L-Leu-D-Ala | 17664-98-1

• 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: L-Leu-D-Ala
• 英文别名: N-L-leucyl-D-alanine；D-2-(L-2-Amino-4-methyl-valerylamino)-propionsaeure；N-L-Leucyl-D-alanin；D-Alanine, L-leucyl-；(2R)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]propanoic acid
• CAS: 17664-98-1
• 化学式: C₉H₁₈N₂O₃
• 分子量: 202.254
• InChiKey: HSQGMTRYSIHDAC-RQJHMYQMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.4
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  96.9
• 氢给体数：
  2
• 氢受体数：
  3

安全信息

• 海关编码：
  2924199090

反应信息

• 作为反应物：
  描述：

  L-Leu-D-Ala 在 recombinant Streptomyces coelicolor Sco₃₀₅₈ dipeptidase 、 水 作用下， 生成 D-丙氨酸 、 L-亮氨酸
  参考文献：
  名称：

  Structure, Mechanism, and Substrate Profile for Sco3058: The Closest Bacterial Homologue to Human Renal Dipeptidase,

  摘要：

  Human renal dipeptidase, an enzyme associated With glutathione metabolism and the hydrolysis of beta-lactams, is similar in sequence to a cluster of similar to 400 microbial proteins currently annotated as nonspecific dipeptidases within the amidohydrolase superfamily. The closest homologue to the human renal dipeptidase from a Fully sequenced microbe is Sco3058 from Streptomyces coelicolor. Dipeptide Substrates of Sco3058 were identified by screening a comprehensive series Of L-Xaa-L-Xaa, L-Xaa-D-Xaa, and D-Xaa-L-Xaa dipeptide libraries. The substrate specificity profile shows that Sco3058 hydrolyzes a broad range of dipeptides with a marked preference for all L-amino acid at the N-terminus and a D-amino acid at the C-terminus. The best Substrate identified was L-Arg-D-Asp (k(eat)/K-m = 7.6 x 10(5) M-1 s(-1)). The three-dimensional structure of Sco3058 was determined in the absence and presence of the inhibitors citrate and a phosphinate mimic Of L-Ala-D-Asp. The enzyme folds as (beta/alpha)(8) barrel, and two zinc Ions are bound in the active site. Site-directed mutagenesis was used to probe the importance of specific residues that have direct interactions with the substrate analogues in the active site (Asp-22, His-150, Arg-223, and Asp-320). The solvent viscosity and kinetic effects of D2O indicate that Substrate binding is relatively sticky and that proton transfers do not occur during the rate-limiting step. A bell-shaped pH-rate profile for k(cat) and k(cat)/k(m) indicated that one group needs to he deprotonated and a second group Must be protonated for optimal turnover. Computational docking of high-energy intermediate forms Of L/D-Ala-L/D-Ala to the three-dimensional Structure of Sco3058 identified the Structural determinants for the stereochemical preferences for Substrate binding and turnover.

  DOI：

  10.1021/bi901935y
• 作为产物：
  描述：

  N-Z-亮氨酸氯化物 在 sodium hydroxide 、 丙酮 作用下， 生成 L-Leu-D-Ala
  参考文献：
  名称：

  Bergmann et al., Journal of Biological Chemistry, 1935, vol. 109, p. 344

  摘要：

  DOI：

文献信息

• Self‐assembly of heterochiral, aliphatic dipeptides with Leu
  作者：Erica Scarel、Marco De Corti、Maurizio Polentarutti、Giovanni Pierri、Consiglia Tedesco、Silvia Marchesan

  DOI：10.1002/psc.3559

  日期：——

  aliphatic dipeptides, l-Leu-d-Xaa (Xaa = Ala, Val, Ile, Leu), in green solvents such as acetonitrile (MeCN) and buffered water at neutral pH. Interestingly, water plays a structuring role because at 1% v/v, it enables dipeptide self-assembly in MeCN to yield organogels, which then undergo transition towards crystals. Other organic solvents and oils were tested for gelation, and metastable gels were formed

  这项工作描述了异手性脂肪族二肽l -Leu- d -Xaa（Xaa = Ala、Val、Ile、Leu）在乙腈 (MeCN) 等绿色溶剂和中性 pH 值缓冲水中的自组装行为。有趣的是，水起着结构化作用，因为在 1% v/v 时，它使二肽在 MeCN 中自组装产生有机凝胶，然后转变为晶体。测试了其他有机溶剂和油的凝胶作用，并且在四氢呋喃中形​​成了亚稳态凝胶，尽管肽浓度很高（80 mM）。单晶 X 射线衍射揭示了二肽在两亲层中的超分子堆积模式，这与报道的纯手性 Leu-Leu 的水通道或报道的纯手性 Leu-Val 和 Leu-Ile 的疏水柱相反。
• Polglase; Smith, Journal of the American Chemical Society, 1949, vol. 71, p. 3083
  作者：Polglase、Smith

  DOI：——

  日期：——
• Bergmann et al., Journal of Biological Chemistry, 1935, vol. 109, p. 344
  作者：Bergmann et al.

  DOI：——

  日期：——
• Structure, Mechanism, and Substrate Profile for Sco3058: The Closest Bacterial Homologue to Human Renal Dipeptidase,
  作者：Jennifer A. Cummings、Tinh T. Nguyen、Alexander A. Fedorov、Peter Kolb、Chengfu Xu、Elena V. Fedorov、Brian K. Shoichet、David P. Barondeau、Steven C. Almo、Frank M. Raushel

  DOI：10.1021/bi901935y

  日期：2010.1.26

  Human renal dipeptidase, an enzyme associated With glutathione metabolism and the hydrolysis of beta-lactams, is similar in sequence to a cluster of similar to 400 microbial proteins currently annotated as nonspecific dipeptidases within the amidohydrolase superfamily. The closest homologue to the human renal dipeptidase from a Fully sequenced microbe is Sco3058 from Streptomyces coelicolor. Dipeptide Substrates of Sco3058 were identified by screening a comprehensive series Of L-Xaa-L-Xaa, L-Xaa-D-Xaa, and D-Xaa-L-Xaa dipeptide libraries. The substrate specificity profile shows that Sco3058 hydrolyzes a broad range of dipeptides with a marked preference for all L-amino acid at the N-terminus and a D-amino acid at the C-terminus. The best Substrate identified was L-Arg-D-Asp (k(eat)/K-m = 7.6 x 10(5) M-1 s(-1)). The three-dimensional structure of Sco3058 was determined in the absence and presence of the inhibitors citrate and a phosphinate mimic Of L-Ala-D-Asp. The enzyme folds as (beta/alpha)(8) barrel, and two zinc Ions are bound in the active site. Site-directed mutagenesis was used to probe the importance of specific residues that have direct interactions with the substrate analogues in the active site (Asp-22, His-150, Arg-223, and Asp-320). The solvent viscosity and kinetic effects of D2O indicate that Substrate binding is relatively sticky and that proton transfers do not occur during the rate-limiting step. A bell-shaped pH-rate profile for k(cat) and k(cat)/k(m) indicated that one group needs to he deprotonated and a second group Must be protonated for optimal turnover. Computational docking of high-energy intermediate forms Of L/D-Ala-L/D-Ala to the three-dimensional Structure of Sco3058 identified the Structural determinants for the stereochemical preferences for Substrate binding and turnover.