L-tyrosine-D-leucine | 79205-72-4

• 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-tyrosine-D-leucine
• 英文别名: L-Tyr-D-Leu；(2R)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoic acid
• CAS: 79205-72-4
• 化学式: C₁₅H₂₂N₂O₄
• 分子量: 294.351
• InChiKey: AUEJLPRZGVVDNU-QWHCGFSZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.8
• 重原子数：
  21
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  113
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-tyrosine-D-leucine 在 recombinant Streptomyces coelicolor Sco₃₀₅₈ dipeptidase 、 水 作用下， 生成 D-亮氨酸 、 L-酪氨酸
  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-苄氧羰基-L-酪氨酸 在 N-羟基丁二酰亚胺 、 氢气 、 N,N'-二环己基碳二亚胺 作用下， 生成 L-tyrosine-D-leucine
  参考文献：
  名称：

  电位计和分光光度法研究铜（II）与含酪氨酸的二肽之间形成的配位化合物

  摘要：

  L-酪氨酰甘氨酸（H 2 L），L-酪氨酰-L-亮氨酸，L-酪氨酰-D-亮氨酸，糖基酪氨酸，L-亮氨酰-L-酪氨酸和L-酪氨酸酰胺与H +和Cu之间形成的配位化合物已经在25°C和I = 0.10 mol dm –3（K [NO 3 ]）的条件下对2+进行了电位研究。除了预期的复杂化合物[Cu（HL）] +，[CuL]，[Cu（H –1 L）] –，[Cu（H –2 L）] 2–，和[Cu（HL 2）] –是双核络合物[{Cu（H –1 L）} 2 ] 2–，在pH范围8–10.5中与酪氨酰甘氨酸和酪氨酰-D / L-一起形成。亮氨酸（产生绿色溶液），但是当酪氨酸是二肽的末端羧基时则不存在。分光光度滴定法表明该二聚体涉及铜（II）-酚盐的氧键。描述了二聚体的结构，其解释了不存在可与甘氨酰-和亮氨酰-酪氨酸相当的二聚体，以及酪氨酸-D / L-亮氨酸非对映异构体发现的立体选择性。

  DOI：

  10.1039/dt9810001331

文献信息

• Potentiometric and spectrophotometric study of the co-ordination compounds formed between copper(II) and dipeptides containing tyrosine
  作者：Robert J. W. Hefford、Leslie D. Pettit

  DOI：10.1039/dt9810001331

  日期：——

  Co-ordination compounds formed between L-tyrosylglycine (H2L), L-tyrosyl-L-leucine, L-tyrosyl-D-leucine, glycyltyrosine, L-leucyl-L-tyrosine, and L-tyrosineamide and H+ and Cu2+ have been studied potentiometrically at 25 °C and I= 0.10 mol dm–3(K[NO3]). In addition to the expected complex compounds [Cu(HL)]+, [CuL], [Cu(H–1L)]–, [Cu(H–2L)]2–, and [Cu(HL2)]–, a binuclear complex, [Cu(H–1L)}2]2–, was

  L-酪氨酰甘氨酸（H 2 L），L-酪氨酰-L-亮氨酸，L-酪氨酰-D-亮氨酸，糖基酪氨酸，L-亮氨酰-L-酪氨酸和L-酪氨酸酰胺与H +和Cu之间形成的配位化合物已经在25°C和I = 0.10 mol dm –3（K [NO 3 ]）的条件下对2+进行了电位研究。除了预期的复杂化合物[Cu（HL）] +，[CuL]，[Cu（H –1 L）] –，[Cu（H –2 L）] 2–，和[Cu（HL 2）] –是双核络合物[Cu（H –1 L）} 2 ] 2–，在pH范围8–10.5中与酪氨酰甘氨酸和酪氨酰-D / L-一起形成。亮氨酸（产生绿色溶液），但是当酪氨酸是二肽的末端羧基时则不存在。分光光度滴定法表明该二聚体涉及铜（II）-酚盐的氧键。描述了二聚体的结构，其解释了不存在可与甘氨酰-和亮氨酰-酪氨酸相当的二聚体，以及酪氨酸-D / L-亮氨酸非对映异构体发现的立体选择性。
• 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.