The non-equivalence of the active sites and the mechanism of a mutationally altered E. coli alkaline phosphatase

D Chappelet-Tordo et al. Biochem Biophys Res Commun. 1975.

. 1975 Mar 17;63(2):529-34.

doi: 10.1016/0006-291x(75)90720-2.

No abstract available

Similar articles

Hydrogen-tritium exchange of partially and fully reconstituted zinc and cobalt alkaline phosphatase of Escherichia coli.
Brown EM, Ulmer DD, Vallee BL. Brown EM, et al. Biochemistry. 1974 Dec 17;13(26):5328-34. doi: 10.1021/bi00723a012. Biochemistry. 1974. PMID: 4611482 No abstract available.
A mutationally altered alkaline phosphatase from Escherichia coli. I. Formation of an active enzyme in vitro and phenotypic suppression in vivo.
Halford SE, Lennette DA, Kelley PM, Schlesinger MJ. Halford SE, et al. J Biol Chem. 1972 Apr 10;247(7):2087-94. J Biol Chem. 1972. PMID: 4552687 No abstract available.
Mutationally altered rate constants in the mechanism of alkaline phosphatase.
Halford SE, Schlesinger MJ. Halford SE, et al. Biochem J. 1974 Sep;141(3):845-52. doi: 10.1042/bj1410845. Biochem J. 1974. PMID: 4618778 Free PMC article.
Structure and mechanism of alkaline phosphatase.
Coleman JE. Coleman JE. Annu Rev Biophys Biomol Struct. 1992;21:441-83. doi: 10.1146/annurev.bb.21.060192.002301. Annu Rev Biophys Biomol Struct. 1992. PMID: 1525473 Review.
Alkaline phosphatase. Biochemistry of mammalian alkaline phosphatases.
Butterworth PJ. Butterworth PJ. Cell Biochem Funct. 1983 Jul;1(2):66-70. doi: 10.1002/cbf.290010202. Cell Biochem Funct. 1983. PMID: 6383642 Review. No abstract available.