L-alanine-L-alanine-p-nitroanilide | 57282-69-6

• 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-alanine-L-alanine-p-nitroanilide
• 英文别名: L-alanyl-L-alanine-p-nitroanilide；alanyl-alanine-p-nitro-anilide；L-Ala-Ala-p-nitroanilide；Ala-Ala-pNA；L-Ala-Ala-pNA；L-Alaninamide, L-alanyl-N-(4-nitrophenyl)-；(2S)-2-amino-N-[(2S)-1-(4-nitroanilino)-1-oxopropan-2-yl]propanamide
• CAS: 57282-69-6；115846-28-1；115846-37-2
• 化学式: C₁₂H₁₆N₄O₄
• 分子量: 280.283
• InChiKey: DGJXYQXDZRCZAS-YUMQZZPRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  20
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  130
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-alanine-L-alanine-p-nitroanilide 在 religiosin B 作用下， 生成 4-硝基苯胺
  参考文献：
  名称：

  Religiosin B, a milk-clotting serine protease from Ficus religiosa

  摘要：

  A novel milk-clotting serine protease, named religiosin B, is purified from Ficus religiosa. The molecular mass of the protein is 63,000 with pI value of pH 7.6. The proteolytic activity of the enzyme is strongly inhibited by phenylmethanesulfonyl fluoride (PMSF) and chymostatin. Religiosin B acts optimally at pH 8.0-8.5 and temperature 55 degrees C. The molar absorption coefficient of the enzyme is 149,725 M-1 cm(-1) with 23 tryptophan, 15 tyrosine and 7cysteine residues per molecule of the enzyme. The enzyme shows broad substrate specificity with natural as well as synthetic substrates. Religiosin B is highly stable against denaturants and metal ions as well as over a wide range of pH and temperature. The de novo sequencing confirms the novelty of the enzyme. In addition to its high milk-clotting ability, it could be used in the cheese industry, as well as other food and biotechnological industries. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.foodchem.2011.09.122

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。
• A Stable Serine Protease, Wrightin, from the Latex of the Plant Wrightia tinctoria (Roxb.) R. Br.: Purification and Biochemical Properties
  作者：Ritu Tomar、Reetesh Kumar、M. V. Jagannadham

  DOI：10.1021/jf0726536

  日期：2008.2.1

  Today proteases have become an integral part of the food and feed industry, and plant latex could be a potential source of novel proteases with unique substrate specificities and biochemical properties. A new protease named "wrightin" is purified from the latex of the plant Wrightia tinctoria (Family Apocynaceae) by cation-exchange chromatography. The enzyme is a monomer having a molecular mass of 57.9 kDa (MALDI-TOF), an isoelectric point of 6.0, and an extinction coefficient epsilon(1%)280) of 36.4. Optimum activity is achieved at a pH of 7.5-10 and a temperature of 70 degrees C. Wrightin hydrolyzes denatured natural substrates such as casein, azoalbumin, and hemoglobin with high specific activity; for example, the Km value is 50 mu M for casein as substrate. Wrightin showed weak amidolytic activity toward L-Ala-Ala-p-nitroanilide but completely failed to hydrolyze N-alpha-benzoyl-DL-arginine-p-nitroanilide (BAPNA), a preferred substrate for trypsin-like enzymes. Complete inhibition of enzyme activity by serine protease inhibitors such as PMSF and DFP indicates that the enzyme belongs to the serine protease class. The enzyme was not inhibited by SBTl and resists autodigestion. Wrightin is remarkably thermostable, retaining complete activity at 70 degrees C after 60 min of incubation and 74% of activity after 30 min of incubation at 80 degrees. Besides, the enzyme is very stable over a broad range of pH from 5.0 to 11.5 and remains active in the presence of various denaturants, surfactants, organic solvents, and metal ions. Thus, wrightin might be a potential candidate for various applications in the food and biotechnological industries, especially in operations requiring high temperatures.
• Religiosin C, a cucumisin-like serine protease from Ficus religiosa
  作者：Anurag Sharma、Moni Kumari、M.V. Jagannadham

  DOI：10.1016/j.procbio.2012.02.015

  日期：2012.6

  A serine protease was purified to homogeneity from the latex of Ficus religiose. The enzyme, named religiosin C is a monomer with molecular mass of 80 kDa. The enzymatic activity of the protein was inhibited by serine protease inhibitors. Isoelectric point of the enzyme is pH 4.6 with optimum pH and temperature of pH 6-8 and 45-50 degrees C, respectively. The specific extinction coefficient (epsilon(1%)(280)) of the enzyme is 14.68 with 16 tryptophan, 20 tyrosine and 7 cysteine residues in its molecular structure. The enzyme shows broad substrate specificity and hydrolyzes both natural and synthetic substrates. The enzyme is highly stable over a broad range of pH and temperature as well as in the presence of high concentration of chemical denaturants, organic solvents and metal ions. The N-terminal residues of religiosin C exhibited considerable homology with cucumisin and other cucumisin/subtilisin-like serine proteases. The high milk-clotting ability of religiosin C supports its probable use in the food and other biotechnological industries. (C) 2012 Elsevier Ltd. All rights reserved.
• Weidhase; Welker; Dove, Pharmazie, 1984, vol. 39, # 12, p. 835 - 837
  作者：Weidhase、Welker、Dove、Neubert、Yoshimoto、Tsuru、Barth

  DOI：——

  日期：——
• PROTEASES FROM STREPTOMYCES AND USE THEREOF IN PROTEIN EXPRESSION SYSTEMS
  申请人：Cangene Corporation

  公开号：EP0731841A1

  公开（公告）日：1996-09-18