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The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
- Source :
- Trends in Biochemical Sciences. April, 1998, Vol. 23 Issue 4, p127, 3 p.
- Publication Year :
- 1998
-
Abstract
- The P-type ATPases belong to a superfamily of hydrolases whose structure is typified by the L-2-haloacid dehalogenase (HAD) 7,8 from Pseudomonas sp. The catalytic mechanism of P-type ATPases and HAD 7,8 are similar, providing clues to the evolution of these enzymes. The catalytic domain of P-type ATPases has been found to have the structural fold of haloacid dehalogenases. Thus, P-type ATPases might have evolved by fusion of a transmembrane protein with a HAD superfamily phosphatase domain.
Details
- ISSN :
- 09680004
- Volume :
- 23
- Issue :
- 4
- Database :
- Gale General OneFile
- Journal :
- Trends in Biochemical Sciences
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.20742201