoadenylyl-sulfate reductase (thioredoxin)

1.8.4.9 adenylyl-sulfate reductase (glutathione)

1.8.4.10 adenylyl-sulfate reductase (thioredoxin)

1.8.4.11 peptide-methionine (S)-S-oxide reductase

1.8.4.12 peptide-methionine (R)-S-oxide reductase

1.8.4.13 L-methionine (S)-S-oxide reductase

1.8.4.14 L-methionine (R)-S-oxide reductase

1.8.4.15 protein dithiol oxidoreductase (disulfide-forming)

1.8.4.16 thioredoxin:protein disulfide reductase

1.8.5 With a quinone or similar compound as acceptor

1.8.5.1 glutathione dehydrogenase (ascorbate)

1.8.5.2 thiosulfate dehydrogenase (quinone)

1.8.5.3 respiratory dimethylsulfoxide reductase

1.8.5.4 bacterial sulfide:quinone reductase

1.8.5.5 thiosulfate reductase (quinone)

1.8.5.6 sulfite dehydrogenase (quinone)

1.8.5.7 glutathionyl-hydroquinone reductase

1.8.5.8 eukaryotic sulfide quinone oxidoreductase

1.8.5.9 protein dithiol:quinone oxidoreductase DsbB

1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass)

1.8.7 With an iron-sulfur protein as acceptor

1.8.98 With other, known, physiological acceptors

1.8.99 With unknown physiological acceptors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)