Ala-Arg-AMC | 263843-56-7

• 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: Ala-Arg-AMC
• 英文别名: AR-MCA；Ala-Arg-MCA；L-Argininamide, L-alanyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-；(2S)-2-[[(2S)-2-aminopropanoyl]amino]-5-(diaminomethylideneamino)-N-(4-methyl-2-oxochromen-7-yl)pentanamide
• CAS: 263843-56-7
• 化学式: C₁₉H₂₆N₆O₄
• 分子量: 402.453
• InChiKey: AJIRULQIKVSCED-FZMZJTMJSA-N

物化性质

• 密度：
  1.42±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  29
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  175
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Ala-Arg-AMC 在 human dipeptidyl peptidase III, a metallopeptidase of the M₄₉ family 作用下， 以 aq. buffer 为溶剂， 生成 7-氨基-4-甲基香豆素
  参考文献：
  名称：

  Hydrolysis of dipeptide derivatives reveals the diversity in the M49 family

  摘要：

  二肽酶III是M49家族的金属肽酶，最初在垂体中通过特定的二精氨酰芳胺裂解而被识别出来，这些芳胺一直被用作首选的测定底物。在这里，我们同时检测了酵母和人类二肽酶III的活性。人类酶更喜欢Arg₂-β-萘胺，并显示出这种底物的620倍高的k_cat/K_m。相比之下，酵母酶对分析的任何X-Arg-β-萘胺都没有显示出偏好。用Asp取代Gly⁵⁰⁵导致酵母酶形成了一个活性较低但更具选择性的形式。这些结果表明M49家族的裂解特异性存在多样性。

  DOI：

  10.1515/hsz-2012-0347

文献信息

• 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.
• MATRIPTASE, A SERINE PROTEASE AND ITS APPLICATIONS
  申请人：GEORGETOWN UNIVERSITY

  公开号：EP1161266A1

  公开（公告）日：2001-12-12
• EP1161266A4
  申请人：——

  公开号：EP1161266A4

  公开（公告）日：2007-09-19
• [EN] MATRIPTASE, A SERINE PROTEASE AND ITS APPLICATIONS<br/>[FR] MATRIPTASE, PROTEASE DE LA SERINE, ET SON UTILISATION
  申请人：UNIV GEORGETOWN

  公开号：WO2000053232A1

  公开（公告）日：2000-09-14

  The invention is directed to a method of detecting a malignancy or a pre-malignant lesion in breast or other tissue, or a pathologic condition, by detecting the presence of single-chain or two-chain forms of matriptase in the tissue. The invention is further directed to a method of treating malignancies, which have the phenotype of matriptase production by administering a tumor formation inhibiting effective amount of a concentrate of Bowman-Birk inhibitor (BBIC), or other matriptase inhibitor. The invention also is directed to nucleic acids encoding a matriptase protein or fragments thereof, and their use for structure elucidation and modeling to identify other inhibitors of matriptase, as well as to methods of identifying matriptase modulating agents, including activators and inhibitors.
• Hydrolysis of dipeptide derivatives reveals the diversity in the M49 family
  作者：Nina Jajčanin-Jozić、Marija Abramić

  DOI：10.1515/hsz-2012-0347

  日期：2013.6.1

  Dipeptidyl peptidase III, a metallopeptidase of the M49 family, was first identified (in the pituitary) by its specific cleavage of diarginyl arylamides, which have been used as preferred assay substrates until now. Here we examined the activity of the yeast and human dipeptidyl peptidase III in parallel. The human enzyme preferred Arg₂-β-naphthylamide and showed 620-fold higher k _cat/K _m for this substrate. In contrast, the yeast enzyme did not display a preference for any of the X-Arg-β-naphthylamide analyzed. The replacement of Gly⁵⁰⁵ with Asp, resulted in a less active, but more selective, yeast enzyme form. These results indicate diversity in cleavage specificity in the M49 family.

  二肽酶III是M49家族的金属肽酶，最初在垂体中通过特定的二精氨酰芳胺裂解而被识别出来，这些芳胺一直被用作首选的测定底物。在这里，我们同时检测了酵母和人类二肽酶III的活性。人类酶更喜欢Arg₂-β-萘胺，并显示出这种底物的620倍高的k_cat/K_m。相比之下，酵母酶对分析的任何X-Arg-β-萘胺都没有显示出偏好。用Asp取代Gly⁵⁰⁵导致酵母酶形成了一个活性较低但更具选择性的形式。这些结果表明M49家族的裂解特异性存在多样性。