The role of histidine 63 in the catalytic mechanism of Bordetella pertussis adenylate cyclase.
Open Access
- 1 May 1992
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (14) , 9816-9820
- https://doi.org/10.1016/s0021-9258(19)50166-1
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetaseBiochemistry, 1991
- Intrinsic fluorescence of a truncated Bordetella pertussis adenylate cyclase expressed in Escherichia coliBiochemistry, 1990
- Characterization of ATP and calmodulin-binding properties of a truncated form of Bacillus anthracis adenylate cyclaseBiochemistry, 1990
- How do serine proteases really work?Biochemistry, 1989
- Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanismBiochemistry, 1988
- Dissecting the catalytic triad of a serine proteaseNature, 1988
- The calmodulin‐sensitive adenylate cyclase of Bordetella pertussis: cloning and expression in Escherichia colMolecular Microbiology, 1988
- 3-(Bromoacetyl)chloramphenicol, an active site-directed inhibitor for chloramphenicol acetyltransferaseBiochemistry, 1985
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970