@article{
 title = {Structure and inhibition of orotidine 5′-monophosphate decarboxylase from Plasmodium falciparum},
 type = {article},
 year = {2008},
 pages = {3842-3854},
 volume = {47},
 id = {a141dd55-ab8c-3d60-ae66-5bb20bb77e87},
 created = {2023-01-10T01:45:40.465Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:45:40.465Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {Orotidine 5′-monophosphate (OMP) decarboxylase from Plasmodium falciparum (PfODCase, EC 4.1.1.23) has been overexpressed, purified, subjected to kinetic and biochemical analysis, and crystallized. The native enzyme is a homodimer with a subunit molecular mass of 38 kDa. The saturation curve for OMP as a substrate conformed to Michaelis-Menten kinetics with Km = 350 ± 60 nM and Vmax = 2.70 ± 0.10 μmol/min/mg protein. Inhibition patterns for nucleoside 5′-monophosphate analogues were linear competitive with respect to OMP with a decreasing potency of inhibition of PfODCase in the order: pyrazofurin 5′-monophosphate (Ki = 3.6 ± 0.7 nM) > xanthosine 5′-monophosphate (XMP, Ki = 4.4 ± 0.7 nM) > 6-azauridine 5′-monophosphate (AzaUMP, K i = 12 ±3 nM) > allopurinol-3-riboside 5′- monophosphate (Ki = 240 ± 20 nM). XMP is an ∼150-fold more potent inhibitor of PfODCase compared with the human enzyme. The structure of PfODCase was solved in the absence of ligand and displays a classic TIM-barrel fold characteristic of the enzyme. Both the phosphate-binding loop and the βα5-loop have conformational flexibility, which may be associated with substrate capture and product release along the reaction pathway. © 2008 American Chemical Society.},
 bibtype = {article},
 author = {Langley, D.B. and Shojaei, M. and Chan, C. and Hiu, C.L. and Mackay, J.P. and Traut, T.W. and Guss, J.M. and Christopherson, R.I.},
 doi = {10.1021/bi702390k},
 journal = {Biochemistry},
 number = {12}
}

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The native enzyme is a homodimer with a subunit molecular mass of 38 kDa. The saturation curve for OMP as a substrate conformed to Michaelis-Menten kinetics with Km = 350 ± 60 nM and Vmax = 2.70 ± 0.10 μmol/min/mg protein. Inhibition patterns for nucleoside 5′-monophosphate analogues were linear competitive with respect to OMP with a decreasing potency of inhibition of PfODCase in the order: pyrazofurin 5′-monophosphate (Ki = 3.6 ± 0.7 nM) > xanthosine 5′-monophosphate (XMP, Ki = 4.4 ± 0.7 nM) > 6-azauridine 5′-monophosphate (AzaUMP, K i = 12 ±3 nM) > allopurinol-3-riboside 5′- monophosphate (Ki = 240 ± 20 nM). XMP is an ∼150-fold more potent inhibitor of PfODCase compared with the human enzyme. The structure of PfODCase was solved in the absence of ligand and displays a classic TIM-barrel fold characteristic of the enzyme. Both the phosphate-binding loop and the βα5-loop have conformational flexibility, which may be associated with substrate capture and product release along the reaction pathway. © 2008 American Chemical Society.","bibtype":"article","author":"Langley, D.B. and Shojaei, M. and Chan, C. and Hiu, C.L. and Mackay, J.P. and Traut, T.W. and Guss, J.M. and Christopherson, R.I.","doi":"10.1021/bi702390k","journal":"Biochemistry","number":"12","bibtex":"@article{\n title = {Structure and inhibition of orotidine 5′-monophosphate decarboxylase from Plasmodium falciparum},\n type = {article},\n year = {2008},\n pages = {3842-3854},\n volume = {47},\n id = {a141dd55-ab8c-3d60-ae66-5bb20bb77e87},\n created = {2023-01-10T01:45:40.465Z},\n file_attached = {false},\n profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},\n group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},\n last_modified = {2023-01-10T01:45:40.465Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {Orotidine 5′-monophosphate (OMP) decarboxylase from Plasmodium falciparum (PfODCase, EC 4.1.1.23) has been overexpressed, purified, subjected to kinetic and biochemical analysis, and crystallized. 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