Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.5.3 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
Search for more literature for 1.2.5.3

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information rapid reaction kinetics, steady-state kinetics Afipia carboxidovorans
0.0107
-
 CO pH 7.2, 25°C Afipia carboxidovorans

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CO + a quinone + H2O Afipia carboxidovorans
-
 CO2 + a quinol
-
 ?

Organism

Organism UniProt Comment Textmining
Afipia carboxidovorans
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Synonyms

Synonyms Comment Organism
CO dehydrogenase
-
 Afipia carboxidovorans
CODH
-
 Afipia carboxidovorans
molybdenum-copper CO dehydrogenase
-
 Afipia carboxidovorans

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
-
 Afipia carboxidovorans

pH Range

pH Minimum pH Maximum Comment Organism
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

Cofactor

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

General Information

General Information Comment Organism
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