1X1Z

Orotidine 5'-monophosphate decarboxylase (odcase) complexed with BMP (produced from 6-cyanoump)

Summary for 1X1Z

• Entry DOI: 10.2210/pdb1x1z/pdb
• Related: 1DV7 1DVJ 1KLY 1KLZ 1KM0 1KM1 1KM2 1KM3 1KM4 1KM5 1KM6 1LOL 1LOQ 1LOR 1LOS 1LP6
• Descriptor: Orotidine 5'-phosphate decarboxylase, 6-HYDROXYURIDINE-5'-PHOSPHATE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: orotidine 5'-monophosphate decarboxylase (odcase), barbituric acid ribosyl 5'-monophosphate (bmp), 6-cyanoump, lyase
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 2
• Total formula weight: 55807.54

Authors

Fujihashi, M.,Bello, A.M.,Poduch, E.,Wei, L.,Annedi, S.C.,Pai, E.F.,Kotra, L.P. (deposition date: 2005-04-15, release date: 2005-12-06, Last modification date: 2024-05-29)

Primary citation

Fujihashi, M.,Bello, A.M.,Poduch, E.,Wei, L.,Annedi, S.C.,Pai, E.F.,Kotra, L.P.
An unprecedented twist to ODCase catalytic activity
J.Am.Chem.Soc., 127:15048-15050, 2005

PubMed Abstract: Orotidine-5'-monophosphate decarboxylase (ODCase) has evolved to catalyze a decarboxylation reaction, most probably via a carbanion species at the C6 position of orotidine-5'-monophosphate. We reveal an unusual biochemical pathway of conversion of 6-cyano-uridine-5'-monophosphate by ODCase to barbiturate-5'-monophosphate via perhaps an electrophilic center at the C6 position, leading to inhibition. This potential of ODCase is very useful in the design of novel inhibitors.

PubMed: 16248642
DOI: 10.1021/ja054865u

Experimental method

X-RAY DIFFRACTION (1.45 Å)