1.2.5.3: aerobic carbon monoxide dehydrogenase
This is an abbreviated version!
For detailed information about aerobic carbon monoxide dehydrogenase, go to the full flat file.
Reaction
Synonyms
aerobic Mo/Cu-containing CO dehydrogenase, Carbon monoxide dehydrogenase, CO dehydrogenase, CODH, CoxS, coxSML, CutL, CutM, CutS, EC 1.2.2.4, EC 1.2.3.10, Mo-CODH, Mo-Cu carbon monoxide dehydrogenase, Mo/Cu CODH, MoCu-CODH, molybdenum- and copper-containing carbon monoxide dehydrogenase, molybdenum- and copper-dependent CO dehydrogenase, molybdenum-containing carbon monoxide dehydrogenase, molybdenum-containing CO dehydrogenase, molybdenum-copper carbon monoxide dehydrogenase, molybdenum-copper CO dehydrogenase, molybdenum/copper-containing carbon monoxide dehydrogenase, molybdoenzyme carbon monoxide dehydrogenase
ECTree
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Engineering
Engineering on EC 1.2.5.3 - aerobic carbon monoxide dehydrogenase
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additional information
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metal cluster composition, structure and function of CO dehydrogenase synthesized in mutants of Oligotropha carboxidovorans strain OM5 in which the genes coxE, coxF and coxG are disrupted by insertional mutagenesis, recombinant expression in Escherichia coli strain S17-1, overview. Mutants in coxG retain the ability to utilize CO, although at a lower growth rate. They contain a regular CO dehydrogenase with a functional catalytic site. The CoxD protein is a distinct AAA+ ATPase. CoxD operates in the maturation of the CO dehydrogenase bimetallic cluster, particularly in the sulfuration of the [MoO3]-site and in ATP-dependent chaperone function. Disruption of coxD leads to a phenotype of D-km which is impaired in the utilization of CO, whereas the utilization of H2 plus CO2 is not affected. Under appropriate induction conditions, bacteria synthesize a fully assembled apo-CO dehydrogenase, which cannot oxidize CO. Apo-CO dehydrogenase contained a [MoO3] site in place of the [CuSMoO2] clusters. The genes coxE and coxF are both obligatory for the utilization of CO as a growth substrate
additional information
the flavoprotein can be removed from CO dehydrogenase by dissociation with sodium dodecylsulfate, the resulting M(LS)2- or (LS)2-structured CO dehydrogenase species can be reconstituted with the recombinant apoflavoprotein produced in Escherichia coli. Binding of FAD to the reconstituted deflavo (LMS)2 species occurs with second-order kinetics and high affinity. Same fold and binding of the flavoprotein as in wild-type CO dehydrogenase, whereas the S-selanylcysteine 388 in the active-site loop on the molybdoprotein is disordered. The structural changes related to heterotrimeric complex formation or FAD binding are transmitted to the iron-sulfur protein, structural and functional analysis of FAD binding in CO dehydrogenase
additional information
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the flavoprotein can be removed from CO dehydrogenase by dissociation with sodium dodecylsulfate, the resulting M(LS)2- or (LS)2-structured CO dehydrogenase species can be reconstituted with the recombinant apoflavoprotein produced in Escherichia coli. Binding of FAD to the reconstituted deflavo (LMS)2 species occurs with second-order kinetics and high affinity. Same fold and binding of the flavoprotein as in wild-type CO dehydrogenase, whereas the S-selanylcysteine 388 in the active-site loop on the molybdoprotein is disordered. The structural changes related to heterotrimeric complex formation or FAD binding are transmitted to the iron-sulfur protein, structural and functional analysis of FAD binding in CO dehydrogenase
additional information
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the flavoprotein can be removed from CO dehydrogenase by dissociation with sodium dodecylsulfate, the resulting M(LS)2- or (LS)2-structured CO dehydrogenase species can be reconstituted with the recombinant apoflavoprotein produced in Escherichia coli. Binding of FAD to the reconstituted deflavo (LMS)2 species occurs with second-order kinetics and high affinity. Same fold and binding of the flavoprotein as in wild-type CO dehydrogenase, whereas the S-selanylcysteine 388 in the active-site loop on the molybdoprotein is disordered. The structural changes related to heterotrimeric complex formation or FAD binding are transmitted to the iron-sulfur protein, structural and functional analysis of FAD binding in CO dehydrogenase
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