2-acetolactate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: 2-acetolactate
• 英文别名: 2-Acetyllactate；2-hydroxy-2-methyl-3-oxobutanoate
• 化学式: C₅H₇O₄
• 分子量: 131.108
• InChiKey: NMDWGEGFJUBKLB-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  9
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  77.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-acetolactate 在 acetolactate decarboxylase 作用下， 生成 (R)-acetoin
  参考文献：
  名称：

  乙酰乳酸脱羧酶的生物转化：两种底物对映异构体异常转化为高光学纯度的产物

  摘要：

  乙酰乳酸脱羧酶催化2-乙基-2-羟基-3-氧代丁酸的两个对映异构体脱羧化为高光学纯度的异构酮和α-乙酰乳酸（2-羟基-2-甲基-3-氧代丁酸）的两个对映异构体脱乙酰化（ 3-羟基丁烷-2-酮）具有高的光学纯度。

  DOI：

  10.1039/c39880000098
• 作为产物：
  描述：

  piruvate 在 protein AlsSQ₄₂₄S 作用下， 生成 2-acetolactate
  参考文献：
  名称：

  枯草芽孢杆菌乙酰乳酸合酶的详细结构-功能相关性

  摘要：

  乙酰乳酸合酶（ALS）是设计异丁醇生物合成途径中必不可少的酶。由于其有效的丙酮酸催化转化为乙酰乳酸以及对替代底物酮异戊酸酯（KIV）的反应性，枯草芽孢杆菌的ALS特别受关注。这项研究为这种催化机制的结构-功能关系提供了新的见解。

  DOI：

  10.1002/cbic.201402541

文献信息

• Inhibition studies of ketol-acid reductoisomerases from pathogenic microorganisms
  作者：Shun Jie Wun、Lambro A. Johnson、Lv You、Ross P. McGeary、Thomas Brueck、Gerhard Schenk、Luke W. Guddat

  DOI：10.1016/j.abb.2020.108516

  日期：2020.10

  Ketol-acid reductoisomerase (KARI), the second enzyme in the branched-chain amino acid (BCAA) biosynthesis pathway, is an emerging target for the discovery of biocides. Here, we demonstrate that cyclopropane-1,1-dicarboxylate (CPD) inhibits KARIs from the pathogens Mycobacterium tuberculosis (Mt) and Campylobacter jejuni (Cj) reversibly with K-i values of 3.03 mu M and 0.59 mu M, respectively. Another reversible inhibitor of both KARIs, Hoe 704, is more potent than CPD with K-i values of 300 nM and 110 nM for MtKARI and CjKARI, respectively. The most potent inhibitor tested here is N-hydroxy-N-isopropyloxamate (IpOHA). It has a K-i of similar to 26 nM for MtKARI, but binds rather slowly (k(on) similar to 900 M(-1)s(-1)). In contrast, IpOHA binds more rapidly (k(on) similar to 7000 M(-1)s(-1)) to CjKARI and irreversibly.
• CROUT, DAVID H. G.;RATHBONE, DANIEL L., J. CHEM. SOC. CHEM. COMMUN.,(1988) N 2, 98-99
  作者：CROUT, DAVID H. G.、RATHBONE, DANIEL L.

  DOI：——

  日期：——
• Biosynthesis of isoleucine and valine in Mycobacterium tuberculosis H37 Rv
  作者：H.S. Allaudeen、T. Ramakrishnan

  DOI：10.1016/0003-9861(68)90655-3

  日期：1968.4
• 10.1002/anie.202404045
  作者：Lanza, Lucrezia、Rabe von Pappenheim, Fabian、Bjarnesen, Daniela、Leogrande, Camilla、Paul, Alexandra、Krug, Leonhard、Tittmann, Kai、Müller, Michael

  DOI：10.1002/anie.202404045

  日期：——

  The thiamine diphosphate (ThDP)‐binding motif, characterized by the canonical GDG(X)24‐27N sequence, is highly conserved among ThDP‐dependent enzymes. We investigated a ThDP‐dependent lyase (JanthE from Janthinobacterium sp. HH01) with an unusual cysteine (C458) replacing the first glycine of this motif. We found that JanthE has a high substrate promiscuity accepting long aliphatic α‐keto acids as donors. Sterically hindered aromatic aldehydes or non‐activated ketones are acceptor substrates, giving access to a variety of secondary and tertiary alcohols as carboligation products. The crystal structure solved at a resolution of 1.9 Å reveals that C458 is not primarily involved in the cofactor binding as previously thought for the canonical glycine. Instead, it coordinates methionine 406, thus ensuring the integrity of the active site and the enzyme activity. We further determined the long‐sought genuine tetrahedral intermediates formed with pyruvate and 2‐oxo‐butyrate in the pre‐decarboxylation states and unravel atomic details for their stabilization in the active site. Collectively, we unravel an unexpected role for the first residue of the ThDP‐binding motif and unlock a family of lyases able to perform valuable carboligation reactions.
• Detailed Structure-Function Correlations of<i>Bacillus subtilis</i>Acetolactate Synthase
  作者：Bettina Sommer、Holger von Moeller、Martina Haack、Farah Qoura、Clemens Langner、Gleb Bourenkov、Daniel Garbe、Bernhard Loll、Thomas Brück

  DOI：10.1002/cbic.201402541

  日期：2015.1.2

  Acetolactate synthase (ALS) is an essential enzyme in designed isobutanol biosynthesis pathways. Because of its efficient catalytic conversion of pyruvate to acetolactate and its reactivity towards the alternative substrate ketoisovalerate (KIV), the ALS of B. subtilis is of particular interest. This study provides new insights into the structure–function relationships of this catalytic mechanism.

  乙酰乳酸合酶（ALS）是设计异丁醇生物合成途径中必不可少的酶。由于其有效的丙酮酸催化转化为乙酰乳酸以及对替代底物酮异戊酸酯（KIV）的反应性，枯草芽孢杆菌的ALS特别受关注。这项研究为这种催化机制的结构-功能关系提供了新的见解。