Orotidine 5'-phosphate decarboxylase (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Orotidine 5'-phosphate decarboxylase" in English language version.

refsWebsite

Global rank English rank

15nih.gov

4^th place

14doi.org

2^nd place

1rcsb.org

8,838^th place

8,783^rd place

doi.org

PDB: 1EIX; Harris P, Navarro Poulsen JC, Jensen KF, Larsen S (April 2000). "Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase". Biochemistry. 39 (15): 4217–24. doi:10.1021/bi992952r. PMID 10757968.
Radzicka A, Wolfenden R (January 1995). "A proficient enzyme". Science. 267 (5194): 90–3. doi:10.1126/science.7809611. PMID 7809611.
Miller BG, Smiley JA, Short SA, Wolfenden R (August 1999). "Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals". J. Biol. Chem. 274 (34): 23841–3. doi:10.1074/jbc.274.34.23841. PMID 10446147.
Miller BG, Wolfenden R (2002). "Catalytic proficiency: the unusual case of OMP decarboxylase". Annu. Rev. Biochem. 71: 847–85. doi:10.1146/annurev.biochem.71.110601.135446. PMID 12045113.
Wu N, Pai EF (August 2002). "Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase". J. Biol. Chem. 277 (31): 28080–7. doi:10.1074/jbc.M202362200. PMID 12011084.
Beak P, Siegel B (1976). "Mechanism of decarboxylation of 1,3-dimethylorotic acid. A model for orotidine 5'-phosphate decarboxylase". J Am Chem Soc. 98 (12): 3601–6. doi:10.1021/ja00428a035. PMID 1270703.
Lee JK, Houk KN (May 1997). "A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase". Science. 276 (5314): 942–5. doi:10.1126/science.276.5314.942. PMID 9139656.
Silverman, R.B.; Groziak, M.P. (1982). "Model Chemistry for a Covalent Mechanism of Action of Orotidine 5'-Phosphate Decarboxylase". J. Am. Chem. Soc. 104 (23): 6434–6439. doi:10.1021/ja00387a047.
Richavy MA, Cleland WW (2000). "Determination of the Mechanism of Orotidine 5'-Monophosphate Decarboxylase by Isotope Effects". Biochemistry. 39 (16): 4569–4574. doi:10.1021/bi000376p. PMID 10769111.
Toth K, Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP (October 2007). "Product Deuterium Isotope Effect for Orotidine 5'-Monophosphate Decarboxylase: Evidence for the Existence of a Short-Lived Carbanion Intermediate". J. Am. Chem. Soc. 129 (43): 12946–7. doi:10.1021/ja076222f. PMC 2483675. PMID 17918849.
Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP (February 2008). "Formation and Stability of a Vinyl Carbanion at the Active Site of Orotidine 5′-Monophosphate Decarboxylase: pKa of the C-6 Proton of Enzyme-Bound UMP". J. Am. Chem. Soc. 130 (5): 1574–5. doi:10.1021/ja710384t. PMC 2652670. PMID 18186641.
Van Vleet JL, Reinhardt LA, Miller BG, Sievers A, Cleland WW (January 2008). "Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediate". Biochemistry. 47 (2): 798–803. doi:10.1021/bi701664n. PMID 18081312.
Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW (1996). "Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase". J Biol Chem. 271 (18): 10704–10708. doi:10.1074/jbc.271.18.10704. PMID 8631878.
Boeke JD, LaCroute F, Fink GR (1984). "A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance". Mol Gen Genet. 197 (2): 345–346. doi:10.1007/BF00330984. PMID 6394957.

nih.gov

pubmed.ncbi.nlm.nih.gov

PDB: 1EIX; Harris P, Navarro Poulsen JC, Jensen KF, Larsen S (April 2000). "Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase". Biochemistry. 39 (15): 4217–24. doi:10.1021/bi992952r. PMID 10757968.
Radzicka A, Wolfenden R (January 1995). "A proficient enzyme". Science. 267 (5194): 90–3. doi:10.1126/science.7809611. PMID 7809611.
Miller BG, Smiley JA, Short SA, Wolfenden R (August 1999). "Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals". J. Biol. Chem. 274 (34): 23841–3. doi:10.1074/jbc.274.34.23841. PMID 10446147.
Miller BG, Wolfenden R (2002). "Catalytic proficiency: the unusual case of OMP decarboxylase". Annu. Rev. Biochem. 71: 847–85. doi:10.1146/annurev.biochem.71.110601.135446. PMID 12045113.
Wu N, Pai EF (August 2002). "Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase". J. Biol. Chem. 277 (31): 28080–7. doi:10.1074/jbc.M202362200. PMID 12011084.
Beak P, Siegel B (1976). "Mechanism of decarboxylation of 1,3-dimethylorotic acid. A model for orotidine 5'-phosphate decarboxylase". J Am Chem Soc. 98 (12): 3601–6. doi:10.1021/ja00428a035. PMID 1270703.
Lee JK, Houk KN (May 1997). "A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase". Science. 276 (5314): 942–5. doi:10.1126/science.276.5314.942. PMID 9139656.
Richavy MA, Cleland WW (2000). "Determination of the Mechanism of Orotidine 5'-Monophosphate Decarboxylase by Isotope Effects". Biochemistry. 39 (16): 4569–4574. doi:10.1021/bi000376p. PMID 10769111.
Toth K, Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP (October 2007). "Product Deuterium Isotope Effect for Orotidine 5'-Monophosphate Decarboxylase: Evidence for the Existence of a Short-Lived Carbanion Intermediate". J. Am. Chem. Soc. 129 (43): 12946–7. doi:10.1021/ja076222f. PMC 2483675. PMID 17918849.
Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP (February 2008). "Formation and Stability of a Vinyl Carbanion at the Active Site of Orotidine 5′-Monophosphate Decarboxylase: pKa of the C-6 Proton of Enzyme-Bound UMP". J. Am. Chem. Soc. 130 (5): 1574–5. doi:10.1021/ja710384t. PMC 2652670. PMID 18186641.
Van Vleet JL, Reinhardt LA, Miller BG, Sievers A, Cleland WW (January 2008). "Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediate". Biochemistry. 47 (2): 798–803. doi:10.1021/bi701664n. PMID 18081312.
Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW (1996). "Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase". J Biol Chem. 271 (18): 10704–10708. doi:10.1074/jbc.271.18.10704. PMID 8631878.
Boeke JD, LaCroute F, Fink GR (1984). "A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance". Mol Gen Genet. 197 (2): 345–346. doi:10.1007/BF00330984. PMID 6394957.

ncbi.nlm.nih.gov

Toth K, Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP (October 2007). "Product Deuterium Isotope Effect for Orotidine 5'-Monophosphate Decarboxylase: Evidence for the Existence of a Short-Lived Carbanion Intermediate". J. Am. Chem. Soc. 129 (43): 12946–7. doi:10.1021/ja076222f. PMC 2483675. PMID 17918849.
Amyes TL, Wood BM, Chan K, Gerlt JA, Richard JP (February 2008). "Formation and Stability of a Vinyl Carbanion at the Active Site of Orotidine 5′-Monophosphate Decarboxylase: pKa of the C-6 Proton of Enzyme-Bound UMP". J. Am. Chem. Soc. 130 (5): 1574–5. doi:10.1021/ja710384t. PMC 2652670. PMID 18186641.

rcsb.org

PDB: 1EIX; Harris P, Navarro Poulsen JC, Jensen KF, Larsen S (April 2000). "Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase". Biochemistry. 39 (15): 4217–24. doi:10.1021/bi992952r. PMID 10757968.