1996
DOI: 10.1128/jb.178.19.5781-5786.1996
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Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme

Abstract: We have cloned a gene (aphA) encoding acetylpolyamine amidohydrolase from Mycoplana ramosa ATCC 49678 (previously named Mycoplana bullata). A genomic library of M. ramosa was screened with an oligonucleotide probe designed from a N-terminal amino acid sequence of the enzyme purified from M. ramosa. Nucleotide sequence analysis revealed an open reading frame of 1,023 bp which encodes a polypeptide with a molecular mass of 36,337 Da. This is the first report of the structure of acetylpolyamine amidohydrolase. Th… Show more

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Cited by 43 publications
(72 citation statements)
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References 23 publications
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“…2a). This enzymatic property of AphA is consistent with that reported for AphA from Mycoplana ramosa (28). The promoters of aphA and aphB were both induced by exogenous acetylputrescine to a much higher level than that of agmatine in the wild-type strain PAO1.…”
Section: Discussionsupporting
confidence: 89%
See 1 more Smart Citation
“…2a). This enzymatic property of AphA is consistent with that reported for AphA from Mycoplana ramosa (28). The promoters of aphA and aphB were both induced by exogenous acetylputrescine to a much higher level than that of agmatine in the wild-type strain PAO1.…”
Section: Discussionsupporting
confidence: 89%
“…The AphA protein of P. aeruginosa PAO1 exhibits 70% sequence similarity to acetylpolyamine amidohydrolase of Mycoplana ramosa, which requires metals (zinc or cobalt) for its catalytic reaction on a variety of acetylpolyamines, including acetylputrescine (28). To demonstrate the proposed enzymatic activity of AphA, a recombinant form of AphA was overexpressed in E. coli and purified to homogeneity, as described in Materials and Methods.…”
Section: Resultsmentioning
confidence: 99%
“…Sources of published sequences : a, van Berkum et al (1996) ; b, Willems & Collins (1993) ;c, van Berkum et al (1998) ; d, Rome et al (1996) ;e, de Lajudie et al (1994) ; f, Nour et al (1994) ; g, Yanagi & Yamasato (1993) ; h, Nour et al (1995) ; i, Wang et al (1999) ; j, Barrera et al (1997) ; k, Sakurada et al (1996) ; l, Hiraishi & Ueda (1994) ; m, Dryden & Kaplan (1990) ; n, Weisburg et al (1989) ;o, Eckloff et al (1994) ; p, Liesack et al (1992) ; q, Borghese et al (1998) ; r, Tybulewicz et al (1984) ; s, Andersson et al (1998) ;t, McGowan et al (1997) ; u, Ronner et al (1991) ;v, Fernandez de Henestrosa et al (1995) ;w, Calero et al (1994) ;x, Dunkin & Wood (1994) ; y, Thompson & Blaser (1995).…”
Section: Methodsmentioning
confidence: 99%
“…Class I and II ancestors are acetylpolyamine amidohydrolases that participate in the degradation of acetylpolyamines via a deacetylation mechanism similar to that of eukaryotic HDACs (Sakurada et al, 1996;Leipe and Landsman, 1997). Class III members are related to bacterial CobB that deacetylates and thus regulates acetyl-CoA synthetase (ACS) activity (Starai et al, 2002).…”
Section: Histone Deacetylationmentioning
confidence: 99%