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Literature summary extracted from

  • Zhang, B.; Hemann, C.F.; Hille, R.
    Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans (2010), J. Biol. Chem., 285, 12571-12578.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.5.3 additional information
-
 additional information rapid reaction kinetics, steady-state kinetics Afipia carboxidovorans
1.2.5.3 0.0107
-
 CO pH 7.2, 25°C Afipia carboxidovorans
1.2.7.4 0.0107
-
 methylene blue at pH 7.2 and 25°C Afipia carboxidovorans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.3 Cu essential for enzyme activity, 1.69 Cu per mol of enzyme dimer Afipia carboxidovorans
1.2.5.3 Fe2+ 8.05 Fe per mol of enzyme dimer, in the Fe-S cluster Afipia carboxidovorans
1.2.5.3 Mo3+ essential for enzyme activity, 1.82 Mo per mol of enzyme dimer Afipia carboxidovorans
1.2.5.3 additional information metal contents are determined by inductively coupled plasma atomic emission spectrometry Afipia carboxidovorans
1.2.5.3 Se
-
 Afipia carboxidovorans
1.2.7.4 copper contains copper, essential for activity Afipia carboxidovorans
1.2.7.4 Molybdenum contains molybdenum, essential for activity Afipia carboxidovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.5.3 CO + a quinone + H2O Afipia carboxidovorans
-
 CO2 + a quinol
-
 ?
1.2.7.4 CO + H2O + acceptor Afipia carboxidovorans
-
 CO2 + reduced acceptor + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.3 Afipia carboxidovorans
-
-
-
1.2.7.4 Afipia carboxidovorans P19919 and P19920 and P19921 P19919 large subunit, P19920 medium subunit, P19921 small subunit
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.7.4 Q-Sepharose column chromatography and Sephacryl S-300 gel filtration Afipia carboxidovorans

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.5.3 CO + a quinone + H2O = CO2 + a quinol CO initially binds rapidly to the enzyme, possibly at the Cu(I) of the active site, prior to undergoing oxidation. A Mo(V) species exhibits strong coupling to the copper of the active center, the rate-limiting step of overall turnover is likely in the reductive half-reaction Afipia carboxidovorans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.3 CO + a quinone + H2O
-
 Afipia carboxidovorans CO2 + a quinol
-
 ?
1.2.5.3 CO + a quinone + H2O the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+ Afipia carboxidovorans CO2 + a quinol
-
 ?
1.2.7.4 CO + H2O + acceptor
-
 Afipia carboxidovorans CO2 + reduced acceptor + H+
-
 ?
1.2.7.4 CO + H2O + methylene blue
-
 Afipia carboxidovorans CO2 + reduced methylene blue
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.5.3 CO dehydrogenase
-
 Afipia carboxidovorans
1.2.5.3 CODH
-
 Afipia carboxidovorans
1.2.5.3 molybdenum-copper CO dehydrogenase
-
 Afipia carboxidovorans
1.2.7.4 CO dehydrogenase
-
 Afipia carboxidovorans
1.2.7.4 CODH
-
 Afipia carboxidovorans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.5.3 25
-
 assay at Afipia carboxidovorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.5.3 51.1
-
 CO pH 7.2, 25°C, reductive half-reaction of enzyme CODH with CO Afipia carboxidovorans
1.2.5.3 93.3
-
 CO pH 7.2, 25°C Afipia carboxidovorans
1.2.7.4 57.8
-
 methylene blue at pH 7.2 and 25°C Afipia carboxidovorans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.5.3 7.2
-
-
 Afipia carboxidovorans
1.2.7.4 7.2
-
-
 Afipia carboxidovorans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.5.3 5.5 10 only modest loss of activity at these extreme pHs indicates that ionization of functional groups in the active site is not as critical to catalysis for CODH Afipia carboxidovorans
1.2.7.4 5 10
-
 Afipia carboxidovorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.3 FAD
-
 Afipia carboxidovorans
1.2.5.3 additional information presence of FAD, Fe/S clusters, and a [CuSMoO2] coordination in the active site determined by Raman spectra Afipia carboxidovorans
1.2.5.3 [CuSMoO2] cofactor
-
 Afipia carboxidovorans
1.2.7.4 FAD
-
 Afipia carboxidovorans
1.2.7.4 Fe-S center
-
 Afipia carboxidovorans

General Information

EC Number General Information Comment Organism
1.2.5.3 physiological function Oligotropha carboxidovorans is a carboxydotrophic bacterium capable of aerobic, chemolithoautotrophic growth using COas a sole source of carbon and energy. The key enzyme involved in this facultative metabolism is an air-stable molybdenum-containing CO dehydrogenase that catalyzes the oxidation of CO to CO2 Afipia carboxidovorans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.7.4 8700
-
 methylene blue at pH 7.2 and 25°C Afipia carboxidovorans