L-alanyl-L-glutamate(1-)

• 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-alanyl-L-glutamate(1-)
• 英文别名: (2S)-2-[[(2S)-2-azaniumylpropanoyl]amino]pentanedioate
• 化学式: C8H13N2O5-
• 分子量: 217.2
• InChiKey: VYZAGTDAHUIRQA-WHFBIAKZSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 重原子数：
  15
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  137
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-alanyl-L-glutamate(1-) 生成 L-Alanyl-D-glutamate
  参考文献：
  名称：

  Evolution of Enzymatic Activities in the Enolase Superfamily:  Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as l-Ala-d/l-Glu Epimerases

  摘要：

  The members of the mechanistically diverse enolase superfamily catalyze different overall reactions by using a common catalytic strategy and structural scaffold. In the muconate lactonizing enzyme (MLE) subgroup of the superfamily, abstraction of a proton adjacent to a carboxylate group initiates reactions, including cycloisomerization (MLE), dehydration [o-succinylbenzoate synthase (OSBS)], and 1,1-proton transfer (catalyzed by an OSBS that also catalyzes a promiscuous N-acylamino acid racemase reaction). The realization that a member of the MLE subgroup could catalyze a 1,1-proton transfer reaction, albeit poorly, led to a search for other enzymes which might catalyze a 1,1-proton transfer as their physiological reaction. YcjG from Escherichia coli and YkfB from Bacillus subtilis, proteins of previously unknown function, were discovered to be L-Ala-D/L-Glu epimerases, although they also catalyze the epimerization of other dipeptides. The values of k(cat)/K-M for L-Ala-D/L-Glu for both proteins are similar to10(4) M-1 s(-1). The genomic context and the substrate specificity of both YcjG and YkfB suggest roles in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Homologues possessing L-Ala-D/L-Glu epimerase activity have been identified in at least two other organisms.

  DOI：

  10.1021/bi011640x

文献信息

• Recycling of the Anhydro- <i>N</i> -Acetylmuramic Acid Derived from Cell Wall Murein Involves a Two-Step Conversion to <i>N</i> -Acetylglucosamine-Phosphate
  作者：Tsuyoshi Uehara、Kyoko Suefuji、Noelia Valbuena、Brian Meehan、Michael Donegan、James T. Park

  DOI：10.1128/jb.187.11.3643-3649.2005

  日期：2005.6

  Escherichia coli breaks down over 60% of the murein of its side wall and reuses the component amino acids to synthesize about 25% of the cell wall for the next generation. The amino sugars of the murein are also efficiently recycled. Here we show that the 1,6-anhydro- N -acetylmuramic acid (anhMurNAc) is returned to the biosynthetic pathway by conversion to N -acetylglucosamine-phosphate (GlcNAc-P). The sugar is first phosphorylated by a nhydro- N -acetyl m uramic acid k inase (AnmK), yielding MurNAc-P, and this is followed by action of an etherase which cleaves the bond between d -lactic acid and the N -acetylglucosamine moiety of MurNAc-P, yielding GlcNAc-P. The kinase gene has been identified by a reverse genetics method. The enzyme was overexpressed, purified, and characterized. The cell extract of an anmK deletion mutant totally lacked activity on anhMurNAc. Surprisingly, in the anmK mutant, anhMurNAc did not accumulate in the cytoplasm but instead was found in the medium, indicating that there was rapid efflux of free anhMurNAc.

  摘要 大肠杆菌 大肠杆菌能分解其侧壁 60% 以上的木脂素，并将其中的氨基酸成分重新用于合成下一代细胞壁的约 25%。木脂素中的氨基糖也被有效地回收利用。在这里，我们展示了 1,6-anhydro- N -乙酰木氨酸（anhMurNAc）通过转化为 N -乙酰葡糖胺磷酸盐（GlcNAc-P）返回生物合成途径。这种糖首先通过 a nhydro- N -乙酰基 m 尿氨酸 k 酶 (AnmK)的作用，产生 MurNAc-P，随后乙酸酶的作用，裂解了 d -乳酸和 N -乙酰葡糖胺分子之间的键，生成 GlcNAc-P。激酶基因是通过反向遗传学方法确定的。对该酶进行了过表达、纯化和鉴定。细胞提取物 amK 缺失突变体的细胞提取物完全缺乏对 anhMurNAc 的活性。令人惊讶的是，在 anmK 突变体中，anhMurNAc 并未在细胞质中积累，而是出现在培养基中，这表明游离的 anhMurNAc 快速外流。
• Evolution of Enzymatic Activities in the Enolase Superfamily:  Functional Assignment of Unknown Proteins in <i>Bacillus subtilis </i>and <i>Escherichia coli</i> as <scp>l</scp>-Ala-<scp>d</scp>/<scp>l</scp>-Glu Epimerases
  作者：Dawn M. Z. Schmidt、Brian K. Hubbard、John A. Gerlt

  DOI：10.1021/bi011640x

  日期：2001.12.1

  The members of the mechanistically diverse enolase superfamily catalyze different overall reactions by using a common catalytic strategy and structural scaffold. In the muconate lactonizing enzyme (MLE) subgroup of the superfamily, abstraction of a proton adjacent to a carboxylate group initiates reactions, including cycloisomerization (MLE), dehydration [o-succinylbenzoate synthase (OSBS)], and 1,1-proton transfer (catalyzed by an OSBS that also catalyzes a promiscuous N-acylamino acid racemase reaction). The realization that a member of the MLE subgroup could catalyze a 1,1-proton transfer reaction, albeit poorly, led to a search for other enzymes which might catalyze a 1,1-proton transfer as their physiological reaction. YcjG from Escherichia coli and YkfB from Bacillus subtilis, proteins of previously unknown function, were discovered to be L-Ala-D/L-Glu epimerases, although they also catalyze the epimerization of other dipeptides. The values of k(cat)/K-M for L-Ala-D/L-Glu for both proteins are similar to10(4) M-1 s(-1). The genomic context and the substrate specificity of both YcjG and YkfB suggest roles in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Homologues possessing L-Ala-D/L-Glu epimerase activity have been identified in at least two other organisms.