alaninyl adenylate | 17004-38-5

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: alaninyl adenylate
• 英文别名: Ala-O-AMP；[5']adenylic acid L-alanine anhydride；[5']Adenylsaeure-L-alanin-anhydrid；(L-alanyl)adenylate；[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl [(2S)-2-azaniumylpropanoyl] phosphate
• CAS: 17004-38-5
• 化学式: C₁₃H₁₉N₆O₈P
• 分子量: 418.303
• InChiKey: ISYFCRWDMNBLTM-MACXSXHHSA-N

物化性质

• 沸点：
  757.3±70.0 °C(Predicted)
• 密度：
  2.08±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -5.7
• 重原子数：
  28
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.54
• 拓扑面积：
  218
• 氢给体数：
  5
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  水 、 alaninyl adenylate 生成 L-丙氨酸 、 5'-腺嘌呤核苷酸
  参考文献：
  名称：

  Meister; Scott, Biochemical Preparations, 1961, vol. 8, p. 11,15

  摘要：

  DOI：
• 作为产物：
  描述：

  adenosine-5'-monophosphoric N-(carboxybenzyloxy)alanyl mixed anhydride 在 钯 、 溶剂黄146 作用下， 生成 alaninyl adenylate
  参考文献：
  名称：

  Moldave et al., Journal of Biological Chemistry, 1959, vol. 234, p. 841,843

  摘要：

  DOI：

文献信息

• Amino Acid Dependent Formation of Phosphate Anhydrides in Water Mediated by Carbonyl Sulfide
  作者：Luke J. Leman、Leslie E. Orgel、M. Reza Ghadiri

  DOI：10.1021/ja056036e

  日期：2006.1.1

  an efficient condensing agent in the context of phosphate chemistry in aqueous solutions. We report that high-energy aminoacyl-phosphate anhydrides and aminoacyl adenylates are generated in solutions containing amino acids, COS, and the corresponding phosphate molecule. We further show that the mixed anhydrides of amino acids and inorganic phosphate are phosphorylating agents, producing pyrophosphate

  硫化羰 (COS) 是火山气体排放和星际气体云的组成部分，在水溶液中的磷酸盐化学背景下被证明是一种有效的冷凝剂。我们报告说，在含有氨基酸、COS 和相应的磷酸盐分子的溶液中会产生高能氨酰磷酸酐和氨酰腺苷酸。我们进一步表明，氨基酸和无机磷酸盐的混合酸酐是磷酸化剂，在 Ca2+ 沉淀存在的情况下，焦磷酸盐的产率高于 30%。这里报道的磷酸的氨基酸依赖性激活与肽的产生同时发生，表明这两个反应可能在益生元地球上共享一个共同的中间体。
• Phosphinothricin Tripeptide Synthetases in <i>Streptomyces viridochromogenes</i> Tü494
  作者：Dirk Schwartz、Nicolas Grammel、Eva Heinzelmann、Ullrich Keller、Wolfgang Wohlleben

  DOI：10.1128/aac.49.11.4598-4607.2005

  日期：2005.11

  The tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes , is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N -acetyl-demethylphosphinothricin ( N -Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. Both phsB and phsC appear to be cotranscribed together with two other genes from a single promoter and they are located at a distance of 20 kb from the gene phsA , encoding PhsA, in the PTT biosynthesis gene cluster of S. viridochromogenes . PhsB and PhsC represent single nonribosomal peptide synthetase elongation modules lacking a thioesterase domain. Gene inactivations, genetic complementations, determinations of substrate specificity of the heterologously produced proteins, and comparison of PhsC sequence with the amino terminus of the alanine-activating nonribosomal peptide synthetase PTTSII from S. viridochromogenes confirmed the role of the two genes in the bialanylation of Ac-DMPT. The lack of an integral thioesterase domain in the PTT assembly system points to product release possibly involving two type II thioesterase genes ( the1 and the2 ) located in the PTT gene cluster alone or in conjunction with an as yet unknown mechanism of product release.

  摘要 一种具有除草活性的化合物--phosphinothricin（PT）三肽（PTT）的三肽骨架来自于 链霉菌（StrePTomyces viridochromogenes 由三个独立的肽合成酶模块组装而成。酶 PhsA（66 kDa）招募 PT 前体 N -乙酰基-去甲基磷霉素（N N -Ac-DMPT），而 PTT 的两个丙氨酸残基则由 PhsB 和 PhsC 酶（分别为 129 和 119 kDa）组装。在组装过程中或组装后，肽中的 N-Ac-DMPT 残基会通过甲基化和去乙酰化转化为 PT。两个 phsB 和 phsC 似乎与另外两个基因共同转录自一个启动子，它们与基因 phsA 的距离为 20 kb。 病毒色素 .PhsB 和 PhsC 代表缺乏硫酯酶结构域的单一非核糖体肽合成酶延伸模块。基因失活、基因互补、确定异源生产的蛋白质的底物特异性，以及将 PhsC 序列与来自 S. viridochromogenes 的丙氨酸活化非核糖体肽合成酶 PTTSII 的氨基末端进行比较。 的丙氨酸活化非核糖体肽合成酶 PTTSII 证实了这两个基因在 Ac-DMPT 的双乙酰化过程中的作用。PTT 组装系统中缺乏一个完整的硫酯酶结构域，这表明产物的释放可能涉及两个 II 型硫酯酶基因（the1和the2）。 和 和 2 ）单独或与一种尚不清楚的产物释放机制共同作用。
• The Pseudomonas aeruginosa antimetabolite L -2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor
  作者：Nelson Rojas Murcia、Xiaoyun Lee、Patrice Waridel、Alessandro Maspoli、Heidi J. Imker、Tiancong Chai、Christopher T. Walsh、Cornelia Reimmann

  DOI：10.3389/fmicb.2015.00170

  日期：——

  The Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoic acid (AMB) is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE), and two iron(II)/a-ketoglutaratedependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. Using a combination of ATP-PP; exchange assays, aminoacylation assays, and mass spectrometry-based analysis of enzyme-bound substrates and pathway intermediates, the AmbB substrate was identified to be L-alanine (L-Ala), while the Ti and T2 domains of AmbE were loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurred only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE revealed the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD were included in the assay, these peptides were no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide was found at T2. These data are in agreement with a biosynthetic model in which L-Glu is converted into AMB by the action of AmbC, AmbD, and tailoring domains of AmbE. The importance of the flanking L-Ala residues in the precursor tripeptide is discussed.