Table 1.
Enzyme commission numbers associated with carbon monoxide
| EC number | Functional classifications in KEGG | Name and description | Proposed functional classification |
|---|---|---|---|
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/2/2/4.html | Unknown | CO dehydrogenase (cytochrome b 561); although present in strict aerobes, O2 is not required for the reaction. CO is oxidized to CO2 with water as the oxidant 49 | Energy Metabolism; Carbon fixation pathways in prokaryotes |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/2/5/3.html | Unknown | Aerobic Carbon Monoxide dehydrogenase (quinone) | Energy Metabolism; Carbon fixation pathways in prokaryotes |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/2/7/4.html | Carbon fixation pathways in prokaryotes; Methane metabolism; Nitrotoluene degradation | Anaerobic carbon‐monoxide dehydrogenase (ferredoxin) | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC2/3/1/169.html | Carbon fixation pathways in prokaryotes | CO‐methylating acetyl‐CoA synthase | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC2/1/1/258.html | Carbon fixation pathways in prokaryotes | 5‐methyltetrahydrofolate:corrinoid/iron‐sulfur protein Co‐methyltransferase; two step reaction: Tetrahydrofolate + acetyl‐CoA ↔ 5‐methyltetrahydrofolate + CoA + CO | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/13/11/24.html | Unknown | Quercetin 2,3‐dioxygenase. CO is a byproduct in this reaction. | Xenobiotics biodegradation and metabolism |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/13/11/47.html | Unknown | 3‐hydroxy‐4‐oxoquinoline 2,4‐dioxygenase. CO is a byproduct in this reaction. | Xenobiotics biodegradation and metabolism |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/13/11/48.html | Unknown | 3‐hydroxy‐2‐methylquinolin‐4‐one 2,4‐dioxygenase. CO is a byproduct in this reaction. | Xenobiotics biodegradation and metabolism |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/13/11/53.html | Cysteine and methionine metabolism | Acireductone dioxygenase (Ni2+‐requiring). CO is a byproduct in this reaction. Unknown function; the same enzyme, when binding iron, is the one leading to the salvage of methionine (http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/13/11/54.html) 97, 98. | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/14/14/18.html | Porphyrin and chlorophyll metabolism | Heme oxygenase (biliverdin‐producing). CO is a byproduct in this reaction. | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/14/15/20.html | Porphyrin and chlorophyll metabolism | Heme oxygenase (biliverdin‐producing, ferredoxin). CO is a byproduct in this reaction. | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC4/1/99/5.html | Cutin, suberine and wax biosynthesis | Aldehyde oxygenase (deformylating) | |
| http://www.chem.qmul.ac.uk/iubmb/enzyme/EC4/1/99/17.html | Thiamine metabolism | Phosphomethylpyrimidine synthase. CO is a byproduct in this reaction. |