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Structure and kinetics of phosphonopyruvate hydrolase from voriovorax sp. Pal2: New insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily
- Source :
- Biochemistry. Sept 26, 2006, Vol. 45 Issue 38, 11491-11504
- Publication Year :
- 2006
-
Abstract
- The structure and properties of recombinant phosphonopyruvate (P-pyr) hydrolase (PPH) from variovorax sp. Pal2 expressed in E. coli is reported. Structure alignment of PPH with other superfamily members revealed two pairs of invariant or conservatively replaced residues that anchor the flexible gating loop.
Details
- Language :
- English
- ISSN :
- 00062960
- Volume :
- 45
- Issue :
- 38
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.154106936