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PMID: 15982 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium.

Journal of bacteriology ·Vol. 130 ·No. 1 ·1977-04-00 ·Pages 411-9

Weppelman R, Kier LD, Ames BN

Abstract

The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits.

MeSH Terms
2',3'-Cyclic-Nucleotide Phosphodiesterases/metabolism Acid Phosphatase/metabolism Adenosine Monophosphate/metabolism Arsenates/pharmacology Cobalt/pharmacology Glucosephosphates/metabolism Hexoses Hydrogen-Ion Concentration Kinetics Mercury/pharmacology Molecular Weight Phosphates/pharmacology Phosphoric Diester Hydrolases/metabolism Salmonella typhimurium/enzymology Zinc/pharmacology
Chemicals
Arsenates Glucosephosphates Hexoses Phosphates Cobalt Adenosine Monophosphate Acid Phosphatase 2',3'-Cyclic-Nucleotide Phosphodiesterases Phosphoric Diester Hydrolases Mercury Zinc
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Weppelman R
Kier L D
Ames B N
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17 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.130.1.411-419.1977
Published
1977-04-00
Pages
411-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC235219
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.130.1.411-419.1977 PMC Full Text View journal details
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