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Literature summary extracted from

  • Nishimura, H.; Nomura, Y.; Iwata, E.; Sato, N.; Sako, Y.
    Purification and characterization of carbon monoxide dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix (2010), Fish. Sci., 76, 999-1006.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.5.3 genes coxS, coxM, and coxL, DNA and amino acid sequence determination and analysis, sequence comparisons with Aeropyrum pernix strain K1, phylogenetic analysis Aeropyrum pernix

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.3 Molybdenum
-
 Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.5.3 12600
-
 LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE Aeropyrum pernix
1.2.5.3 34500
-
 LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE Aeropyrum pernix
1.2.5.3 163700
-
 gel filtration Aeropyrum pernix
1.2.5.3 168100
-
 about, sequence calculation Aeropyrum pernix
1.2.7.4 12600
-
 1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE Aeropyrum pernix
1.2.7.4 34500
-
 1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE Aeropyrum pernix
1.2.7.4 86600
-
 1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE Aeropyrum pernix
1.2.7.4 163700
-
 calculated from amino acid sequence Aeropyrum pernix
1.2.7.4 210000
-
 gel filtration Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.3 Aeropyrum pernix B8YAC9 and B8YAC8 and B8YAD0 small, medium, and large subunit
-
1.2.5.3 Aeropyrum pernix TB5 B8YAC9 and B8YAC8 and B8YAD0 small, medium, and large subunit
-
1.2.7.4 Aeropyrum pernix
-
-
-
1.2.7.4 Aeropyrum pernix TB5
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.2.7.4 100% of activity remains after 48 h of oxygen exposure, and after 168 h of air exposure, activity is 88% of the initial activity Aeropyrum pernix

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.5.3 native enzyme 13fold to homogeneity by ultracentrifugation, anion exchange chromatography, ultrafiltration, hydroxyapatite chromatography, again ultrafiltration, and gel filtration Aeropyrum pernix
1.2.7.4 Q-Sepharose column chromatography, CHT-I column chromatography, and Superdex 200 gel filtration Aeropyrum pernix

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.5.3 0.96
-
 purified native enzyme, pH 8.0, 95°C, using 1 mM methyl blue as electron acceptor Aeropyrum pernix
1.2.5.3 2.1
-
 purified native enzyme, pH 8.0, 95°C, using 1 mM methyl viologen as electron acceptor Aeropyrum pernix
1.2.5.3 2.45
-
 purified native enzyme, pH 8.0, 95°C, using 1 mM NADP+ as electron acceptor Aeropyrum pernix
1.2.5.3 2.47
-
 purified ative enzyme, pH 8.0, 95°C, using 1 mM NAD+ as electron acceptor Aeropyrum pernix
1.2.7.4 0.96
-
 after 12.92fold purification, at 95°C, pH 8.0, using methylene blue as electron acceptor Aeropyrum pernix
1.2.7.4 2.08
-
 after 12.92fold purification, at 95°C, pH 8.0, using methyl viologen as electron acceptor Aeropyrum pernix
1.2.7.4 2.45
-
 after 12.92fold purification, at 95°C, pH 8.0, using NADP+ as electron acceptor Aeropyrum pernix
1.2.7.4 2.47
-
 after 12.92fold purification, at 95°C, pH 8.0, using NAD+ as electron acceptor Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.3 CO + methyl viologen + H2O methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix CO2 + reduced methylene blue
-
 ?
1.2.5.3 CO + methyl viologen + H2O methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix TB5 CO2 + reduced methylene blue
-
 ?
1.2.5.3 CO + methylene blue + H2O methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix CO2 + NAD+
-
 ?
1.2.5.3 CO + methylene blue + H2O methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix TB5 CO2 + NAD+
-
 ?
1.2.5.3 CO + NADH + H+ + H2O
-
 Aeropyrum pernix CO2 + NADP+
-
 ?
1.2.5.3 CO + NADH + H+ + H2O
-
 Aeropyrum pernix TB5 CO2 + NADP+
-
 ?
1.2.5.3 CO + NADPH + H+ + H2O
-
 Aeropyrum pernix CO2 + reduced methyl viologen
-
 ?
1.2.5.3 CO + NADPH + H+ + H2O
-
 Aeropyrum pernix TB5 CO2 + reduced methyl viologen
-
 ?
1.2.7.4 CO + H2O + methyl viologen
-
 Aeropyrum pernix CO2 + reduced methyl viologen + H+
-
 ?
1.2.7.4 CO + H2O + methyl viologen
-
 Aeropyrum pernix TB5 CO2 + reduced methyl viologen + H+
-
 ?
1.2.7.4 CO + H2O + NAD+ the specific activity is increased by approximately 20% with NAD+ as the electron acceptor compared to methyl viologen Aeropyrum pernix CO2 + NADH + H+
-
 ?
1.2.7.4 CO + H2O + NAD+ the specific activity is increased by approximately 20% with NAD+ as the electron acceptor compared to methyl viologen Aeropyrum pernix TB5 CO2 + NADH + H+
-
 ?
1.2.7.4 CO + H2O + NADP+ the specific activity is increased by approximately 20% with NADP+ as the electron acceptor compared to methyl viologen Aeropyrum pernix CO2 + NADPH + H+
-
 ?
1.2.7.4 CO + H2O + NADP+ the specific activity is increased by approximately 20% with NADP+ as the electron acceptor compared to methyl viologen Aeropyrum pernix TB5 CO2 + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.5.3 More Mo-CODH is composed of a heterotrimer, each heterotrimer has a molybdopterin (L-subunit) that contains the molybdopterin-cytosine dinucleotide (MCD)-type of molybdenum cofactor, a flavoprotein (M-subunit) that contains the flavin adenine dinucleotide (FAD) cofactor, and an iron-sulfur protein (S-subunit) carrying type I and II [2Fe-2S] clusters Aeropyrum pernix
1.2.5.3 oligomer LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE Aeropyrum pernix
1.2.7.4 heterotetramer 1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
1.2.5.3 Mo-CODH
-
 Aeropyrum pernix
1.2.7.4 CODH
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.5.3 95
-
-
 Aeropyrum pernix
1.2.7.4 95
-
-
 Aeropyrum pernix

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.7.4 75 100 about 65% activity at 75°C, about 75% activity at 80°C, about 80% activity at 85°C, about 90% activity at 90°C, 100% activity at 95°C, about 30% activity at 100°C, respectively Aeropyrum pernix

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.5.3 75
-
 purifed enzyme, pH 8.0, 10 min, 65% of optimal activity remains Aeropyrum pernix
1.2.5.3 100
-
 purifed enzyme, pH 8.0, 10 min, 30% of optimal activity remains Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.5.3 8
-
 assay at Aeropyrum pernix

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.3 methyl viologen
-
 Aeropyrum pernix
1.2.5.3 methylene blue
-
 Aeropyrum pernix
1.2.5.3 molybdopterin cofactor
-
 Aeropyrum pernix
1.2.5.3 additional information CODH shows carbon monoxide oxidation activity with all tested electron acceptors, including methyl viologen, NAD+, NADP+, and methylene blue. Specific activity is increased by about 20% when NAD+ and NADP+ are used as electron acceptors, compared with methyl viologen, and by about 50% when methylene blue is used Aeropyrum pernix
1.2.5.3 NAD+
-
 Aeropyrum pernix
1.2.5.3 NADP+
-
 Aeropyrum pernix

General Information

EC Number General Information Comment Organism
1.2.5.3 evolution CODH enzymes are classified into two groups, Ni-CODH and Mo-CODH, based on the type of metal in the active center. The Ni-CODH active center is constructed from nickel, iron, and sulfur clusters. Ni-CODH is distributed among anaerobic carboxydotrophs. The Mo-CODH active center contains molybdenum. Aerobic carboxydotrophs use Mo-CODH. The CODH protein isolated from Aeropyrum pernix is a distinct type of archaeal Mo-CODH. Phylogenetic analysis, overview Aeropyrum pernix
1.2.5.3 metabolism carbon monoxide dehydrogenase (CODH) is a key enzyme of carbon monoxide metabolism in carboxydotrophic bacteria, it catalyzes carbon monoxide oxidation Aeropyrum pernix