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Literature summary for 1.2.5.3 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
Search for more literature for 1.2.5.3

Cloned(Commentary)

Cloned (Comment) Organism
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

Metals/Ions Comment Organism Structure
Molybdenum
-
 Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12600
-
 LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE Aeropyrum pernix
34500
-
 LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE Aeropyrum pernix
163700
-
 gel filtration Aeropyrum pernix
168100
-
 about, sequence calculation Aeropyrum pernix

Organism

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

Purification (Commentary)

Purification (Comment) Organism
native enzyme 13fold to homogeneity by ultracentrifugation, anion exchange chromatography, ultrafiltration, hydroxyapatite chromatography, again ultrafiltration, and gel filtration Aeropyrum pernix

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.96
-
 purified native enzyme, pH 8.0, 95°C, using 1 mM methyl blue as electron acceptor Aeropyrum pernix
2.1
-
 purified native enzyme, pH 8.0, 95°C, using 1 mM methyl viologen as electron acceptor Aeropyrum pernix
2.45
-
 purified native enzyme, pH 8.0, 95°C, using 1 mM NADP+ as electron acceptor Aeropyrum pernix
2.47
-
 purified ative enzyme, pH 8.0, 95°C, using 1 mM NAD+ as electron acceptor Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO + methyl viologen + H2O methyl viologen as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix CO2 + reduced methylene blue
-
 ?
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
-
 ?
CO + methylene blue + H2O methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix CO2 + NAD+
-
 ?
CO + methylene blue + H2O methyl blue as an electron acceptor and saturated carbon monoxide as an electron donor Aeropyrum pernix TB5 CO2 + NAD+
-
 ?
CO + NADH + H+ + H2O
-
 Aeropyrum pernix CO2 + NADP+
-
 ?
CO + NADH + H+ + H2O
-
 Aeropyrum pernix TB5 CO2 + NADP+
-
 ?
CO + NADPH + H+ + H2O
-
 Aeropyrum pernix CO2 + reduced methyl viologen
-
 ?
CO + NADPH + H+ + H2O
-
 Aeropyrum pernix TB5 CO2 + reduced methyl viologen
-
 ?

Subunits

Subunits Comment Organism
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
oligomer LM2S structure, 1 x 86700, large subunit L, + 1 * 34500, medium subunit M, + 1 * 12600, small subunit S, SDS-PAGE Aeropyrum pernix

Synonyms

Synonyms Comment Organism
Mo-CODH
-
 Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
-
 Aeropyrum pernix

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
methyl viologen
-
 Aeropyrum pernix
methylene blue
-
 Aeropyrum pernix
molybdopterin cofactor
-
 Aeropyrum pernix
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
NAD+
-
 Aeropyrum pernix
NADP+
-
 Aeropyrum pernix

General Information

General Information Comment Organism
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
metabolism carbon monoxide dehydrogenase (CODH) is a key enzyme of carbon monoxide metabolism in carboxydotrophic bacteria, it catalyzes carbon monoxide oxidation Aeropyrum pernix