A Model of the Transition State in the Alkaline Phosphatase Reaction
Open Access
- 1 March 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (13) , 8351-8354
- https://doi.org/10.1074/jbc.274.13.8351
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- A Horner-Wittig Synthesis of 1-Chlorovinyl Sulfoxides.Phosphorus, Sulfur, and Silicon and the Related Elements, 1996
- Mutations at Positions 153 and 328 inEscherichia coliAlkaline Phosphatase Provide Insight Towards the Structure and Function of Mammalian and Yeast Alkaline PhosphatasesJournal of Molecular Biology, 1995
- Crystal structures of rat acid phosphatase complexed with the transition‐state analogs vanadate and molybdateEuropean Journal of Biochemistry, 1994
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Reaction mechanism of alkaline phosphatase based on crystal structuresJournal of Molecular Biology, 1991
- Function of arginine-166 in the active site of Escherichia coli alkaline phosphataseBiochemistry, 1988
- Nuclear magnetic resonance and neutron diffraction studies of the complex of ribonuclease A with uridine vanadate, a transition-state analogBiochemistry, 1985
- Vanadium ion inhibition of alkaline phosphatase-catalyzed phosphate ester hydrolysisArchives of Biochemistry and Biophysics, 1976
- 17 E. coli Alkaline PhosphatasePublished by Elsevier ,1971
- A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphataseBiochimica et Biophysica Acta, 1960