• BMB Reports
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• v.33 no.4
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• pp.332-336
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• 2000

Phenazine 1-carboxylic acid (PCA) is an antifungal antibiotic isolated from a culture filtrate of Bacillus sp. B-6 producing an acyl CoA synthetase inhibitor. This antibiotic is reported as an inhibitor of an acyl CoA synthetase from Pseudomonas sp.. Bacillus sp. B-6 was resistant to PCA up to 350 ${\mu}g/ml$. We investigated the mechanism of the resistance of Bacillus sp. B-6 to PCA. The rate of growth in a medium containing up to 100 ${\mu}g/ml$ was as rapid as the PCA-free medium. At a PCA concentration of 300 ${\mu}g/ml$, the growth rate was more than half that of the control. In this work, we purified acyl CoA synthetase from Bacillus sp. B-6 and found that this acyl CoA synthetase was much less sensitive to PCA than the acyl CoA synthetase from other source. These findings suggested that the insensitivity of Bacillus sp. B-6 acyl CoA synthetase plays an important role in the PCA resistance of this bacterium.

• Proceedings of the Korean Society of Developmental Biology Conference
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• 2003.10a
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• pp.96-96
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• 2003

Acyl-CoA synthetase 4는 생쥐에 있어서 거의 모든 조직에서 발현하며 아라키돈산에 특이적인 효소이다. 아라키돈산은 세포막의 인지질로부터 cPLA2에 의하여 유리되고 cyclooxygenase-1, -2에 의하여 eicosanoid로 변환된다. 이렇게 생산된 prostaglandin과 같은 eicosanoid는 배란, 수정, 임신에 있어서 중요한 기능을 수행하고 있다. 그러나 세포막으로부터 유리된 아라키돈산은 acyl-CoA synthetase 4에 의하여 다시 세포막으로 재에스테르화되어 eicosaniod의 생산을 조절하는 것으로 생각되어지고 있다. 또한 acyl-CoA synthetase 4 유전자 한쪽이 knock-out된 heterozygote mouse에서는 사산, 유산과 난소에 있어서 황체 수의 증가 등을 보고하고 있다. 그러므로 본 연구에서는 정상 생쥐 (C57BL/6) 임신 기간 중 acyl-CoA synthetase 4 유전자의 발현을 확인하기 위하여 자궁, 난소, 태아에서 RT-PCR을 수행하였다. 또한 cPLA2, cyclooxygenase-1, cyclooxygenase-2 유전자의 발현 양상을 분석하여 eicosanoid 생산에 관여하는 유전자 상호간의 발현 을 확인하였다. acyl-CoA synthetase 4는 임신 0 day에서부터 19.5 day까지 자궁과 난소에서 모두 발현하고 있었다. 또한 5.5 day에서부터 19.5 day까지의 태아에서도 그 발현이 확인되었다. 그리고 cPLA2와 cyclooxygenase-1은 acyl-CoA synthetase 4와 유사한 양상을 보였으나 cyclooxygenase-2는 임신기간 중의 자궁, 난소, 태아에서 전혀 발현하지 않았다. 그러므로 임신 중 생쥐 자궁, 난소, 태아에 있어서 eicosanoid 생산에는 cPLA2, cyclooxygenase-1, acyl-CoA synthetase 4 유전자가 관여하고 있는 것으로 생각된다.

• Journal of The Korean Society of Inherited Metabolic disease
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• v.15 no.2
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• pp.98-100
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• 2015

Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is a rare mitochondrial fatty-acid oxidation disorder that is inherited as an autosomal recessive pattern. SCAD deficiency is caused by mutations in the ACADS gene (Acyl-CoA Dehydrogenase, Short-chain, OMIM #606885), which encodes SCAD, the mitochondrial enzyme that catalyzes the first reaction in the beta-oxidation of fatty acids four to six carbons in length. Here, we describe one Korean pediatric case of SCAD deficiency, which was diagnosed during newborn screening through tandem mass spectrometry. An increased concentration of butyrylcarnitine was detected on the newborn screening test, and the urine organic acid analysis showed increased urinary excretion of ethylmalonic acid. The patient has been asymptomatic and has shown normal growth and development by 8 months of age without any intervention during follow-up period.

• YAKHAK HOEJI
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• v.40 no.6
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• pp.713-719
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• 1996

Identification of soil microorganism strain B-6. a producer of acyl CoA synthetase inhibitor, based on its morphological, physiological, biochemical and chemotaxonomical charact eristics was performed. The strain B-6 was identified as Bacillus subtilis. Ihe acyl CoA synthetase inhibitor produced by this strain was highly achieved in fermentation medium that contained glucose 1.0%, soluble starch 1.0%, NH$_4$Cl 0.3%, oatmeal 1.0%, pharmamedia 1.0%, basic magnesium carbonate 0.5%. pH 7.5 at 30$^{\circ}$C for 7 days. The optimal pH and temperature for growth were 9.0 and 30$^{\circ}$C, respectively. Butanol extract of culture filterate of strain B-6 in acyl CoA synthetase inhibitor production medium containing corn steep liquor exhibited high acyl CoA synthetase inhibitor activity and antimicrobial activity against C. albicans. But chloroform extract of culture filterate of strain B-6 in medium containing NH$_4$Cl, ($NH_4)_2SO_4$ or urea instead of corn steep liquor exhibited higher antimicrobial activity against C. albicans than that of butanol extract.

• Reproductive and Developmental Biology
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• v.28 no.2
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• pp.89-94
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• 2004

This study was conducted to determine expression of acyl-CoA synthetase 4(ACS4), which is involved in converts arachidonic acid to postaglandins, in the mouse uterus during pregnancy. In arachidonic acid metabolism, acyl-CoA synthetase plays a key role in the esterification of free arachidonic acid into membrane phospholipids. Following its release by the action of calcium dependent phospholipases, free arachidonic acid is believed to be rapidly converted to arachidonoyl-CoA and reesterified into phospholipids in order to prevent excessive synthesis of prostaglandins. Here we demonstrate that ACS4 gene are differentially regulated in the peri-implatation mouse uterus. During the preimplantation period(days 0.5∼3.5), the ACS4 gene was expressed in the uterus until day 3.5 after which the expression was downregulated. The expression of cPLA2, COX1, and COX2 gene was similar to that of ACS4 gene in the preimplantation periods. However expression levels of COX1 gene show much variation on the various days of pregnancy examined. These data, suggest that ACS4 expression in preimplantation period is involved in initial attachment reaction with cPLA2, COX1, and COX2 gene.

• Journal of Microbiology and Biotechnology
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• v.28 no.4
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• pp.597-605
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• 2018

Acyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid ${\beta}$-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast Yarrowia lipolytica can utilize fatty acids as a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3 from Y. lipolytica (YlACOX3) was determined at a resolution of $2.5{\AA}$. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains; $N{\alpha}$, $N{\beta}$, $C{\alpha}1$, and $C{\alpha}2$ domains. The cofactor flavin adenine dinucleotide was bound in the dimer interface. The substrate-binding pocket was located near the cofactor, and formed at the interface between the $N{\alpha}$, $N{\beta}$, and $C{\alpha}1$ domains. Comparisons with other ACOX structures provided structural insights into how YlACOX has a substrate preference for short-chain acyl-CoA. In addition, the structure of YlACOX3 was compared with those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed.

• YAKHAK HOEJI
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• v.42 no.6
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• pp.552-557
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• 1998

Acyl CoA synthetase inhibitor, was purified from the culture broth of a Bacillus sp. B-6, which had been isolated from soil, by chloroform extract, silica gel column chro matography and preparative TLC. The purified acyl CoA synthetase inhibitor showed higher Antifungal activity against C. al-bicans (MIC: 8${\mu}$g/ml). Though the analysis of UV spectrum, melting point, IR spectrum, Mass-spectrum, $^1H$-NMR and $^{13}C$-NMR spectrum, the inhibitor could be identified as phenazine-l-carboxylic acid.

• Journal of The Korean Society of Inherited Metabolic disease
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• v.15 no.2
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• pp.93-97
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• 2015

Short-chain acyl-CoA dehydrogenase (SCAD) deficiency is an autosomal recessive hereditary metabolic disorder of mitochondrial fatty acid beta-oxidation. Mutations in the ACADS gene cause short-chain acyl-CoA dehydrogenase deficiency, which is characterized by developmental delay, hypotonia, seizure, and hypoglycemia. Here, we describe one Korean pediatric case of SCAD deficiency, which was diagnosed during newborn screening by tandem mass spectrometry and confirmed by molecular analysis. The level of C4 was typically elevated 5.23 mg/dL (reference range <1.5 mg/dL). This patient had a homozygous mutation [c.1031A>G, p. E344G] in ACADS. Therefore, we present a case of SCAD deficiency in an otherwise healthy neonate and her subsequent development and growth over four years.

• Korean Journal of Plant Tissue Culture
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• v.28 no.4
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• pp.201-204
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• 2001

Acyl-CoA binding proteins (ACBP) are small highly-conserved cytosolic proteins that bind long-chain acyl-CoAs. A cDNA encoding ACBP was identified from cDNA library constructed from hairy root poly $A^{＋}$ RNA in expressed sequence tags (EST) analysis. The cDNA clone was 453 bp long and carried an open reading frame of 264 bp (10 kDa). The ginseng ACBP amino acid sequence was compared with other reported plant ACBPs using the CLUSTALW. Ginseng ACBP is 89%, 81%, 80%, and 73% identical with ACBP from castor bean, lilly, Digitalis and Arabidopsis, respectively. However, ginseng ACBP is 5 amino acids smaller than Arabidopsis and rape seed ACBPs. Also there is no any known signal peptide sequence in ginseng ACBP.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.4
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• pp.958-962
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• 1999

Hydroxy methylglutaryl CoA(HMG CoA) reductase and acyl CoA:cholesterol acyltransferase(ACAT) are two important enzymes that are associated with regulation of cholesterol metabolism. The inhibitors of HMG CoA reductase and ACAT are very effective in lowering serum cholesterol in most animal species. In present study, various plant extracts with hot water were used to examine the inhibitory activities against HMG CoA reductase and ACAT that are involved in cholesterol biosynthesis and cholesterol esterification in tissues, respectively. The extracts of Fagophyrum rotundatum, Rosa multiflora, Rosa rugosa and Alisma orientalis exhibited significant inhibitory activities against the ACAT, 29%, 24%, 19%, and 18%, respectively. However the extracts of Typha augustifolia, Polygonum cuspidatum, Crataegus pinnatifida, Polygonum multiflorum inhibited the HMG CoA reductase activity by 53%, 42%, 37%, and 33% respectively. Results suggest that these plant extracts might play important roles in the regulation of the cholesterol metabolism in vivo.