The 5′-Nucleotidases and Cyclic Phosphodiesterases (3′-Nucleotidases) of the Enterobacteriaceae
AUTOR(ES)
Neu, Harold C.
RESUMO
All members of the Enterobacteriaceae possess distinct 5′-nucleotidases and cyclic phosphodiesterases (3′-nucleotidases) that can be differentiated from the acid and alkaline phosphatases and the acid sugar hydrolases. The nucleotidases and cyclic phosphodiesterases of the various Enterobacteriaceae are remarkably similar in properties. All of the 5′-nucleotidases hydrolyze 5′-nucleotides, adenosine triphosphate, and uridine diphosphoglucose. Their pH optimum is from 5.7 to 6.1. The cyclic phosphodiesterases hydrolyze 3′-nucleotides, cyclic phosphonucleotides, bis-(p-nitrophenyl)phosphate, and p-nitrophenylphosphate. Their pH optimum is from 7.2 to 7.8. For both enzymes, cobalt showed optimal metal stimulation. An intracellular protein inhibitor for the 5′-nucleotidase is present in all of the Enterobacteriaceae. No inhibitor of cyclic phosphodiesterase activity exists, although hydrolysis of both cyclic phosphonucleotides and 3′-nucleotides is inhibited by ribonucleic acid. Neither of the enzymes is subject to control by phosphate level or by catabolite repression. Of the other bacteria studied, only Haemophilus and Bacillus subtilis contained significant 3′- or 5′-nucleotidase activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=252204Documentos Relacionados
- Repressible extracellular phosphodiesterases showing cyclic 2',3'- and cyclic 3',5'-nucleotide phosphodiesterase activities in Neurospora crassa.
- Metabolism of Cytokinin 1: DEPHOSPHORYLATION OF CYTOKININ RIBONUCLEOTIDE BY 5′-NUCLEOTIDASES FROM WHEAT GERM CYTOSOL
- The Inhibition of Plant and Animal Adenosine 3′:5′-Cyclic Monophosphate Phosphodiesterases by a Cell-Division-Promoting Substance from Tissues of Higher Plant Species
- T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3
- The content and metabolism of cyclic adenosine 3', 5'-monophosphate and cyclic guanosine 3', 5'-monophosphate in adenocarcinoma of the human colon.