Porcine d-amino acid Oxidase: Determination of the mRNA nucleotide sequence by the characterization of genomic and cDNA clones

Jacobs, P.; Brockly, Frédérique; Massaer, Marc; Loriau, R.; Guillaume, J; Ciccarelli, Ernesto; Heinderyckx, Michel; Cravador, A.; Biemans, Ralph; Elsen, A Van; Herzog, Albert; Bollen, Alex

doi:10.1016/0378-1119(87)90266-6

Cited by 7 publications

(3 citation statements)

References 15 publications

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“…those from pig kidney (Jacobs et al, 1987), Rhodotorula gracilis (Rhodosporidium toruloides) (Pilone et al, 1987), Trigonopsis variabilis (Pollegioni et al, 1993) and Fusarium solani (Isogai et al, 1990). More recently, the primary structure of the DAAO from R. gracilis has been determined by Edman degradation (Faotto et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…Although some DAOZ genes have been cloned and sequenced (Fukui et al, 1987;Furuya & Matsuda, 1993;Isogai et a/., 1990;Jacobs et al, 1987;Momoi et al, 1988Momoi et al, , 1990Tada et al, 1990), only four enzymes have been isolated to homogeneity, i.e. those from pig kidney (Jacobs et al, 1987), Rhodotorula gracilis (Rhodosporidium toruloides) (Pilone et al, 1987), Trigonopsis variabilis (Pollegioni et al, 1993) and Fusarium solani (Isogai et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

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D-Amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217

Alonso

Barredo²,

Dı́ez³

et al. 1998

Microbiology

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The complete nucleotide sequence of the DA07 gene encoding D-amino-acid oxidase (DAAO) in the yeast Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217 has been determined. The primary structure of DAAO was deduced from the nucleotide sequence of a cDNA clone that covered the entire amino acid coding sequence. Comparison of cDNA and genomic sequences of DA07 revealed the presence of five introns. Because this is the first gene of strain ATCC 26217 that has been cloned so far, the nucleotide sequences of these introns were compared to those from other fungi. Upstream of the structural gene there was a stretch of C + T-rich DNA similar to that found in the promoter region of a number of yeast genes. The cDNA gene, which encoded a protein of 368 amino acids (molecular mass 40 kDa), was overexpressed in Escherichia coli under the control of the strong lipoprotein promoter. Interestingly, a significant fraction (13-62 %) of the total DAAO activity was recovered in i t s apoenzyme form, the percentage depending on the culture conditions. This fact allowed a rapid purification of the recombinant DAAO by affinity chromatography. The high level of expression achieved in f . coli and the possibility of modifying its catalytic properties by protein engineering provide a new model for the study of this enzyme.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

D-Amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217

Alonso

Barredo²,

Dı́ez³

et al. 1998

Microbiology

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“…The precise physiological significance of this enzyme which in mammals is most abundant in liver, kidney, and brain is still unclear (Le Hir and Dubach, 1981;Momoi et al, 1988;Konno et al, 1989). The cDNA sequence of porcine DAO has been described by Jacobs et al (1987) and Fukui et al (1987).…”

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confidence: 99%

Localization of four new markers to pig chromosomes 1, 6, and 14 by radioactive in situ hybridization

Mellink

Lahbib-Mansais

Yerle

et al. 1993

Cytogenet Genome Res

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The genes coding for glucose regulated protein, 78kDal (GRP78), hormone-sensitive lipase (LIPE), plasminogen activator or urokinase (PLAU), and D-amino acid oxidase (DAO) were localized in the pig by radioactive in situ hybridization. GRP78 was mapped to 1q2.10→q2.13 and LIPE was localized to chromosome 6cen→q12. The genes for PLAU and DAO were both assigned to chromosome 14, in the region q2.4→q2.6 and q2.1→q2.3, respectively. The results are compared to mapping data in other mammalian species.

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Porcine D-amino acid oxidase: Production of the biologically active enzyme in Escherichia coli

Ciccarelli¹,

Massaer²,

Guillaume³

et al. 1989

Biochemical and Biophysical Research Communications

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DNA molecules coding either for mature porcine D-amino acid oxidase or for truncated forms of the enzyme have been obtained by stepwise addition of synthetic oligonucleotides to a partial cDNA. Under the control of the lambda PL thermoregulatable promoter, these DNAs were respectively expressed in Escherichia coli as 36, 28 and 25 kilodalton polypeptides, specifically recognised by antibodies raised against the natural enzyme. None of the truncated proteins were biologically active whereas the mature recombinant species was able to hydrolyze D-alanine in vitro as efficiently as the natural product.

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Porcine d-amino acid Oxidase: Determination of the mRNA nucleotide sequence by the characterization of genomic and cDNA clones

Cited by 7 publications

References 15 publications

D-Amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217

D-Amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217

Localization of four new markers to pig chromosomes 1, 6, and 14 by radioactive in situ hybridization

Porcine D-amino acid oxidase: Production of the biologically active enzyme in Escherichia coli

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