(2R)-2-azaniumyl-5-hydroxypentanoate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (2R)-2-azaniumyl-5-hydroxypentanoate
• 化学式: C5H11NO3
• 分子量: 133.15
• InChiKey: CZWARROQQFCFJB-SCSAIBSYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  9
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  83.6
• 氢给体数：
  3
• 氢受体数：
  4

文献信息

• Simple syntheses of (S)-2- and 4-amino-5-hydroxypentanoic acids
  作者：Kleomenis Barlos、Petros Mamos、Dionysios Papaioannou、Stella Patrianakou

  DOI：10.1039/c39870001583

  日期：——

  The title compounds were efficiently prepared by selective reductions of α- and γ-methyl (S)-N-tritylglutamates with LiAlH4

  通过用LiAlH 4选择性还原α-和γ-甲基（S）-N-三苯甲基谷氨酸盐可以有效地制备标题化合物
• Berlinguet; Gaudry, Journal of Biological Chemistry, 1952, vol. 198, p. 765,766
  作者：Berlinguet、Gaudry

  DOI：——

  日期：——
• Biosynthesis of 4-Methylproline in Cyanobacteria:  Cloning of <i>n</i><i>osE</i> and <i>n</i><i>osF</i> Genes and Biochemical Characterization of the Encoded Dehydrogenase and Reductase Activities
  作者：Hendrik Luesch、Dietmar Hoffmann、Joan M. Hevel、Julia E. Becker、Trimurtulu Golakoti、Richard E. Moore

  DOI：10.1021/jo026479q

  日期：2003.1.1

  The biosynthesis of the unusual amino acid 4-methylproline in the Nostoc genus of cyanobacteria was investigated on the genetic and enzymatic level. Two genes involved in the biosynthesis were cloned and the corresponding enzymes, a zinc-dependent long-chain dehydrogenase and a Delta(1)-pyrroline-5-carboxylic acid (P5C) reductase homologue, were overexpressed in Escherichia coli and biochemically characterized. Putative substrates were synthesized to test enzyme substrate specificities, and deuterium labeling studies were carried out to reveal the stereospecificities of the enzymatic reactions with respect to the substrates as well as to the coenzymes.
• Micropeptins from the Freshwater Cyanobacterium <i>Microcystis aeruginosa</i> (NIES-100)
  作者：Takaya Kisugi、Tatsufumi Okino

  DOI：10.1021/np800631t

  日期：2009.4.24

  Micropeptins C (1), D (2), E (3), and F (4) have been isolated from the freshwater cyanobacterium Microcystis aeruginosa (NIES-100). The structures were elucidated by analyses of MS, NMR spectra, and chemical degradation. Micropeptins C, D, E, and F inhibited chymotrypsin with IC50's of 1.1, 1.2, 1.0, and 1.5 mu g/mL, respectively.