• BMB Reports
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• 제30권4호
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• pp.246-252
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• 1997

Malonate decarboxylase from Acinetobacter calcoaceticus is shown to have malonyl-CoA: acetate CoA transferase. acetyl-CoA: malonate CoA transferase, and malonyl-CoA decarboxylase activity. These enzyme activities were elucidated by isotope exchange reactions. The enzyme modified by N-ethylmaleimide completely lost its malonate decarboxylase activity, whereas it still kept CoA transferases and malonyl-CoA decarboxylase activities. The existence of CoA transferases and malonyl-CoA decarboxylase activity is clear, but their physiological significance is obscure. The catalytic reactions for two eoA transfers and malonyl-CoA decarboxylation proceed via a cyclic mechanism, which is through two covalent intermediates, enzyme-Smalonyl and enzyme-S-acetyL proposed for malonate decarboxylation of the enzyme.

• Journal of Microbiology and Biotechnology
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• 제17권3호
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• pp.408-413
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• 2007

Putrescine has a negative effect on health and is also used as an indicator of quality on meat products. We investigated the genes involved in putrescine production by Serratia liquefaciens IFI65 isolated from a spoiled Spanish dry-cured ham. We report here the genetic organization of its ornithine decarboxylase encoding region. The 5,506-bp DNA region showed the presence of three complete and two partial open reading frames. Putative functions have been assigned to several gene products by sequence comparison with proteins included in the databases. The second gene putatively coded for an ornithine decarboxylase. The functionality of this decarboxylase has been experimentally demonstrated by complementation to an E. coli defective mutant. Based on sequence comparisons of some enterobacterial ornithine decarboxylase regions, we have elaborated a hypothetical pathway for the acquisition of putrescine biosynthetic genes in some Enterobacteriaceae strains.

• KSBB Journal
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• 제14권3호
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• pp.264-272
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• 1999

Mandelate pathway를 거치는 Pseudomonas putida(KCTC 1751)의 전세포 benzoylformate dcarboxylase를 이용하여 benzoylformate를 benzaldehyde로 변환하였고 성장배지의 조성이 cell내부에 축적되는 benzoylformate dcarboxylase의 양에 미치는 영향을 조사하였다. 전세포효소의 재사용을 위하여 calcumalginate 캡슐 고정회법을 이용하여 캡슐고정화 Pseudomonas putida를 제조하였다. 캡슐 고정화 미생물을 M3배지에서 3일간 배양한 후 M1배지에서 1일간 배양한 결과 77.75g/L의 미생물 건조중량을 얻었다. 캡슐 고정화 전세포 benzoyltormate decarboxylase의 비활생도는 자유배양에 의한 전세포효소의 비활성도에 비해 약 1/2값을 나타내었으며 캡슐 고정화 전세포 benzoyltormate decarboxylase를 20회 재사용시 20%의 실활을 보였으며 캡슐 재사용 30회 이후 미생물의 건조중량은 약 10% 감소를 보였다.

• BMB Reports
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• 제28권2호
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• pp.107-111
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• 1995

In malonate grown Pseudomonas fluorescens, malonate decarboxylase and acetyl-CoA synthetase were induced, whereas in Acinetobacter calcoaceticus malonate decarboxylase, acetate kinase, and phosphate acetyltransferase were induced. In both bacteria malonate decarboxylase was the first, key enzyme catalyzing the decarboxylation of malonate to acetate, and it was localized in the periplasmic space. Acetate thus formed was metabolized to acetyl-CoA directly by acetyl-CoA synthetase in Pseudomonas, and to acetyl-CoA via acetyl phosphate by acetate kinase and phosphate acetyltransferase in Acinetobacter.

• Applied Biological Chemistry
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• 제51권4호
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• pp.344-345
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• 2008

• 한국식품영양과학회지
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• 제24권3호
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• pp.415-419
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• 1995

Ornithine decarboxylase(ODC) catalyzes the first and key step in the polyamine biosynthetic pathway. Ornithine decarboxylase is known to the enzyme that increase substantially its activity in regenerating liver. We found that activity and mRNA level for ODC increase significantly after partial hepatectomy in the rat. After laparotomy, there was significant decrease in activity ; however, mRNA content was unaltered in contrast to previous reports of no change in ornithine decarboxylase and thymidine kinase after sham hepatectomy. This may be mediated by the decrease in food intake after hepatectomy. Therefore it is necessary to examine the effect of food intake after hepatectomy on the ODC activity and mRNA level in the future.

• Journal of Plant Biology
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• 제27권1호
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• pp.1-6
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• 1984

Kinetin(4.7$\times$10\ulcornerM) and 6-benzylaminopurine (2.2$\times$10\ulcornerM) were found to increase ca. 1.5-fold putrescice content in corn grown in medium containing kinetin and 6-benzylaminopurine(6-BAP) for 3days whereas kinetin was found to decrase ca. 30% spermidine and spermine, respectively. KCI (3$\times$10\ulcornerM) was found to decrease more than 50% putrescine content. After germination, ornithine decarboxylase activity was observed to increase constantly whereas arginine decarboxylase activity remained constant, suggesting involvement in putrescine biosynthesis. 6-benzylaminopurine was shown to increase more activities of arginine ornithine decarboxylase than kinetin when they were added to medium.

• BMB Reports
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• 제32권4호
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• pp.414-418
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• 1999

A novel gene for malonyl-CoA decarboxylase was discovered in the mat operon, which encodes a set of genes involved in the malonate metabolism of Rhizobium trifolii (An and Kim, 1998). The subunit mass determined by SDS-PAGE was 53 kDa, which correspond to the deduced mass from the sequence data. The molecular mass of the native enzyme determined by field flow fractionation was 208 kDa, indicating that R. trifolii malonyl-CoA decarboxylase is homotetrameric. R. trifolii malonyl-CoA decarboxylase converted malonyl-CoA to acetyl-CoA with a specific activity of 100 unit/mg protein. Methylmalonyl-CoA was decarboxylated with a specific activity of 0.1 unit/mg protein. p-Chloromercuribenzoate inhibited this enzyme activity, suggesting that thiol group(s) is(are) essential for this enzyme catalysis. Database analysis showed that malonyl-CoA decarboxylase from R. trifolii shared 32.7% and 28.1% identity in amino acid sequence with those from goose and human, respectively, and it would be located in the cytoplasm. However, there is no sequence homology between this enzyme and that from Saccharopolyspora erythreus, suggesting that malonyl-CoA decarboxylases from human, goose, and R. trifolii are in the same class, whereas that from S. erythreus is in a different class or even a different enzyme, methylmalonyl-CoA decarboxylase. According to the homology analysis, Cys-214 among three cysteine residues in the enzyme was found in the homologous region, suggesting that the cysteine was located at or near the active site and plays a critical role in catalysis.

• BMB Reports
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• 제31권3호
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• pp.233-239
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• 1998

A GABA synthesizing enzyme, glutamate decarboxylase, has been purified from bovine brain by several chromatographic procedures. The preparation appeared homogeneous on SDS-PAGE. The enzyme is a homodimeric protein with a molecular mass of 120 kDa. The activation of glutamate decarboxylase by ginesenosides from Panax ginseng C.A. Meyer has been studied. Preincubation of the enzyme with total ginsenoside, $Rb_2$ and Rc ginsenosides, increased glutamate decarboxylase activities in a dose-dependent manner. There was a reproducible decrease in $K_m$, in addition to a increase in $V_{max}$, in response to increasing concentrations of the Rc ginsenoside fraction. Upon addition of the ginsenoside to the enzyme, a decrease in flurorescence intensity was discernible, together with an increase in emission anisotropy. Judging from the anisotropy values, the ginsenoside is rapidly trapped by the protein matrix. Total ginsenoside was administered to rats and the rat brains were removed for the measurement of the changes of GABA shunt regulating enzyme activities. Among the GABA shunt regulating enzymes, only the glutamate decarboxylase activities were increased after ginsenoside treatment. Therefore, it is suggested that the ginsenosides may elevate the GABA level in brain by activation of glutamate decarboxylase and the enzymatic activation might be due to the conformational change induced by binding of ginsenoside to the enzyme.

• 한국미생물·생명공학회지
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• 제43권3호
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• pp.300-305
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• 2015

효율적인 γ-aminobutyric acid (GABA)의 생산을 위해 Lactobacillus plantarum WCFS1로부터 글루탐산 탈탄산효소(glutamate decarboxylase, GAD)를 대장균에 발현, 정제 후 silica beads에 covalent coupling 방법을 이용하여 고정화하였다. 고정화된 효소의 특성을 고정화하지 않은 효소와 비교한 결과, 모든 pH의 범위(pH 3.5–6.0)에서 80% 이상의 활성을 나타내었으며 pH 안정성과 열 안정성 모두 증대되었다. 이 고정화 효소를 packed-bed reactor에 충진하여 GABA의 생산성을 확인한 결과 1리터당 1시간에 최대 41.7 g의 GABA 생산이 가능한 것으로 확인되었다.