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Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function
- Source :
- Biochemistry. Jan 31, 2006, Vol. 45 Issue 4, p1162, 11 p.
- Publication Year :
- 2006
-
Abstract
- Contributions made by Pseudomonas aeruginosa (PaADI) core residues Cys406, His278, and Asp166 and the contribution from Asp280 to catalysis of the formation and hydrolysis of the Cys406-alkyluronium intermediate were assessed by kinetic analysis of site-directed mutants. The results suggest that electrostatic interactions play a dominant role in PaADI catalysis.
Details
- Language :
- English
- ISSN :
- 00062960
- Volume :
- 45
- Issue :
- 4
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.145038579