His-Pro-Tyr | 136616-45-0

• 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: His-Pro-Tyr
• 英文别名: (2S)-2-[[(2S)-1-[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoic acid
• CAS: 136616-45-0
• 化学式: C₂₀H₂₅N₅O₅
• 分子量: 415.449
• InChiKey: CHIAUHSHDARFBD-ULQDDVLXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.8
• 重原子数：
  30
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  162
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  His-Pro-Tyr 反应 0.17h， 生成 L-酪氨酸 、 组氨酰脯氨酸
  参考文献：
  名称：

  Catalytic Properties of X-Prolyl Dipeptidyl Aminopeptidase fromLactococcus lactissubsp.cremorisnTR

  摘要：

  在Lactococcus lactis subsp. cremoris nTR的内细胞膜组分上，鉴定出一种松散结合的X-脯氨酰二肽二肽基氨肽酶（X-PDAP；EC 3.4.14.5）。在细菌的后期对数生长阶段之前，X-PDAP的生物合成不断增加。X-PDAP可以水解Gly-Pro-pNA和Ala-Ala-pNA，前者的kcat/Km值约为后者的10倍。X-Pro和Pro-X的Ki比X-Ala更特异于X-PDAP。鉴定出一种以β-酪啡肽为模型的催化模式连续切割二肽的酶，并进一步表征了该酶的一些性质。

  DOI：

  10.1271/bbb.56.704
• 作为产物：
  描述：

  、 Fmoc-His(Trt)-OH 、 alkaline earth salt of/the/ methylsulfuric acid 生成 His-Pro-Tyr
  参考文献：
  名称：

  Benzo[a]pyrene anti-diol epoxide covalently modifies human serum albumin carboxylate side chains and imidazole side chain of histidine(146)

  摘要：

  Human serum albumin was reacted with (+/-)-r-7,t-8-dihydroxy-t-9,t-10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene (anti-BaPDE) in vitro and extracted to remove byproducts not covalently bound to the protein. Enzymatic digestion of the adducted protein in (HO)-H-2-O-18 at pH 8.2 and pH 10.0, followed by analysis of the released 7,8,9,10-tetrahydrotetrols by positive chemical ionization mass spectrometry for O-18 incorporation, revealed that carboxylic esters are formed by the epoxide. Analysis by HPLC/UV of the protein digest indicated that esters are the major product formed. Two additional stable products were also observed, accounting for 22 and 8% of chromatographed material. These were identical in UV absorption spectral characteristics with synthetic N(im)-histidine-anti-BaPDE adducts. Amino acid analysis of the peptide portion of the major product, in combination with its FAB mass spectrum, was consistent with a composition of histidine, proline, and tyrosine, while like analysis of the minor adducted peptide was consistent with a composition of histidine and proline. The first combination of amino acids occurs only once within the sequence of human albumin as His(146)-Pro(147)-Tyr(148). The second could be a subsequence of the first or correspond to His(338)-Pro(339) or His(440)-Pro(441). When synthetic His-Pro-Tyr was reacted with anti-BaPDE, a product which was chromatographically and spectrally (UV, FAB-MS) identical with the material isolated from alkylated albumin was formed in low yield. Reaction with fluorescamine followed by acid-catalyzed rearrangement of the products and analysis of the fluorescence spectra from the resulting materials revealed that the adducts in the protein resulted from alkylation of the imidazole tau-nitrogen of histidine. These results indicate that, in addition to the unknown amino acids esterified, His(146) and possibly His(338) or His(440), the former two of which are in a previously recognized binding site for certain covalent and noncovalent bulky aromatic ligands, are alkylated by anti-BaPDE to form enzymatically stable adducts.

  DOI：

  10.1021/ja00022a044

文献信息

• Catalytic Properties of X-Prolyl Dipeptidyl Aminopeptidase from<i>Lactococcus lactis</i>subsp.<i>cremoris</i>nTR
  作者：Tsong-Rong Yan、Shih-Ching Ho、Chia-Lung Hou

  DOI：10.1271/bbb.56.704

  日期：1992.1

  An X-prolyl dipeptidyl aminopeptidase (X-PDAP; EC 3.4.14.5) was identified to be loosely bound on the inner cell membrane fraction of Lactococcus lactis subsp. cremoris nTR. The biosynthesis of X-PDAP was continuously increased before the late-log growth phase of the bacteria. Both Gly-Pro-pNA and Ala-Ala-pNA were hydrolyzed by X-PDAP; the kcat/Km value of the former was about 10-fold that of the latter. The Ki of X-Pro and Pro-X were more specific to X-PDAP than those of X-Ala. The enzyme splitting a dipeptide sequentially from β-casomorphin as a model catalytic pattern was identified and some properties of the enzyme were further characterized.

  在Lactococcus lactis subsp. cremoris nTR的内细胞膜组分上，鉴定出一种松散结合的X-脯氨酰二肽二肽基氨肽酶（X-PDAP；EC 3.4.14.5）。在细菌的后期对数生长阶段之前，X-PDAP的生物合成不断增加。X-PDAP可以水解Gly-Pro-pNA和Ala-Ala-pNA，前者的kcat/Km值约为后者的10倍。X-Pro和Pro-X的Ki比X-Ala更特异于X-PDAP。鉴定出一种以β-酪啡肽为模型的催化模式连续切割二肽的酶，并进一步表征了该酶的一些性质。
• Benzo[a]pyrene anti-diol epoxide covalently modifies human serum albumin carboxylate side chains and imidazole side chain of histidine(146)
  作者：Billy W. Day、Paul L. Skipper、Joseph Zaia、Steven R. Tannenbaum

  DOI：10.1021/ja00022a044

  日期：1991.10

  Human serum albumin was reacted with (+/-)-r-7,t-8-dihydroxy-t-9,t-10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene (anti-BaPDE) in vitro and extracted to remove byproducts not covalently bound to the protein. Enzymatic digestion of the adducted protein in (HO)-H-2-O-18 at pH 8.2 and pH 10.0, followed by analysis of the released 7,8,9,10-tetrahydrotetrols by positive chemical ionization mass spectrometry for O-18 incorporation, revealed that carboxylic esters are formed by the epoxide. Analysis by HPLC/UV of the protein digest indicated that esters are the major product formed. Two additional stable products were also observed, accounting for 22 and 8% of chromatographed material. These were identical in UV absorption spectral characteristics with synthetic N(im)-histidine-anti-BaPDE adducts. Amino acid analysis of the peptide portion of the major product, in combination with its FAB mass spectrum, was consistent with a composition of histidine, proline, and tyrosine, while like analysis of the minor adducted peptide was consistent with a composition of histidine and proline. The first combination of amino acids occurs only once within the sequence of human albumin as His(146)-Pro(147)-Tyr(148). The second could be a subsequence of the first or correspond to His(338)-Pro(339) or His(440)-Pro(441). When synthetic His-Pro-Tyr was reacted with anti-BaPDE, a product which was chromatographically and spectrally (UV, FAB-MS) identical with the material isolated from alkylated albumin was formed in low yield. Reaction with fluorescamine followed by acid-catalyzed rearrangement of the products and analysis of the fluorescence spectra from the resulting materials revealed that the adducts in the protein resulted from alkylation of the imidazole tau-nitrogen of histidine. These results indicate that, in addition to the unknown amino acids esterified, His(146) and possibly His(338) or His(440), the former two of which are in a previously recognized binding site for certain covalent and noncovalent bulky aromatic ligands, are alkylated by anti-BaPDE to form enzymatically stable adducts.