Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL047113-06
Application #
2223422
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1991-08-01
Project End
2000-07-31
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
6
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
Purdue University
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907

  Publications

Steussy, C Nicklaus; Vartia, Anthony A; Burgner 2nd, John W et al. (2005) X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA. Biochemistry 44:14256-67
Sutherlin, Autumn; Hedl, Matija; Sanchez-Neri, Barbara et al. (2002) Enterococcus faecalis 3-hydroxy-3-methylglutaryl coenzyme A synthase, an enzyme of isopentenyl diphosphate biosynthesis. J Bacteriol 184:4065-70
Hedl, Matija; Sutherlin, Autumn; Wilding, E Imogen et al. (2002) Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase, a dual-function protein of isopentenyl diphosphate biosynthesis. J Bacteriol 184:2116-22
Kim, D Y; Stauffacher, C V; Rodwell, V W (2000) Dual coenzyme specificity of Archaeoglobus fulgidus HMG-CoA reductase. Protein Sci 9:1226-34
Kim, D Y; Stauffacher, C V; Rodwell, V W (2000) Engineering of Sulfolobus solfataricus HMG-CoA reductase to a form whose activity is regulated by phosphorylation and dephosphorylation. Biochemistry 39:2269-75
Wilding, E I; Kim, D Y; Bryant, A P et al. (2000) Essentiality, expression, and characterization of the class II 3-hydroxy-3-methylglutaryl coenzyme A reductase of Staphylococcus aureus. J Bacteriol 182:5147-52
Bochar, D A; Tabernero, L; Stauffacher, C V et al. (1999) Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochemistry 38:8879-83
Bochar, D A; Stauffacher, C V; Rodwell, V W (1999) Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mol Genet Metab 66:122-7
Tabernero, L; Bochar, D A; Rodwell, V W et al. (1999) Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci U S A 96:7167-71
Bochar, D A; Stauffacher, C V; Rodwell, V W (1999) Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase. Biochemistry 38:15848-52

Showing the most recent 10 out of 27 publications