共查询到19条相似文献,搜索用时 189 毫秒
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手性芳醇是合成手性化合物的重要中间体.本文从近几年来发展起来的生物催化的催化剂筛选、催化反应体系等领域,综述了生物不对称还原合成手性芳醇及其衍生物的研究进展. 相似文献
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手性氰醇是一类重要的手性药物与农药中间体,并能够转化成具有不同官能团的光学活性中间体,在手性药物的合成中具有极其重要的地位。本文从氰醇醛缩酶的来源、酶催化合成手性氰醇的条件因素等几个方面系统介绍了手性氰醇的酶催化合成研究进展以及手性氰醇的应用。 相似文献
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不对称合成是当前有机合成中热门研究领域,利用手性金属络合物催化剂催化不对称硅氢化、烷基化,以烯烃、酮、亚胺、醛等合成手性醇、手性胺、手性酮等具有很好的工业应用前景。本文论述了手性金属络合物催化剂在不对称硅氢化反应及其在二烷基锌对醛的不对称烷基化反应中的应用。 相似文献
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药物分子的立体化学决定其生物活性,手性已成为药物研究的一个关键因素。利用微生物或酶催化的方法进行手性化合物的不对称合成已经成为一个极具吸引力的方向。综述了近年来利用面包酵母催化不对称合成手性化合物的研究进展,着重讨论了利用面包酵母可进行的多种手性试剂的催化合成的反应类型。 相似文献
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Optically pure (R)-γ-and (R)-δ-lactones can be prepared by intramolecular cyclization of chiral hydroxy acids/ esters reduced asymmetrically from γ-and δ-keto acids/esters using Saccharomyces cerevisiae (S.cerevisiae) as a whole-cell biocatalyst.However,some of the enzymes catalyzing these reactions in S.cerevisiae are still unknown up to date.In this report,two carbonyl reductases,OdCR1 and OdCR2,were successfully discovered,and cloned from S.cerevisiae using a genome-mining approach,and overexpressed in Escherichia coli (E.coli).Compared with OdCR1,OdCR2 can reduce 4-oxodecanoic acid and 5-oxodecanoic acid asymmetrically with higher stereoselectivity,generating (R)-γ-decalactone (99% ee) and (R)-δ-decalactone (98% ee) in 85% and 92% yields,respectively.This is the first report of native enzymes from S.cerevisiae for the enzymatic synthesis of chiral γ-and δ-lactones which is of wide uses in food and cosmetic industries. 相似文献
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2,4-二氯-α-氯甲基苯甲醇是合成硝酸咪(益)康唑、抑霉唑等的重要中间体,具有非常广泛的用途。参考了国内有关2,4-二氯-α-氯甲基苯甲醇合成的文献,综述了我国2,4-二氯-α-氯甲基苯甲醇的合成研究,提出了孔分子筛中负载金属氧化物、手性配体等活性组分将是今后研究发展的主要方向。 相似文献
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以混合溶剂法由D 氨基酸和异氰酸酯制备一系列3,5 二取代手性海因,用大孔吸附树脂作载体,制成固载型手性催化剂,并考察了不同结构手性海因化合物在3 苯氧基苯甲醛氰醇化反应中的催化活性。结果表明,所采用的手性海因制备方法简便,在(S) α 氰基 3 苯氧基苯甲醇的不对称合成中表现了较好的对映选择性,其氰醇ee值约为20%~35.5%。 相似文献
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Optically pure (R)-γ- and (R)-δ-lactones can be prepared by intramolecular cyclization of chiral hydroxy acids/esters reduced asymmetrically from γ- and δ-keto acids/esters using Saccharomyces cerevisiae (S. cerevisiae) as a whole-cell biocatalyst. However, some of the enzymes catalyzing these reactions in S. cerevisiae are still unknown up to date. In this report, two carbonyl reductases, OdCR1 and OdCR2, were successfully discovered, and cloned from S. cerevisiae using a genome-mining approach, and overexpressed in Escherichia coli (E. coli). Compared with OdCR1, OdCR2 can reduce 4-oxodecanoic acid and 5-oxodecanoic acid asymmetrically with higher stereoselectivity, generating (R)-γ-decalactone (99% ee) and (R)-δ-decalactone (98% ee) in 85% and 92% yields, respectively. This is the first report of native enzymes from S. cerevisiae for the enzymatic synthesis of chiral γ- and δ-lactones which is of wide uses in food and cosmetic industries. 相似文献
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二烷基锌对醛的不对称加成反应是合成手性二级醇的有效方法,反应产物手性二级醇是药物、精细化学品、天然产物的重要中间体,手性氨基醇是诱导这类反应手性配体的重要组成部分并且表现出了很高的对映选择性。综述了催化该类反应手性氨基醇配体的一些研究新进展。 相似文献
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LUAN Pengqian ZHOU Dandan WANG Xiaotian CHEN Ran GAO Shiqi ZHAO Hao HUANG Chen LIU Yunting GAO Jing JIANG Yanjun 《化工学报》2021,71(12):5361-5375
The chemoenzymatic cascade catalysis combines the broad reactivity of chemical catalysis with the high selectivity of biocatalysis, and is an effective way to asymmetrically synthesize high value-added chiral compounds. However, the incompatibilities between the chemo- and biocatalysts as well as between their respective reaction conditions greatly restricted the development of this field. The design of feasible approaches to solve these problems can achieve the compatibility and complementary advantages of the two catalytic categories, thus making the chemoenzymatic cascade catalytic reactions more widely applied. In this review, the recent progress in developing strategies to overcome the incompatibility between chemical catalysis and enzymatic catalysis, such as temporal separation, spatial separation and integrated catalysts, is reviewed. The applications of chemoenzymatic cascade catalysis in dynamic kinetic resolution of chiral compounds and synthesis of chiral drugs are also introduced. Finally, the future limitations and the development trends of this field are prospected. 相似文献
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化学-酶级联催化结合了化学催化的广泛反应性与生物催化的高选择性,是不对称合成高附加值手性化合物的有效途径。然而,化学催化剂和酶之间以及它们反应条件之间的不相容性极大地限制了这一领域的发展。因此设计可行的方法解决这些问题,实现两种催化范畴的兼容和优势互补,将使化学-酶级联催化反应得到更广泛的应用。综述了近年来克服化学催化与酶催化不相容性所采取的一些策略以及相关的研究进展,如时间分隔、空间分隔和集成催化剂等,并介绍了化学-酶级联催化在手性化合物动态动力学拆分及手性药物合成方面的应用,最后展望了该领域未来的局限性和发展趋势。 相似文献
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Ziegelmann-Fjeld KI Musa MM Phillips RS Zeikus JG Vieille C 《Protein engineering, design & selection : PEDS》2007,20(2):47-55
The secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus 39E (TeSADH) is highly thermostable and solvent-stable, and it is active on a broad range of substrates. These properties make TeSADH an excellent template to engineer an industrial catalyst for chiral chemical synthesis. (S)-1-Phenyl-2-propanol was our target product because it is a precursor to major pharmaceuticals containing secondary alcohol groups. TeSADH has no detectable activity on this alcohol, but it is highly active on 2-butanol. The structural model we used to plan our mutagenesis strategy was based on the substrate's orientation in a horse liver alcohol dehydrogenase*p-bromobenzyl alcohol*NAD(+) ternary complex (PDB entry 1HLD). The W110A TeSADH mutant now uses (S)-1-phenyl-2-propanol, (S)-4-phenyl-2-butanol and the corresponding ketones as substrates. W110A TeSADH's kinetic parameters on these substrates are in the same range as those of TeSADH on 2-butanol, making W110A TeSADH an excellent catalyst. In particular, W110A TeSADH is twice as efficient on benzylacetone as TeSADH is on 2-butanol, and it produces (S)-4-phenyl-2-butanol from benzylacetone with an enantiomeric excess above 99%. W110A TeSADH is optimally active at 87.5 degrees C and remains highly thermostable. W110A TeSADH is active on aryl derivatives of phenylacetone and benzylacetone, making this enzyme a potentially useful catalyst for the chiral synthesis of aryl derivatives of alcohols. As a control in our engineering approach, we used the TbSADH*(S)-2-butanol binary complex (PDB entry 1BXZ) as the template to model a mutation that would make TeSADH active on (S)-1-phenyl-2-propanol. Mutant Y267G TeSADH did not have the substrate specificity predicted in this modeling study. Our results suggest that (S)-2-butanol's orientation in the TbSADH*(S)-2-butanol binary complex does not reflect its orientation in the ternary enzyme-substrate-cofactor complex. 相似文献