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Titolo:
Identification and characterization of DdPDE3, a cGMP-selective phosphodiesterase from Dictyostelium
Autore:
Kuwayama, H; Snippe, H; Derks, M; Roelofs, J; van Haastert, PJM;
Indirizzi:
Univ Groningen, Dept Biochem, GBB, NL-9747 AG Groningen, Netherlands Univ Groningen Groningen Netherlands NL-9747 AG G Groningen, Netherlands
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 353, anno: 2001,
parte:, 3
pagine: 635 - 644
SICI:
0264-6021(20010201)353:<635:IACODA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE; CAMP-SPECIFIC PHOSPHODIESTERASE; DEPENDENT PROTEIN-KINASE; SIGNAL-TRANSDUCTION; GMP PHOSPHODIESTERASE; CHEMOTACTIC MUTANTS; DISCOIDEUM AMEBAS; GUANYLYL CYCLASES; BINDING; ADENYLYL;
Keywords:
chemotaxis; cloning; guanylate cyclase; mutant stmF;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: van Haastert, PJM Univ Groningen, Dept Biochem, GBB, Nijenborgh 4, NL-9747AG Groningen, Netherlands Univ Groningen Nijenborgh 4 Groningen Netherlands NL-9747 AG
Citazione:
H. Kuwayama et al., "Identification and characterization of DdPDE3, a cGMP-selective phosphodiesterase from Dictyostelium", BIOCHEM J, 353, 2001, pp. 635-644

Abstract

In Dictyostelium cAMP and cGMP have important functions as first and second messengers in chemotaxis and development. Two cyclic-nucleotide phosphodiesterases (DdPDE 1 and 2) have been identified previously, an extracellulardual-specificity enzyme and an intracellular cAMP-specific enzyme (encodedby the psdA and regA genes respectively). Biochemical data suggest the presence of at least one cGMP-specific phosphodiesterase (PDE) that is activated by cGMP. Using bioinformatics we identified a partial sequence in the Dictyostelium expressed sequence tag database that shows a high degree of amino acid sequence identity with mammalian PDE catalytic domains (DdPDE3). The deduced amino acid sequence of a full-length DdPDE3 cDNA isolated in thisstudy predicts a 60 kDa protein with a 300-residue C-terminal PDE catalytic domain, which is preceded by approx. 200 residues rich in asparagine and glutamine residues. Expression of the DdPDE3 catalytic domain in Escherichia coli shows that the enzyme has Michaelis-Menten kinetics and a higher affinity for cGMP (K-m = 0.22 muM) than for cAMP (K-m = 145 muM); cGMP does not stimulate enzyme activity. The enzyme requires bivalent cations for activity; Mn2+ is preferred to Mg2+, whereas Ca2+ yields no activity. DdPDE3 is inhibited by 3-isobutyl-1-methylxanthine with an IC50 of approx. 60 muM. Overexpression of the DdPDE3 catalytic domain in Dictyostelium confirms thesekinetic properties without indications of its activation by cGMP. The properties of DdPDE3 resemble those of mammalian PDE9, which also shows the highest sequence similarity within the catalytic domains. DdPDE3 is the first cGMP-selective PDE identified in lower eukaryotes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 00:42:23