丁氧羰基-苯丙氨酰-丝氨酰-精氨酸-AMC | 73554-90-2

• 物质功能分类: 生物化工 - 氨基酸及其衍生物 - 精氨酸类衍生物
• 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
• 中文名称: 丁氧羰基-苯丙氨酰-丝氨酰-精氨酸-AMC
• 中文别名: 叔丁氧羰基-苯丙氨酰-丝氨酰-精氨酸-7-氨基-4-甲基香豆素
• 英文名称: Boc-Phe-Ser-Arg-MCA
• 英文别名: tert-butyl N-[(2S)-1-[[(2S)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• CAS: 73554-90-2
• 化学式: C₃₃H₄₃N₇O₈
• 分子量: 665.747
• InChiKey: JLKJMNJZJBEYLQ-SDHOMARFSA-N

物化性质

• 密度：
  1.35±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  48
• 可旋转键数：
  16
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  237
• 氢给体数：
  7
• 氢受体数：
  9

安全信息

• WGK Germany：
  3

反应信息

• 作为反应物：
  描述：

  丁氧羰基-苯丙氨酰-丝氨酰-精氨酸-AMC 在 trypsin from hepatopancreas of Macrobrachium rosenbergii 作用下， 反应 0.17h， 生成 7-氨基-4-甲基香豆素
  参考文献：
  名称：

  Low molecular weight trypsin from hepatopancreas of freshwater prawn (Macrobrachium rosenbergii): Characteristics and biochemical properties

  摘要：

  Trypsin was purified to homogeneity from hepatopancreas of freshwater prawn (HFWP) (Macrobrachium rosenbergii) using a series of chromatographies including Q-Sepharose, Superdex 75 and MonoQ columns. HFWP trypsin was purified 525-fold with a yield of 10.6%. Based on native-PAGE, the purified trypsin showed a single band. Trypsin had a molecular weight of 17 kDa as estimated by SDS-PAGE. The optimal pH and temperature for Boc-Val-Pro-Arg-MCA hydrolysis were 8.0 and 55 degrees C, respectively. Trypsin was stable to heat treatment up to 40 degrees C, and over a pH range of 7.0-11.0. Trypsin activity was strongly inhibited by soybean trypsin inhibitor, N-p-tosyl-L-lysine chloromethyl ketone (TLCK) and Pefabloc SC and was partially inhibited by ethylenediaminetetraacetic acid (EDTA). Apparent K-m value of trypsin was 0.24 mu M and K-cat value was 607.56 s(-1) for Boc-Val-Pro-Arg-MCA. The N-terminal amino acid sequence of 20 residues of HFWP trypsin was IVGGDEAAPGEFPHQISMQV, which was highly homologous with those from other species of prawn. HFWP trypsin also showed high collagenolytic activity toward prawn, shrimp and fish collagens, suggesting its possible role in muscle softening of freshwater prawn during extended storage. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.foodchem.2012.02.173

文献信息

• Nucleic acid sequence encoding trypsin-like enzyme and process for
  申请人：Teijin Limited

  公开号：US05804410A1

  公开（公告）日：1998-09-08

  This invention provides a nucleic acid sequence encoding a trypsin-like enzyme which can be present at the trachea of human lungs, and can selectively digest a synthetic substrate for trypsin and a synthetic substrate for thrombin, and fibrinogen; and a process for producing the trypsin-like enzyme by genetic engineering utilizing the nucleic acid sequence.

  本发明提供了一种核酸序列，编码一种类似胰蛋白酶的酶，可以存在于人类肺部的气管，并且可以选择性地消化类似胰蛋白酶和类似凝血酶的合成底物以及纤维蛋白原；以及利用该核酸序列进行基因工程制备类似胰蛋白酶的酶的方法。
• Novel proteoglycan glycotechnology: chemoenzymatic synthesis of chondroitin sulfate-containing molecules and its application
  作者：Masanori Yamaguchi、Keiichi Takagaki、Kaoru Kojima、Naohiro Hayashi、Fengchao Chen、Ikuko Kakizaki、Atsushi Kon、Masahiko Endo

  DOI：10.1007/s10719-009-9252-y

  日期：2010.1

  Proteoglycans consist of a protein core, with one or more glycosaminoglycan chains (i.e., chondroitin sulfate, dermatan sulfate and heparin sulfate) bound covalently to it. The glycosaminoglycan chains account for many of the functions and properties of proteoglycans. The development of proteoglycan glycotechnology to exploit the functionality of glycosaminoglycan chains is an extremely important aspect of glycobiology. Here we describe an efficient and widely applicable method for chemoenzymatic synthesis of conjugate compounds comprising intact long chondroitin sulfate (ChS) chains. An alkyne containing ChS was prepared by an enzymatic transfer reaction and linked with a chemically synthesized core compound containing an azido group using click chemistry. This method enabled highly efficient introduction of ChS into target materials. Furthermore, the ChS-introduced compounds had marked stability against proteolysis, and the chemically linked ChS chain contributed to the stability of these core compounds. We believe the present method will contribute to the development of proteoglycan glycobiology and technology.

  蛋白多糖由蛋白质核心和一条或多条糖胺聚糖链（即硫酸软骨素、硫酸皮肤素和硫酸肝素）共价结合而成。糖胺聚糖链决定了蛋白多糖的许多功能和性质。开发蛋白多糖糖技术以利用糖胺聚糖链的功能是糖生物学中极为重要的一个方面。在此，我们介绍了一种高效且广泛适用的化学酶促合成完整长硫酸软骨素（ChS）链的共轭化合物的方法。通过酶促转移反应制备了含ChS的炔，并利用点击化学将其与含叠氮基的化学合成核心化合物连接。这种方法能够高效地将ChS引入目标材料。此外，引入ChS的化合物对蛋白水解具有显著的稳定性，而化学连接的ChS链则有助于这些核心化合物的稳定性。我们相信，目前的方法将有助于蛋白多糖糖生物学和技术的发展。
• Identification and Characterization of Prokaryotic Dipeptidyl-peptidase 5 from Porphyromonas gingivalis
  作者：Yuko Ohara-Nemoto、Shakh M.A. Rouf、Mariko Naito、Amie Yanase、Fumi Tetsuo、Toshio Ono、Takeshi Kobayakawa、Yu Shimoyama、Shigenobu Kimura、Koji Nakayama、Keitarou Saiki、Kiyoshi Konishi、Takayuki K. Nemoto

  DOI：10.1074/jbc.m113.527333

  日期：2014.2

  Background: Dipeptidyl-peptidases (DPPs) are key factors for amino acid metabolism and bacterial growth of asaccharolytic Porphyromonas gingivalis. Results: DPP5, which is specific for Ala and hydrophobic residues, is expressed in the periplasmic space of P. gingivalis.Conclusion: DPP5 was discovered in prokaryotes for the first time. Significance: The discovery of DPP5 expands understanding of amino acid and energy metabolism in prokaryotes. Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN_0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated K-m and k(cat)/K-m values for Lys-Ala-MCA of 688 m and 11.02 m(-1) s(-1), respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.
• TENSIDZUBEREITUNG MIT VERMINDERTER ENZYMSCH DIGUNG
  申请人：BEIESRDORF AG

  公开号：EP1863439A2

  公开（公告）日：2007-12-12
• VERWENDUNG VON ZUBEREITUNGEN ZUM SCHUTZ HAUTEIGENER ENZYME
  申请人：BEIERSDORF AG

  公开号：EP1863437B1

  公开（公告）日：2014-02-26