乙酰基-BETA-内啡肽(人) | 80102-04-1

• 物质功能分类: 生物化工 - 多肽
• 中文名称: 乙酰基-BETA-内啡肽(人)
• 中文别名: 乙酰基-beta-内啡肽(人)
• 英文名称: N-(4-Amino-1-carboxybutyl)-3-carboxypropanimidate
• 英文别名: N-[(1S)-4-amino-1-carboxybutyl]-4-hydroxy-4-oxobutanimidate
• CAS: 80102-04-1
• 化学式: C9H15N2O5-
• 分子量: 231.23
• InChiKey: VWXQFHJBQHTHMK-LURJTMIESA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.6
• 重原子数：
  16
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  137
• 氢给体数：
  2
• 氢受体数：
  5

安全信息

• WGK Germany：
  3

反应信息

• 作为反应物：
  描述：

  2-氧代-戊二酸离子(2-) 、 乙酰基-BETA-内啡肽(人) 生成 2-氨基戊二酸酯 、 N-succinyl-L-glutamic 5-semialdehyde(2-)
  参考文献：
  名称：

  Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia

  摘要：

  翻译结果如下：

  Pseudomonas cepacia NCTC 10743利用精氨酸作为唯一的碳和氮源进行生长。精氨酸通过琥珀酰衍生物降解为谷氨酸。该途径中的分解序列为L-精氨酸----N2-琥珀酰精氨酸----N2-琥珀酰鸟氨酸----N2-琥珀酰谷氨酰半胱氨酸----N2-琥珀酰谷氨酸----谷氨酸+琥珀酸。负责精氨酸降解的酶的形成不仅受到诱导的调控，还受到碳和氮代谢抑制的调控。

  DOI：

  10.1128/jb.164.2.882-886.1985
• 作为产物：
  描述：

  L-ornithinium(1+) 、 succinyl-CoA(5-) 生成 coenzyme A 、 氢(+1)阳离子 、 乙酰基-BETA-内啡肽(人)
  参考文献：
  名称：

  Purification and Properties of a Succinyltransferase from Pseudomonas aeruginosa Specific for both Arginine and Ornithine

  摘要：

  The arginine and ornithine succinyltransferase from Pseudomonas aeruginosa, a bifunctional enzyme involved in the aerobic utilization of arginine and ornithine, has been purified to homogeneity. The apparent molecular mass of the native enzyme was 150 kDa by gel filtration and 140 kDa by polyacrylamide gel electrophoresis under non‐denaturing conditions. After SDS/PAGE two subunits of 35 kDa and 37 kDa were evident, indicating that the enzyme is a heterotetramer. Microsequence analysis of the electroblotted protein bands gave two different but well‐conserved N‐terminal amino acid sequences.The l‐arginine saturation curve followed Henri‐Michaelis kinetics with an apparent Km value of 0.5 mM. The sigmoidal saturation curve for l‐ornithine indicated allosteric behaviour. d‐Arginine, a competitive inhibitor with respect to l‐arginine, reduced l‐ornithine cooperativity. In the presence of spermidine, the l‐ornithine saturation curve became increasingly sigmoidal, the Hill coefficient shifting from 2.5 in the absence of the inhibitor, to 3.5 in the presence of 20 mM spermidine. The l‐arginine analog, l‐homoarginine, was also a substrate of the succinyltransferase, and the saturation of the enzyme by this substrate was also cooperative. All these data confirmed the allosteric nature of the enzyme. Moreover, a mutant growing faster on l‐ornithine than the parent strain had a modified succinyltransferase with a reduced l‐ornithine cooperativity.The fate of l‐homoarginine was different depending on whether the succinyltransferase was induced or not; excreted succinylhomoarginine was found in cultures induced for the transferase activity whereas guanidinovalerate was excreted in non‐induced cultures. The ‘waste’ of succinyl CoA, which could not be regenerated from the excreted succinylhomoarginine, explained the inhibition exerted by l‐homoarginine on growth when ornithine or arginine was used as the growth medium.

  DOI：

  10.1111/j.1432-1033.1994.00853.x

文献信息

• Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa
  作者：Y Itoh

  DOI：10.1128/jb.179.23.7280-7290.1997

  日期：1997.12

  The arginine succinyltransferase (AST) pathway is the major arginine and ornithine utilization (aru) pathway under aerobic conditions in Pseudomonas aeruginosa. A 26-kb DNA fragment of the P. aeruginosa PAO1 chromosome carrying the regulatory argR gene and the aru structural gene cluster was cloned. Complementation tests and nucleotide sequence data established the locations of the argR, aruC, aruF, aruG, aruD, aruB, and aruE genes, in that order. The aruR, aruC, aruD, aruB, and aruE genes specify the ArgR regulatory protein, N2-succinylornithine 5-aminotransferase, N-succinylglutamate 5-semialdehyde dehydrogenase, N2-succinylarginine dihydrolase, and N-succinylglutamate desuccinylase, respectively, and the aruF and aruG genes encode the subunits (AruAI and AruAII) of arginine and ornithine N2-succinyltransferases. Furthermore, in vivo analysis of transcriptional aru fusions and of polar insertion mutations located at different sites in the aru cluster indicated the presence of three transcriptional units which are controlled by ArgR. The aruCFGDB genes appear to form an operon transcribed from a promoter upstream of aruC, whereas aruE has its own promoter. The argR gene, which is located upstream of the aruCFGDB operon, is a member of another (aot) operon coding for arginine transport genes. The deduced amino acid sequences of the AST enzymes were compared to those of homologous proteins of Escherichia coli specified by the ast genes lying in the chromosome region from 39.2 to 39.5 min (Kohara clone 327; GenBank/EMBL/DDJB accession no. D90818). The overall organization of the aru and ast genes in both organisms is similar, with the exception that E. coli appears to have a single AST gene.

  辅酶A精氨酸琥珀酰转移酶（AST）途径是铜绿假单胞菌在有氧条件下的主要精氨酸和鸟氨酸利用（aru）途径。克隆了Pseudomonas aeruginosa PAO1染色体的26 kb DNA片段，其中包含调节基因argR和aru结构基因簇。补充试验和核苷酸序列数据确定了argR、aruC、aruF、aruG、aruD、aruB和aruE基因的位置，顺序为上述。aruR、aruC、aruD、aruB和aruE基因指定了ArgR调节蛋白、N2-琥珀酰鸟氨酸5-氨基转移酶、N-琥珀酰谷氨酸5-半醛脱氢酶、N2-琥珀酰精氨酸双氢酶和N-琥珀酰谷氨酸脱琥珀酰酶，aruF和aruG基因编码精氨酸和鸟氨酸N2-琥珀酰转移酶的亚基（AruAI和AruAII）。此外，对位于aru簇不同位点的极性插入突变和转录aru融合体的体内分析表明，存在由ArgR控制的三个转录单元。aruCFGDB基因似乎形成一个从aruC上游启动子转录的operon，而aruE有自己的启动子。位于aruCFGDB operon上游的argR基因是编码精氨酸转运基因的另一个（aot）operon的成员。将AST酶的推导氨基酸序列与Escherichia coli中的aST基因指定的同源蛋白质进行比较，后者位于39.2到39.5分钟的染色体区域（Kohara clone 327; GenBank/EMBL/DDJB accession no. D90818）。两种生物中aru和aST基因的整体组织相似，唯一的区别是E. coli似乎只有单个AST基因。
• Arginine Catabolism and the Arginine Succinyltransferase Pathway in <i>Escherichia coli</i>
  作者：Barbara L. Schneider、Alexandros K. Kiupakis、Lawrence J. Reitzer

  DOI：10.1128/jb.180.16.4278-4286.1998

  日期：1998.8.15

  Arginine catabolism produces ammonia without transferring nitrogen to another compound, yet the only known pathway of arginine catabolism in Escherichia coli (through arginine decarboxylase) does not produce ammonia. Our aims were to find the ammonia-producing pathway of arginine catabolism in E. coli and to examine its function. We showed that the only previously described pathway of arginine catabolism

  精氨酸分解代谢产生氨而没有将氮转移到另一种化合物中，但是大肠杆菌中精氨酸分解代谢的唯一已知途径（通过精氨酸脱羧酶）不会产生氨。我们的目标是找到大肠杆菌中精氨酸分解代谢的产氨途径，并检查其功能。我们表明，先前描述的精氨酸分解代谢的唯一途径（不产生氨）仅占精氨酸消耗量的3％。寻找另一种精氨酸分解代谢途径导致在大肠杆菌中发现产生氨的精氨酸琥珀酰转移酶（AST）途径。氮限制在大肠杆菌和产气克雷伯氏菌中都诱导了该途径，但是在这两种生物中，激活机制明显不同。我们确定了E。琥珀酸鸟氨酸氨基转移酶的大肠杆菌基因，是AST途径的第三个酶，它似乎是aSTCADBE操纵子的第一个。它的破坏阻止了精氨酸的分解代谢，削弱了鸟氨酸的利用，并影响了AST途径中所有酶的合成。破坏aSTB消除了琥珀酰精氨酸二水解酶的活性并阻止了精氨酸的利用，但并未损害鸟氨酸的分解代谢。AST酶的过量生产导致精氨酸和天冬氨酸的生长更快。我们
• Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria
  作者：V. STALON、C. VANDER WAUVEN、P. MOMIN、C. LEGRAIN

  DOI：10.1099/00221287-133-9-2487

  日期：1987.9.1

  SUMMARY: The distribution of the arginine succinyltransferase pathway was examined in representative strains of Pseudomonas and related bacteria able to use arginine as the sole carbon and nitrogen source for growth. The arginine succinyltransferase pathway was induced in arginine-grown cells. The accumulation of succinylornithine following in vivo inhibition of succinylornithine transaminase activity by aminooxyacetic acid showed that this pathway is responsible for the dissimilation of the carbon skeleton of arginine. Catabolism of citrulline as a carbon source was restricted to relatively few of the organisms tested. In P. putida, P. cepacia and P. indigofera, ornithine was the main product of citrulline degradation. In most strains which possessed the arginine succinyltransferase pathway, the first step of ornithine utilization as a carbon source was the conversion of ornithine into succinylornithine through an ornithine succinyltransferase. However P. cepacia and P. putida used ornithine by a pathway which proceeded via proline as an intermediate and involved an ornithine cyclase activity.

  摘要：研究了精氨酸琥珀酰基转移酶途径在假单胞菌和相关细菌代表性菌株中的分布情况，这些菌株能够利用精氨酸作为生长的唯一碳源和氮源。在精氨酸生长的细胞中诱导了精氨酸琥珀酰基转移酶途径。氨基氧乙酸在体内抑制琥珀酰鸟氨酸转氨酶活性后，琥珀酰鸟氨酸的积累表明，该途径负责精氨酸碳骨架的分解。瓜氨酸作为碳源的分解代谢仅限于相对较少的受试生物。在 P. putida、P. cepacia 和 P. indigofera 中，鸟氨酸是瓜氨酸降解的主要产物。在大多数具有精氨酸琥珀酰基转移酶途径的菌株中，鸟氨酸作为碳源利用的第一步是通过鸟氨酸琥珀酰基转移酶将鸟氨酸转化为琥珀酰鸟氨酸。而epacia 和 putida 利用鸟氨酸的途径是以脯氨酸为中间体，并涉及鸟氨酸环化酶活性。
• A single mutation in the active site swaps the substrate specificity of<i>N</i>-acetyl-L-ornithine transcarbamylase and<i>N</i>-succinyl-L-ornithine transcarbamylase
  作者：Dashuang Shi、Xiaolin Yu、Juan Cabrera-Luque、Tony Y. Chen、Lauren Roth、Hiroki Morizono、Norma M. Allewell、Mendel Tuchman

  DOI：10.1110/ps.072919907

  日期：2007.8

  Transcarbamylases catalyze the transfer of the carbamyl group from carbamyl phosphate (CP) to an amino group of a second substrate such as aspartate, ornithine, or putrescine. Previously, structural determination of a transcarbamylase from Xanthomonas campestris led to the discovery of a novel N-acetylornithine transcarbamylase (AOTCase) that catalyzes the carbamylation of N-acetylornithine. Recently

  转氨甲酰酶催化氨基甲酸酯基团从氨基甲酸酯磷酸酯（CP）转移到第二种底物如天冬氨酸，鸟氨酸或腐胺上的氨基。以前，对来自油菜黄单胞菌（Xanthomonas campestris）的转氨酶的结构测定导致发现了新型的N-乙酰鸟氨酸转氨酶（AOTCase），其催化N-乙酰鸟氨酸的氨甲酰化作用。最近，鉴定了一种来自脆弱拟杆菌（Bacteroides fragilis）的新型N-琥珀酰鸟氨酸转氨甲酰酶（SOTCase）。结构的比较，来自X. campestris的AOTCase和来自脆弱的芽孢杆菌的SOTCase，表明残基Glu92（X。campestris编号）在区分AOTCase和SOTCase方面起着关键作用。AOTCase的E92P，E92S，E92V和E92A突变体的酶促测定表明，这些突变均将AOTCase转化为SOTCase。同样，脆弱型芽孢杆菌SOTCase中的P90E突变（相当于X. campestris
• Crystal Structure of N-Succinylarginine Dihydrolase AstB, Bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli
  作者：Ante Tocilj、Joseph D. Schrag、Yunge Li、Barbara L. Schneider、Larry Reitzer、Allan Matte、Miroslaw Cygler

  DOI：10.1074/jbc.m413833200

  日期：2005.4

  The ammonia-producing arginine succinyltransferase pathway is the major pathway in Escherichia coli and related bacteria for arginine catabolism as a sole nitrogen source. This pathway consists of five steps, each catalyzed by a distinct enzyme. Here we report the crystal structure of N-succinylarginine dihydrolase AstB, the second enzyme of the arginine succinyltransferase pathway, providing the first structural insight into enzymes from this pathway. The enzyme exhibits a pseudo 5-fold symmetric alpha/beta propeller fold of circularly arranged betabetaalphabeta modules enclosing the active site. The crystal structure indicates clearly that this enzyme belongs to the amidinotransferase (AT) superfamily and that the active site contains a Cys-His-Glu triad characteristic of the AT superfamily. Structures of the complexes of AstB with the reaction product and a C365S mutant with bound the N-succinylarginine substrate suggest a catalytic mechanism that consists of two cycles of hydrolysis and ammonia release, with each cycle utilizing a mechanism similar to that proposed for arginine deiminases. Like other members of the AT superfamily of enzymes, AstB possesses a flexible loop that is disordered in the absence of substrate and assumes an ordered conformation upon substrate binding, shielding the ligand from the bulk solvent, thereby controlling substrate access and product release.