Cadaverine(2+)

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: Cadaverine(2+)
• 英文别名: 5-azaniumylpentylazanium
• 化学式: C5H16N2+2
• 分子量: 104.19
• InChiKey: VHRGRCVQAFMJIZ-UHFFFAOYSA-P

计算性质

• 辛醇/水分配系数(LogP)：
  -0.6
• 重原子数：
  7
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  55.3
• 氢给体数：
  2
• 氢受体数：
  0

反应信息

• 作为反应物：
  描述：

  2-氧代-戊二酸离子(2-) 、 Cadaverine(2+) 生成 5-Ammoniopentanal 、 2-氨基戊二酸酯
  参考文献：
  名称：

  广泛的细菌赖氨酸降解通过戊二酸和L-2-羟基戊二酸进行。

  摘要：

  在包括大肠杆菌在内的许多生物中，赖氨酸的降解仍然难以捉摸。在这里，我们报道赖氨酸在大肠杆菌中的分解代谢为琥珀酸酯，涉及谷氨酸和L-2-羟基谷氨酸作为中间体。我们表明CsiD充当α-酮戊二酸依赖性双加氧酶，催化将戊二酸羟化为L-2-羟基戊二酸。发现CsiD广泛存在于细菌中。我们提出了与谷氨酸，琥珀酸酯和抑制剂N-草酰甘氨酸复合的CsiD晶体结构，证明了结构上相关配体之间的强烈区别。我们显示L-2-羟基戊二酸通过LhgO转变为α-酮戊二酸，作为膜结合的，泛醌连接的脱氢酶。赖氨酸通过混杂酶GabT和GabD通过5-氨基戊酸酯进入途径。我们证明了谷氨酸结合后，CsiR途径的抑制作用得以缓解。总之，赖氨酸的降解提供了中枢代谢的重要环节。我们的结果暗示肠道微生物组是与人类疾病（例如癌症和有机酸尿症）相关的谷氨酸和L-2-羟基谷氨酸的潜在来源。

  DOI：

  10.1038/s41467-018-07563-6
• 作为产物：
  描述：

  水 、 N-acetylcadaverine(1+) 生成 乙酸盐 、 Cadaverine(2+)
  参考文献：
  名称：

  Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa

  摘要：

  lation酶解作用。

  DOI：

  10.1186/s12858-016-0063-z

文献信息

• <scp>l</scp> -Lysine Catabolism Is Controlled by <scp>l</scp> -Arginine and ArgR in <i>Pseudomonas aeruginosa</i> PAO1
  作者：Han Ting Chou、Mohamed Hegazy、Chung-Dar Lu

  DOI：10.1128/jb.00673-10

  日期：2010.11.15

  In comparison to other pseudomonads, Pseudomonas aeruginosa grows poorly in l -lysine as a sole source of nutrient. In this study, the ldcA gene ( l ysine d e c arboxylase A ; PA1818), previously identified as a member of the ArgR regulon of l -arginine metabolism, was found essential for l -lysine catabolism in this organism. LdcA was purified to homogeneity from a recombinant strain of Escherichia coli , and the results of enzyme characterization revealed that this pyridoxal-5-phosphate-dependent decarboxylase takes l -lysine, but not l -arginine, as a substrate. At an optimal pH of 8.5, cooperative substrate activation by l -lysine was depicted from kinetics studies, with calculated K _m and V _max values of 0.73 mM and 2.2 μmole/mg/min, respectively. Contrarily, the ldcA promoter was induced by exogenous l -arginine but not by l -lysine in the wild-type strain PAO1, and the binding of ArgR to this promoter region was demonstrated by electromobility shift assays. This peculiar arginine control on lysine utilization was also noted from uptake experiments in which incorporation of radioactively labeled l -lysine was enhanced in cells grown in the presence of l -arginine but not l -lysine. Rapid growth on l -lysine was detected in a mutant devoid of the main arginine catabolic pathway and with a higher basal level of the intracellular l -arginine pool and hence elevated ArgR-responsive regulons, including ldcA . Growth on l -lysine as a nitrogen source can also be enhanced when the aruH gene encoding an arginine/lysine:pyruvate transaminase was expressed constitutively from plasmids; however, no growth of the ldcA mutant on l -lysine suggests a minor role of this transaminase in l -lysine catabolism. In summary, this study reveals a tight connection of lysine catabolism to the arginine regulatory network, and the lack of lysine-responsive control on lysine uptake and decarboxylation provides an explanation of l -lysine as a poor nutrient for P. aeruginosa .

  摘要 与其他假单胞菌相比 铜绿假单胞菌 在 l -赖氨酸作为唯一营养源的情况下生长不良。在这项研究中 ldcA 基因（ l 赖氨酸 d e c 羧化酶 A 的 ArgR 调节子的成员。 l -精氨酸代谢所必需。 l -赖氨酸代谢所必需。LdcA 从一株重组的 大肠杆菌 酶鉴定结果表明，这种依赖于 5-磷酸吡哆醛的脱羧酶以 l -赖氨酸，而不是 l -精氨酸作为底物。在最佳 pH 值为 8.5 时，由 l -赖氨酸对底物的协同活化作用。 K m 和 V 最大 分别为 0.73 mM 和 2.2 μmole/mg/min 。相反，ldcA ldcA 启动子被外源 l -精氨酸而不是 l 在野生型菌株 PAO1 中，ldcA 启动子受外源 l -精氨酸的诱导，而不受 l -赖氨酸的诱导，电迁移实验证明了 ArgR 与该启动子区域的结合。这种对赖氨酸利用的特殊精氨酸控制也是从吸收实验中发现的。 l -赖氨酸的吸收增强。 l -精氨酸而非 l -赖氨酸。在 l -赖氨酸的快速生长。 l -精氨酸池，因此 ArgR 响应调节子（包括 ldcA .在 l -赖氨酸作为氮源时，生长也会增强。 aruH 编码精氨酸/赖氨酸：丙酮酸转氨酶的基因由质粒组成型表达时，也能促进其生长；但ldcA ldcA 突变体在 l -然而，ldcA 突变体在赖氨酸上没有生长。 l -赖氨酸代谢中的次要作用。总之，这项研究揭示了赖氨酸分解代谢与精氨酸调控网络之间的紧密联系，赖氨酸摄取和脱羧缺乏赖氨酸响应控制，这为赖氨酸分解代谢和精氨酸调控网络提供了解释。 l -赖氨酸对铜绿微囊藻来说是一种贫乏的营养物质。 铜绿微囊藻 .
• The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme.
  作者：Yoshihiro Yamamoto、Yoshihiro Miwa、Keiko Miyoshi、Jun-ichi Furuyama、Haruo Ohmori

  DOI：10.1266/ggs.72.167

  日期：——

  A gene (designated ldcC) mapped at 4.6 min on the Escherichia coli chromosome codes for a protein of 713 amino acids (aa) that shows strong similarities in both size and amino-acid sequence (69% identical residues and 85% conserved residues) to lysine decarboxylase (LDC) from E. coli (CadA, acid-inducible LDC, 715 aa) or from Hafnia alvei (739 aa). A pUC18 derivative carrying the ldcC gene conferred high LDC activities on an E. coli strain devoid of the functional cadA gene, even when the bacteria were grown under non-inducing conditions at physiological pH. Thus, the gene encodes another lysine decarboxylase, probably a constitutively expressed enzyme, the presence of which was suggested from the previous observations that low LDC activities were detectable in cadA- mutant and non-induced wild-type cells.

  大肠杆菌染色体上4.6分钟处的一个基因（命名为ldcC）编码一种713个氨基酸（aa）的蛋白质，该蛋白质在大肠杆菌赖氨酸脱羧酶（LDC）（CadA，酸诱导型LDC，715个氨基酸）或Hafnia alvei（739个氨基酸）中，在大小和氨基酸序列上均表现出很强的相似性（69%相同的残基和85%保守的残基）。携带ldcC基因的pUC18衍生物赋予大肠杆菌菌株高LDC活性，即使细菌在生理pH值下非诱导条件下生长也是如此。因此，该基因编码另一种赖氨酸脱羧酶，可能是一种恒定表达的酶，其存在从之前的观察中可以看出，在cadA突变体和非诱导型野生型细胞中可以检测到低LDC活性。
• Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme
  作者：K Sakurada、T Ohta、K Fujishiro、M Hasegawa、K Aisaka

  DOI：10.1128/jb.178.19.5781-5786.1996

  日期：1996.10

  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. The aphA gene was subcloned under the control of the trc promoter and was expressed in Escherichia coli MM294. The recombinant enzyme was purified, and the enzymatic properties were characterized. Substrate specificities, Km values, and Vmax values were identical to those of the native enzyme purified from M. ramosa. In the analysis of the metal-substituted enzymes, we found that the acid limb of pH rate profiles shifts from 7.2 for the original zinc enzyme to 6.6 for the cobalt enzyme. This change suggests that the zinc atom is essential for the catalytic activity of the enzyme similarly to the zinc atom in carboxypeptidase A.

  我们已经克隆了一个来自Mycoplana ramosa ATCC 49678（之前被称为Mycoplana bullata）的编码乙酰多胺酰胺水解酶的基因（aphA）。使用从M. ramosa中纯化的酶N末端氨基酸序列设计的寡核苷酸探针筛选了M. ramosa的基因组文库。核苷酸序列分析揭示了一个长1023个碱基的开放阅读框架，编码一个分子量为36,337 Da的多肽。这是有关乙酰多胺酰胺水解酶结构的首次报道。aphA基因在trc启动子的控制下亚克隆，并在大肠杆菌MM294中表达。重组酶被纯化，并对其酶学性质进行了表征。底物特异性，Km值和Vmax值与从M. ramosa中纯化的天然酶相同。在金属替代酶的分析中，我们发现pH速率曲线的酸性端从原始锌酶的7.2转移到钴酶的6.6。这种变化表明锌原子对于酶的催化活性至关重要，类似于羧肽酶A中的锌原子。
• Dual Biosynthesis Pathway for Longer-Chain Polyamines in the Hyperthermophilic Archaeon <i>Thermococcus kodakarensis</i>
  作者：Nanako Morimoto、Wakao Fukuda、Nanami Nakajima、Takeaki Masuda、Yusuke Terui、Tamotsu Kanai、Tairo Oshima、Tadayuki Imanaka、Shinsuke Fujiwara

  DOI：10.1128/jb.00279-10

  日期：2010.10

  Long-chain and/or branched-chain polyamines are unique polycations found in thermophiles. Cytoplasmic polyamines were analyzed for cells cultivated at various growth temperatures in the hyperthermophilic archaeon Thermococcus kodakarensis. Spermidine [34] and N ⁴ -aminopropylspermine [3(3)43] were identified as major polyamines at 60°C, and the amounts of N ⁴ -aminopropylspermine [3(3)43] increased as the growth temperature rose. To identify genes involved in polyamine biosynthesis, a gene disruption study was performed. The open reading frames (ORFs) TK0240, TK0474, and TK0882, annotated as agmatine ureohydrolase genes, were disrupted. Only the TK0882 gene disruptant showed a growth defect at 85°C and 93°C, and the growth was partially retrieved by the addition of spermidine. In the TK0882 gene disruptant, agmatine and N ¹ -aminopropylagmatine accumulated in the cytoplasm. Recombinant TK0882 was purified to homogeneity, and its ureohydrolase characteristics were examined. It possessed a 43-fold-higher k _cat / K _m value for N ¹ -aminopropylagmatine than for agmatine, suggesting that TK0882 functions mainly as N ¹ -aminopropylagmatine ureohydrolase to produce spermidine. TK0147, annotated as spermidine/spermine synthase, was also studied. The TK0147 gene disruptant showed a remarkable growth defect at 85°C and 93°C. Moreover, large amounts of agmatine but smaller amounts of putrescine accumulated in the disruptant. Purified recombinant TK0147 possessed a 78-fold-higher k _cat / K _m value for agmatine than for putrescine, suggesting that TK0147 functions primarily as an aminopropyl transferase to produce N ¹ -aminopropylagmatine. In T. kodakarensis , spermidine is produced mainly from agmatine via N ¹ -aminopropylagmatine. Furthermore, spermine and N ⁴ -aminopropylspermine were detected in the TK0147 disruptant, indicating that TK0147 does not function to produce spermine and long-chain polyamines.

  摘要 长链和/或支链多胺是嗜热菌中特有的多阳离子。研究人员分析了在不同生长温度下培养的嗜热古细菌细胞质多胺。 Thermococcus kodakarensis 的细胞质多胺进行了分析。 精胺 [34] 和 N 4 -氨丙基精胺[3(3)43]被确定为 60°C 时的主要多胺，N. N 4 -氨基丙基精胺 [3(3)43] 的含量随着生长温度的升高而增加。为了确定参与多胺生物合成的基因，进行了基因干扰研究。开放阅读框（ORF）TK0240、TK0474 和 TK0882 被注释为琼脂糖脲水解酶基因。只有 TK0882 基因干扰物在 85°C 和 93°C 温度下出现生长缺陷，加入亚精胺后可部分恢复生长。在 TK0882 基因干扰株中，苦参碱和 N 1 -氨丙基巴马汀在细胞质中积累。对重组 TK0882 进行了纯化，并检测了它的脲水解酶特性。它的 k cat / K m 值为 N 1 -氨基丙基巴马汀的 m 值高于对阿加巴汀的 m 值，这表明 TK0882 的功能主要是作为 N 1 -氨丙基巴马汀脲水解酶来产生精胺。此外，还研究了被注释为精胺/精胺合成酶的 TK0147。TK0147 基因干扰物在 85°C 和 93°C 的温度下表现出明显的生长缺陷。此外，在该基因干扰株中积累了大量的矢车菊碱，而少量的腐胺碱。纯化的重组 TK0147 的 k cat / K m 值，表明TK0147主要作为氨丙基转移酶来产生 N 1 -氨丙基巴马汀。在 中 中，精胺主要由矢车菊碱通过 N 1 -氨基丙基巴马汀生成。此外，精胺和 N 4 -氨丙基精胺，这表明 TK0147 不具有产生精胺和长链多胺的功能。
• The First Agmatine/Cadaverine Aminopropyl Transferase: Biochemical and Structural Characterization of an Enzyme Involved in Polyamine Biosynthesis in the Hyperthermophilic Archaeon <i>Pyrococcus furiosus</i>
  作者：Giovanna Cacciapuoti、Marina Porcelli、Maria Angela Moretti、Francesca Sorrentino、Luigi Concilio、Vincenzo Zappia、Zhi-Jie Liu、Wolfram Tempel、Florian Schubot、John P. Rose、Bi-Cheng Wang、Phillip S. Brereton、Francis E. Jenney、Michael W. W. Adams

  DOI：10.1128/jb.00151-07

  日期：2007.8.15

  here the characterization of the first agmatine/cadaverine aminopropyl transferase (ACAPT), the enzyme responsible for polyamine biosynthesis from an archaeon. The gene PF0127 encoding ACAPT in the hyperthermophile Pyrococcus furiosus was cloned and expressed in Escherichia coli, and the recombinant protein was purified to homogeneity. P. furiosus ACAPT is a homodimer of 65 kDa. The broad substrate specificity

  我们在这里报告第一个胍丁胺/尸胺氨基丙基转移酶（ACAPT）的特性，该酶负责从古细菌中合成多胺。克隆了嗜热热球菌中编码ACAPT的基因PF0127，并在大肠杆菌中表达，并将重组蛋白纯化至同质。强烈假单胞菌ACAPT是65kDa的同型二聚体。酶对胺受体的广泛的底物特异性是独特的，因为胍丁胺，1，3-二氨基丙烷，腐胺，尸胺和顺反-亚精胺都可以作为底物。尽管尸胺具有最大的催化活性，但基于k（cat）/ K（m）值，胍丁胺是优选的底物。P. furiosus ACAPT具有热活性和热稳定性，表观熔融温度为108摄氏度，在尸胺的存在下会升高至112摄氏度。有限的蛋白水解表明唯一的蛋白水解切割位点位于C-末端区域，并且C-末端肽对于活性位点的完整性不是必需的。确定为1.8-A分辨率的酶的晶体结构证实了其二聚体性质，并提供了对蛋白水解分析以及热稳定性机制的深入了解。对P. furiosus的多胺含量的分