منابع مشابه
Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase.
Escherichia coli alkaline phosphatase (AP) is a proficient phosphomonoesterase with two Zn(2+) ions in its active site. Sequence homology suggests a distant evolutionary relationship between AP and alkaline phosphodiesterase/nucleotide pyrophosphatase, with conservation of the catalytic metal ions. Furthermore, many other phosphodiesterases, although not evolutionarily related, have a similar a...
متن کاملSecretion of alkaline phosphatase subunits by spheroplasts of Escherichia coli.
Under conditions that permitted continued protein synthesis, spheroplasts of Escherichia coli were unable to form active alkaline phosphatase, although they synthesized protein that was antigenically related to alkaline phosphatase subunits. This cross-reacting protein was primarily detected in the medium of the spheroplast culture, and it had properties that closely resembled those of the alka...
متن کاملOsmoregulation of alkaline phosphatase synthesis in Escherichia coli K-12.
Alkaline phosphatase, the phoA product, is synthesized constitutively in phoR mutants. This constitutive synthesis, which is independent of phosphate control, varies with changes in the osmolarity of the growth medium; phoA expression increases with increasing osmolarity. Maximum expression of the osmoregulated genes phoA, ompC, and ompF was achieved by osmotic manipulation of minimal medium; c...
متن کاملDephosphorylation of phosphoproteins by Escherichia coli alkaline phosphatase.
A purified commercial preparation of Escherichia coli alkaline phosphatase (EC 3.1.3.1) has been shown to dephosphorylate several phosphoproteins including bovine heart glycogen synthase D, mixed phosphohistones, and rabbit skeletal muscle phosphorylase kinase but not rabbit skeletal muscle glycogen phosphorylase. Alkaline phosphatase completely removed phosphate groups previously added during ...
متن کاملRibosomal alterations controlling alkaline phosphatase isozymes in Escherichia coli.
Different patterns of isozymes were obtained by starch-gel electrophoresis of alkaline phosphatase from Escherichia coli strains differing only by strA or ram mutations, or both, in the 30S ribosomal subunit. The isozyme spread was reduced in strA and increased in ram strains; this strictly parallels the restriction and enhancement of translational ambiguity produced by these mutations. Strepto...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)94433-9