D-malate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羟基酸及其衍生物
• 英文名称: D-malate
• 英文别名: (2R)-2-hydroxybutanedioate
• 化学式: C₄H₄O₅
• 分子量: 132.073
• InChiKey: BJEPYKJPYRNKOW-UWTATZPHSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  0
• 重原子数：
  9
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  101
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (2S)-2-[(4-nitronaphthalen-1-yl)carbamothioylamino]-N-[2-[[4-[2-[[(2S)-2-[(4-nitronaphthalen-1-yl)carbamothioylamino]propanoyl]amino]ethylamino]-9,10-dioxoanthracen-1-yl]amino]ethyl]propanamide 、 D-malate 以 水 、 二甲基亚砜 为溶剂， 生成
  参考文献：
  名称：

  基于丙氨酸的比色传感器的合成以及对天冬氨酸和苹果酸根阴离子的对映选择性识别†

  摘要：

  合成了两个手性比色传感器（1,2），并通过光谱技术对其进行了表征，并通过紫外可见光谱和1 H NMR光谱对它们的手性二羧酸阴离子（D / L-天冬氨酸和D / L-苹果酸）进行对映选择性识别。受体的相互作用1和2与天冬氨酸或苹果酸的对映异构体不同而引起的颜色变化，以及它们作为光学化学传感器用于识别d天冬氨酸与大号天冬氨酸和d -苹果与大号-苹果。受体1对天冬氨酸阴离子具有高对映选择性结合[ KA （D） / KA （L） = 12.15]。

  DOI：

  10.1039/c1ob05135k
• 作为产物：
  描述：

  在 citrate synthase 、 acetyl-CoA synthetase 、 Agrobacterium tumefaciens C₅₈ recombinant Atu₃₂₆₆ protein 、 L-malate dehydrogenase 、 β-烟酰胺腺嘌呤二核苷酸 、 水 、 5’-三磷酸腺苷 、 辅酶 A 、 magnesium chloride 作用下， 生成 D-malate
  参考文献：
  名称：

  Functional Annotation and Three-Dimensional Structure of an Incorrectly Annotated Dihydroorotase from cog3964 in the Amidohydrolase Superfamily

  摘要：

  The substrate specificities of two incorrectly annotated enzymes belonging to cog3964 from the amidohydrolase superfamily were determined. This group of enzymes are currently misannotated as either dihydroorotases or adenine deaminases. Atu3266 from Agrobacterium tumefaciens C58 and Oant2987 from Ochrobactrum anthropi ATCC 49188 were found to catalyze the hydrolysis of acetyl-(R)-mandelate and similar esters with values of K-cat/K-m that exceed 10(5) M-1 s(-1). These enzymes do not catalyze the deamination of adenine or the hydrolysis of dihydroorotate. Atu3266 was crystallized and the structure determined to a resolution of 2.62 angstrom. The protein folds as a distorted (beta/alpha)(8) barrel and binds two zincs in the active site. The substrate profile was determined via a combination of computational docking to the three-dimensional structure of Atu3266 and screening of a highly focused library of potential substrates. The initial weak hit was the hydrolysis of N-acetyl-D-serine (k(cat)/K-m = 4 M-1 s(-1)). This was followed by the progressive identification of acetyl-(R)-glycerate (k(cat)/K-m = 4 x 10(2) M-1 s(-1)), acetyl glycolate (k(cat)/K-m = 1.3 x 10(4) M-1 s(-1)), and ultimately acetyl-(R)-mandelate (k(cat)/K-m = 2.8 x 10(2) M-1 s(-1)).

  DOI：

  10.1021/bi301483z

文献信息

• SALTS OF 6-(5-CHLORO-2-PYRIDYL)-5-[(4-METHYL-1-PIPERAZINYL)CARBONYLOXY]-7-OXO-6,7-DIHY-DRO-5H-PYRROLO[3,4-B]PYRAZINE
  申请人：Wilkinson H. Scott

  公开号：US20110053945A1

  公开（公告）日：2011-03-03

  Novel mesylate, (R)-mandelate, succinate, citrate, fumarate, D-malate, D-tartrate, sulfate and L-tartrate salts of (6-(5-chloro-2-pyridyl)-5-[(4-methyl-1-piperazinyl)carbonyloxy]-7-oxo-6,7-dihydro-5H-pyrrolo[3,4-b]pyrazine) are provided.

  本发明提供了(6-(5-氯-2-吡啶基)-5-[(4-甲基-1-哌嗪基)羰氧基]-7-氧代-6,7-二氢-5H-吡咯并[3,4-b]吡嗪)的甲磺酸盐、(R)-苦杏酸盐、琥珀酸盐、柠檬酸盐、富马酸盐、D-苹果酸盐、D-酒石酸盐、硫酸盐和L-酒石酸盐。
• Screening for microorganisms producing D-malate from maleate
  作者：M J van der Werf、W J van den Tweel、S Hartmans

  DOI：10.1128/aem.58.9.2854-2860.1992

  日期：1992.9

  More than 300 microorganisms were screened for their ability to convert maleate into D-malate as a result of the action of maleate hydratase. Accumulation of fumarate during incubation of permeabilized cells with maleate was shown to be indicative of one of the two enzymes known to transform maleate. The ratio in which fumarate and malate accumulated could be used to estimate the enantiomeric composition of the malate formed. Many strains (n = 128) were found to be capable of converting maleate to D-malate with an enantiomeric purity of more than 97%. Pseudomonas pseudoalcaligenes NCIMB 9867 was selected for more detailed studies. Although this strain was not able to grow on maleate, permeabilized cells were able to degrade maleate to undetectable levels, with a concomitant formation of D-malate. The D-malate was formed with an enantiomeric purity of more than 99.97%.

  超过300种微生物被筛选出来，用于检测它们将丙烯二酸转化为D-苹果酸的能力，这是由丙烯二酸酶的作用所致。在用丙烯二酸孔隙细胞进行孵育时，富马酸的积累表明其中一种已知的转化丙烯二酸酶。积累的富马酸和苹果酸的比率可以用来估计所形成的苹果酸的对映体组成。发现许多菌株（n = 128）能够将丙烯二酸转化为具有97%以上对映纯度的D-苹果酸。选择假单胞菌NCIMB 9867进行更详细的研究。尽管这株菌无法在丙烯二酸上生长，但孔隙细胞能够将丙烯二酸降解至不可检测水平，并同时形成D-苹果酸。所形成的D-苹果酸对映纯度达到99.97%以上。
• Enzymology and Evolution of the Pyruvate Pathway to 2-Oxobutyrate in <i>Methanocaldococcus jannaschii</i>
  作者：Randy M. Drevland、Abdul Waheed、David E. Graham

  DOI：10.1128/jb.00166-07

  日期：2007.6.15

  broad-specificity enzyme, isopropylmalate dehydrogenase (MJ0720), catalyzed the oxidative decarboxylation of beta-isopropylmalate, beta-methylmalate, and d-malate. Combined with these results, phylogenetic analysis suggests that the pyruvate pathway to 2-oxobutyrate (an alternative to threonine dehydratase in isoleucine biosynthesis) evolved several times in bacteria and archaea. The enzymes in the isopropylmalate

  古代甲烷甲烷球菌使用三种不同的2-含氧酸延长途径，这些途径延长了亮氨酸，异亮氨酸和辅酶B生物合成中前体的链长。在这些途径的每一种中，乌头酸酶型水解酶催化羟酸异构化反应。詹氏甲烷球菌的基因组序列编码形成水解酶的每个大亚基和小亚基的两个同源物，但是这些基因不是共转录的。这些基因彼此之间比以前表征的苹果酸异丙酯异构酶或高纯硝酸酶基因更相似。为了鉴定这些同源物的功能，亚单位的四种组合在大肠杆菌中异源表达，纯化并重建以产生全酶的铁硫中心。只有MJ0499和MJ1277蛋白的组合才能催化苹果酸异丙酯和柠檬酸酯的异构化反应。该对还使用柠檬酸柠檬酸酯和马来酸酯催化水合半反应。另一种广泛特异性的酶，苹果酸异丙酯脱氢酶（MJ0720）催化β-异丙基苹果酸，β-甲基苹果酸和d-苹果酸的氧化脱羧。结合这些结果，系统发育分析表明，丙酮酸通向2-氧代丁酸的途径（异亮氨酸生物合成中苏氨酸脱水酶的替代物）在细菌和古细菌中
• Oxidation of <scp>d</scp> -Malic and β-Alkylmalic Acids by Wild-Type and Mutant Strains of <i>Salmonella typhimurium</i> and by <i>Aerobacter aerogenes</i>
  作者：Joseph R. Stern、R. W. O'Brien

  DOI：10.1128/jb.98.1.147-151.1969

  日期：1969.4

  A mutant strain of Salmonella typhimurium (SL 1634 dml-51 ) capable of growth on d -malate as sole carbon source was shown to produce d -malic enzyme. This enzyme was absent in the parent wild-type strain which was unable to grow on d -malate. Growth of the mutant on d -malate also resulted in a greatly increased level of β-isopropylmalic enzyme compared with its level in the wild-type strain grown on citrate or l -malate. The d -malic and β-isopropylmalic enzymes, both of which catalyze a nicotinamide adenine dinucleotide- and Mg ⁺⁺ -dependent oxidative decarboxylation of their respective substrates, were shown to be distinct enzymes by selective inhibition with erythro - dl -β-hydroxyaspartate and by other methods. Cell extracts of the mutant strain also oxidized dl -β-methyl-, dl -β-ethyl-, dl -β-propyl- and dl -ββ-dimethylmalates, in order of decreasing activity. dl -β-Methyl-malate was shown to be oxidized by both the d -malic and the β-isopropylmalic enzymes, whereas the oxidation of the other β-alkylmalates appeared to be effected exclusively by the β-isopropylmalic enzyme. β-Isopropylmalic enzyme activity was induced by d -malate but not by l -malate, showing that it behaved as a d -malictype enzyme. Growth of Aerobacter aerogenes on d -malate, which caused induction of d malic enzyme, resulted in only a small increase in the activity of β-isopropylmalic enzyme.

  一种突变株的沙门氏菌鼠伤寒杆菌（SL 1634 dml-51）能够在d-苹果酸作为唯一的碳源下生长，并产生d-苹果酸酶。这种酶在无法在d-苹果酸上生长的野生型菌株中不存在。突变株在d-苹果酸上的生长也导致β-异丙基苹果酸酶的水平大大增加，与野生型菌株在柠檬酸或l-苹果酸上生长时的水平相比。d-苹果酸酶和β-异丙基苹果酸酶都催化其各自底物的烟酰胺腺嘌呤二核苷酸和Mg++依赖性氧化脱羧反应，通过选择性抑制剂erythro-dl-β-羟基天冬氨酸和其他方法，证明它们是不同的酶。突变株的细胞提取物还能氧化dl-β-甲基、dl-β-乙基、dl-β-丙基和dl-ββ-二甲基苹果酸，活性依次降低。β-异丙基苹果酸酶和d-苹果酸诱导活性，但不是l-苹果酸，表明它的行为类似于d-苹果酸型酶。在d-苹果酸上生长的气生杆菌，导致d-苹果酸酶的诱导，只导致β-异丙基苹果酸酶活性略微增加。
• Properties of Succinyl-Coenzyme A:<scp>d</scp>-Citramalate Coenzyme A Transferase and Its Role in the Autotrophic 3-Hydroxypropionate Cycle of<i>Chloroflexus aurantiacus</i>
  作者：Silke Friedmann、Birgit E. Alber、Georg Fuchs

  DOI：10.1128/jb.00659-06

  日期：2006.9.15

  The phototrophic bacteriumChloroflexus aurantiacususes the 3-hydroxypropionate cycle for autotrophic CO₂fixation. This cycle starts with acetyl-coenzyme A (CoA) and produces glyoxylate. Glyoxylate is an unconventional cell carbon precursor that needs special enzymes for assimilation. Glyoxylate is combined with propionyl-CoA to β-methylmalyl-CoA, which is converted to citramalate. Cell extracts catalyzed the succinyl-CoA-dependent conversion of citramalate to acetyl-CoA and pyruvate, the central cell carbon precursor. This reaction is due to the combined action of enzymes that were upregulated during autotrophic growth, a coenzyme A transferase with the use of succinyl-CoA as the CoA donor and a lyase cleaving citramalyl-CoA to acetyl-CoA and pyruvate. Genomic analysis identified a gene coding for a putative coenzyme A transferase. The gene was heterologously expressed inEscherichia coliand shown to code for succinyl-CoA:d-citramalate coenzyme A transferase. This enzyme, which catalyzes the reactiond-citramalate + succinyl-CoA →d-citramalyl-CoA + succinate, was purified and studied. It belongs to class III of the coenzyme A transferase enzyme family, with an aspartate residue in the active site. The homodimeric enzyme composed of 44-kDa subunits was specific for succinyl-CoA as a CoA donor but also acceptedd-malate and itaconate instead ofd-citramalate. The CoA transferase gene is part of a cluster of genes which are cotranscribed, including the gene ford-citramalyl-CoA lyase. It is proposed that the CoA transferase and the lyase catalyze the last two steps in the glyoxylate assimilation route.

  摘要光营养细菌欧氏绿僵菌利用 3-羟基丙酸循环进行自养型二氧化碳固定。该循环以乙酰辅酶 A（CoA）为起点，产生乙醛酸。乙醛酸是一种非常规的细胞碳前体，需要特殊的酶进行同化。乙醛酸与丙酰-CoA 结合生成 β-甲基丙酰-CoA，然后转化为柠檬醛酸。细胞提取物催化琥珀酰-CoA 依赖性地将柠檬醛酸转化为乙酰-CoA 和丙酮酸（细胞的核心碳前体）。这一反应是由于自养生长过程中上调的酶的联合作用，即使用琥珀酰-CoA 作为 CoA 供体的辅酶 A 转移酶和将柠檬酰-CoA 分解为乙酰-CoA 和丙酮酸的裂解酶。基因组分析确定了一个编码推定辅酶 A 转移酶的基因。该基因在大肠杆菌（Escherichia coli）中进行异源表达，结果显示其编码为琥珀酰-CoA：d-柠檬醛酸辅酶 A 转移酶。对这种催化d-柠檬醛酸+琥珀酰-CoA →d-柠檬醛酸-CoA+琥珀酸反应的酶进行了纯化和研究。它属于辅酶 A 转移酶家族的第三类，活性位点上有一个天冬氨酸残基。这种由 44 kDa 亚基组成的同源二聚体酶对作为 CoA 供体的琥珀酰-CoA 具有特异性，但也接受 d-苹果酸和伊塔康酸，而不是 d-柠檬酸。CoA 转移酶基因是包括 d-柠檬酰-CoA 裂解酶基因在内的同源转录基因簇的一部分。据推测，CoA 转移酶和裂解酶催化乙醛酸同化途径的最后两个步骤。