4,4'-二脱辅基链孢红素 | 53872-50-7

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 中文名称: 4,4'-二脱辅基链孢红素
• 英文名称: 4,4'-Diaponeurosporene
• 英文别名: (4E,6E,8E,10E,12E,14E,16E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,4,6,8,10,12,14,16,18,22-decaene
• CAS: 53872-50-7
• 化学式: C₃₀H₄₂
• 分子量: 402.7
• InChiKey: FPSYVUBUILNSRF-MQMKOTMBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  11.8
• 重原子数：
  30
• 可旋转键数：
  11
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  0
• 氢给体数：
  0
• 氢受体数：
  0

反应信息

• 作为反应物：
  描述：

  4,4'-二脱辅基链孢红素 、 FAD 、 氢(+1)阳离子 生成 all-trans-4,4′-diapolycopene 、 10-[(2S,3S,4R)-5-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2,3,4-trihydroxypentyl]-7,8-dimethyl-5H-benzo[g]pteridine-2,4-diolate
  参考文献：
  名称：

  Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus

  摘要：

  金黄色葡萄球菌Newman产生的主要色素是深黄色的类胡萝卜素4,4'-diaponeurosporene；在长时间培养后，这种色素部分转化为橙色的终产物staphyloxanthin。从该菌株中鉴定出一个3.5 kb的DNA片段，将其克隆到大肠杆菌和肉毒桿菌中后，赋予了产生4,4'-diaponeurosporene的能力。对该片段的DNA序列分析发现了两个开放阅读框（ORFs），这两个ORFs很有可能是共同转录的。ORF1编码一个254氨基酸的疏水性蛋白质CrtM（M(r)，30,121）。CrtM的推导序列在三个领域与酿酒酵母和人类角鲨烷合酶以及各种细菌的类胡萝卜素合酶的序列相似。ORF2编码一个448氨基酸的疏水性蛋白质CrtN，其M(r)为50,853，其推导序列与其他细菌的类胡萝卜素脱氢酶的序列相似。在CrtN的N端发现了一个经典的FAD-，NAD(P)-结合域。大肠杆菌和肉毒桿菌的克隆体中包含ORF1或两个ORFs，经分光光度计和气相色谱质谱分析表明，ORF1和ORF2分别代表脱水角鲨烷合酶基因（crtM）和脱水角鲨烷脱饱和酶基因（crtN）。结果进一步表明，4,4'-diaponeurosporene的生物合成始于2个双萜磷酸分子的脱水角鲨烷合酶（CrtM）的缩合；表明该酶的反应产物是脱水角鲨烷而不是角鲨烷。脱水角鲨烷（4,4'-diapophytoene）被脱饱和酶（CrtN）连续脱氢，形成黄色的主要中间体4,4'-diaponeurosporene。

  DOI：

  10.1128/jb.176.24.7719-7726.1994
• 作为产物：
  描述：

  dehydrosqualene 、 FAD 、 氢(+1)阳离子 生成 4,4'-二脱辅基链孢红素 、 10-[(2S,3S,4R)-5-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2,3,4-trihydroxypentyl]-7,8-dimethyl-5H-benzo[g]pteridine-2,4-diolate
  参考文献：
  名称：

  4,4′-Diapophytoene Desaturase: Catalytic Properties of an Enzyme from the C ₃₀ Carotenoid Pathway of Staphylococcus aureus

  摘要：

  摘要 金黄色葡萄球菌 合成 C 30 类胡萝卜素。类胡萝卜素的形成需要引入三个双键，由一种酶催化。这种酶是来自金黄色葡萄球菌的 4,4′-二叶绿素去饱和酶。 金黄色葡萄球菌 在 大肠杆菌 通过亲和层析法一步纯化了该蛋白，并在底物特异性、辅助因子要求和寡聚化方面对其进行了表征。

  DOI：

  10.1128/jb.181.19.6184-6187.1999

文献信息

• Novel Carotenoid Oxidase Involved in Biosynthesis of 4,4′-Diapolycopene Dialdehyde
  作者：Luan Tao、Andreas Schenzle、J. Martin Odom、Qiong Cheng

  DOI：10.1128/aem.71.6.3294-3301.2005

  日期：2005.6

  but rather a novel carotenoid oxidase catalyzing oxidation of the terminal methyl group(s) of 4,4'-diaponeurosporene and 4,4'-diapolycopene to the corresponding terminal aldehyde. It has moderate to low activity on neurosporene and lycopene and no activity on beta-carotene or zeta-carotene. Using a combination of C(30) carotenoid synthesis genes from Staphylococcus and Methylomonas, 4,4'-diapolycopene

  在自然界中，C（30）类胡萝卜素的生物合成相对受到限制，但在葡萄球菌和甲基营养菌中已有描述。我们在这里报告鉴定涉及一个新的基因（crtNb）的4,4'-双聚番茄红素向4,4'-双聚番茄红素醛的转化。在甲基单胞菌中还鉴定出醛脱氢酶基因（ald），其负责随后将4,4'-双聚庚二烯醛氧化为4,4'-双聚庚二烯酸。CrtNb与泛二烯脱饱和酶（CrtN）具有显着的序列同源性。然而，从敲除crtNb和在大肠杆菌中表达crtNb的数据表明，CrtNb不是去饱和酶，而是一种新型的类胡萝卜素氧化酶，可催化4,4'-diaponeurosporene和4,4'-的末端甲基的氧化。双聚番茄红素对应的末端醛。它对神经孢子和番茄红素具有中等至低的活性，而对β-胡萝卜素或ζ-胡萝卜素没有活性。使用葡萄球菌和甲基单胞菌的C（30）类胡萝卜素合成基因的组合，在大肠杆菌中产生了4,4'-双聚二烯二醛作为主要类胡萝卜素。这种
• 4,4′-Diapophytoene Desaturase: Catalytic Properties of an Enzyme from the C ₃₀ Carotenoid Pathway of <i>Staphylococcus aureus</i>
  作者：Axel Raisig、Gerhard Sandmann

  DOI：10.1128/jb.181.19.6184-6187.1999

  日期：1999.10

  Staphylococcus aureus synthesizes C ₃₀ carotenoids. Their formation involves the introduction of three double bonds, which is catalyzed by a single enzyme. This enzyme, 4,4′-diapophytoene desaturase from S. aureus , was overexpressed in Escherichia coli and purified in one step by affinity chromatography, and then the protein was characterized with respect to substrate specificity, cofactor requirement, and oligomerization.

  摘要 金黄色葡萄球菌 合成 C 30 类胡萝卜素。类胡萝卜素的形成需要引入三个双键，由一种酶催化。这种酶是来自金黄色葡萄球菌的 4,4′-二叶绿素去饱和酶。 金黄色葡萄球菌 在 大肠杆菌 通过亲和层析法一步纯化了该蛋白，并在底物特异性、辅助因子要求和寡聚化方面对其进行了表征。
• Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus
  作者：B Wieland、C Feil、E Gloria-Maercker、G Thumm、M Lechner、J M Bravo、K Poralla、F Götz

  DOI：10.1128/jb.176.24.7719-7726.1994

  日期：1994.12

  The major pigment produced by Staphylococcus aureus Newman is the deep-yellow carotenoid 4,4'-diaponeurosporene; after prolonged cultivation, this pigment is in part converted to the orange end product staphyloxanthin. From this strain a 3.5-kb DNA fragment was identified which after being cloned into Escherichia coli and Staphylococcus carnosus conferred the ability to produce 4,4'-diaponeurosporene. DNA sequencing of this fragment revealed two open reading frames (ORFs) which are very likely cotranscribed. ORF1 encodes a 254-amino-acid hydrophobic protein, CrtM (M(r), 30,121). The deduced sequence of CrtM exhibits in three domains similarities to the sequences of Saccharomyces cerevisiae and human squalene synthases and phytoene synthases of various bacteria. ORF2 encodes a 448-amino-acid hydrophobic protein, CrtN, with an M(r) of 50,853 whose deduced sequence is similar to those of phytoene desaturases of other bacteria. At the N terminus of CrtN a classical FAD-, NAD(P)-binding domain is found. Spectrophotometry and gas chromatography-mass spectrometry analyses of the carotenoid production of E. coli and S. carnosus clones containing either ORF1 or both ORFs together suggest that ORF1 and ORF2 represent the dehydrosqualene synthase gene (crtM) and the dehydrosqualene desaturase gene (crtN), respectively. The results furthermore suggest that the biosynthesis of 4,4'-diaponeurosporene starts with the condensation of two molecules of farnesyl diphosphate by dehydrosqualene synthase (CrtM); it is shown that the reaction product of this enzyme is dehydrosqualene and not squalene. Dehydrosqualene (4,4'-diapophytoene) is successively dehydrogenated by a desaturase (CrtN) to form the yellow main intermediate 4,4'-diaponeurosporene.

  金黄色葡萄球菌Newman产生的主要色素是深黄色的类胡萝卜素4,4'-diaponeurosporene；在长时间培养后，这种色素部分转化为橙色的终产物staphyloxanthin。从该菌株中鉴定出一个3.5 kb的DNA片段，将其克隆到大肠杆菌和肉毒桿菌中后，赋予了产生4,4'-diaponeurosporene的能力。对该片段的DNA序列分析发现了两个开放阅读框（ORFs），这两个ORFs很有可能是共同转录的。ORF1编码一个254氨基酸的疏水性蛋白质CrtM（M(r)，30,121）。CrtM的推导序列在三个领域与酿酒酵母和人类角鲨烷合酶以及各种细菌的类胡萝卜素合酶的序列相似。ORF2编码一个448氨基酸的疏水性蛋白质CrtN，其M(r)为50,853，其推导序列与其他细菌的类胡萝卜素脱氢酶的序列相似。在CrtN的N端发现了一个经典的FAD-，NAD(P)-结合域。大肠杆菌和肉毒桿菌的克隆体中包含ORF1或两个ORFs，经分光光度计和气相色谱质谱分析表明，ORF1和ORF2分别代表脱水角鲨烷合酶基因（crtM）和脱水角鲨烷脱饱和酶基因（crtN）。结果进一步表明，4,4'-diaponeurosporene的生物合成始于2个双萜磷酸分子的脱水角鲨烷合酶（CrtM）的缩合；表明该酶的反应产物是脱水角鲨烷而不是角鲨烷。脱水角鲨烷（4,4'-diapophytoene）被脱饱和酶（CrtN）连续脱氢，形成黄色的主要中间体4,4'-diaponeurosporene。
• Functional Expression and Extension of Staphylococcal Staphyloxanthin Biosynthetic Pathway in Escherichia coli
  作者：Se Hyeuk Kim、Pyung Cheon Lee

  DOI：10.1074/jbc.m112.343020

  日期：2012.6

  The biosynthetic pathway for staphyloxanthin, a C-30 carotenoid biosynthesized by Staphylococcus aureus, has previously been proposed to consist of five enzymes (CrtO, CrtP, CrtQ, CrtM, and CrtN). Here, we report a missing sixth enzyme, 4,4'-diaponeurosporen-aldehyde dehydrogenase (AldH), in the staphyloxanthin biosynthetic pathway and describe the functional expression of the complete staphyloxanthin biosynthetic pathway in Escherichia coli. When we expressed the five known pathway enzymes through artificial synthetic operons and the wild-type operon (crtOPQMN) in E. coli, carotenoid aldehyde intermediates such as 4,4'-diaponeurosporen-4-al accumulated without being converted into staphyloxanthin or other intermediates. We identified an aldH gene located 670 kilobase pairs from the known staphyloxanthin gene cluster in the S. aureus genome and an aldH gene in the non-staphyloxanthin-producing Staphylococcus carnosus genome. These two putative enzymes catalyzed the missing oxidation reaction to convert 4,4'-diaponeurosporen-4-al into 4,4'-diaponeurosporenoic acid in E. coli. Deletion of the aldH gene in S. aureus abolished staphyloxanthin biosynthesis and caused accumulation of 4,4'-diaponeurosporen-4-al, confirming the role of AldH in staphyloxanthin biosynthesis. When the complete staphyloxanthin biosynthetic pathway was expressed using an artificial synthetic operon in E. coli, staphyloxanthin-like compounds, which contained altered fatty acid acyl chains, and novel carotenoid compounds were produced, indicating functional expression and coordination of the six staphyloxanthin pathway enzymes.
• Carotenoid production in Bacillus subtilis achieved by metabolic engineering
  作者：Kazuyuki Yoshida、Shunsaku Ueda、Isamu Maeda

  DOI：10.1007/s10529-009-0082-6

  日期：2009.11

  The carotenoid synthetic genes, crtM and crtN, derived from Staphylococcus aureus, were introduced into B. subtilis, resulting in yellow pigmentation. Absorption maxima of pigments and MALDI-TOF mass spectrometry demonstrated that the pigmented strain accumulated two C-30 carotenoids, 4,4'-diapolycopene and 4,4'-diaponeurosporene. A survival test using H2O2 revealed that the pigmented strain was more resistant to oxidative stress than the strain harboring an empty-vector. These findings indicate that B. subtilis can produce carotenoids, and the strain accumulating the carotenoids, CarotenoBacillus, will become a basal host for production of C-30 carotenoids and evaluation of their antioxidative effects.