Enzymatic transformation of -chloroalanine into useful amino acids

将β-氯丙氨酸酶促转化为有用的氨基酸

基本信息

  • 批准号:
    61560117
  • 负责人:
  • 金额:
    $ 1.22万
  • 依托单位:
  • 依托单位国家:
    日本
  • 项目类别:
    Grant-in-Aid for General Scientific Research (C)
  • 财政年份:
    1986
  • 资助国家:
    日本
  • 起止时间:
    1986 至 1987
  • 项目状态:
    已结题

项目摘要

Recent development of chemical synthesis techniques has made it possible to produce <beta>-chloroalanine economically on a large scale. The enzymatic transformation of chemically synthesized <beta>-chloroalanie into useful amino acids was studied. We isolated microorganisms, Bacillus sphaericus L-118 and Pseudomonas putida CR1-1 which are resistant to <beta>-chloro-L-alanine and -chloro-D-alanine, respectively. The formation of O-acetylserine sulfhydrylase of B. sphaericus L-118, was highly enhanced by (beta)-chloro-L-alanine to the medium. The enzyme catalyzes the <beta>-replacement reaction of <beta>-chloroalanine in the presence of sulfide to produce L-cysteine. We optimized the reaction conditions for the enzymatic production of L-cysteine. Under the optimum conditions. 70 g of L-cysteine/L of reaction mixture was produced (conversion yield 80%). In the crude cell extract of P. putida CR 1-1, we found the new enzyme, <beta>-chloro-D-alanine dehydrochlorinase which catalyzes the <beta>-replacement reaction of <beta>-chloro-D-alanine in the presence of sulfide to produce D-cysteine. When various thiol compounds were added instead of sulfide, the corresponding Salkyl-D-cysteine was synthesized. We optimized the reaction conditions to produce D-cysteine. Under the optimal condition, 22.6 g of D-cysteine/L of reaction mixture was produced (conversion yield 100%). D-Cysteine and its derivatives are useful for the production of the semi-synthetic cephalosporin antibiotics.
最近化学合成技术的发展使大规模经济地生产β-氯丙氨酸成为可能。研究了化学合成的&lt;β&gt;-氯丙氨酸的酶转化为有用氨基酸的方法。我们分离到的球形芽孢杆菌L-118和恶臭假单胞菌CR1-1分别对-氯-L-丙氨酸和-氯-D-丙氨酸产生抗性。(β)-氯-L-丙氨酸对球形芽孢杆菌L-118O-乙酰丝氨酸硫基酶的形成有显著促进作用。该酶催化&lt;β&gt;-氯丙氨酸在硫化物存在下的&lt;β&gt;-取代反应生成L-半胱氨酸。对酶法生产L-半胱氨酸的反应条件进行了优化。在最佳条件下。得到了L-半胱氨酸/L反应混合物70g(转化率80%)。在恶臭假单胞菌CR1-1的粗细胞提取液中,我们发现了一种新的酶&lt;β&gt;-氯-D-丙氨酸脱氢酶,它催化&lt;β&gt;-氯-D-丙氨酸在硫化物存在下发生置换反应,生成D-半胱氨酸。当不同的硫醇化合物取代硫化物时,合成了相应的水杨基-D-半胱氨酸。对合成D-半胱氨酸的反应条件进行了优化。在最佳反应条件下,D-半胱氨酸/L的产率为22.6g(转化率为100%)。D-半胱氨酸及其衍生物用于生产半合成头孢菌素抗生素。

项目成果

期刊论文数量(5)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Toru Nagasawa: "Methods in Enzymology" Academic Press, (1987)
长泽彻:《酶学方法》学术出版社,(1987)
  • DOI:
  • 发表时间:
  • 期刊:
  • 影响因子:
    0
  • 作者:
  • 通讯作者:
Toru Nagasawa: Appl.Biochem.Biotechnol.13. 145-165 (1986)
长泽彻:Appl.Biochem.Biotechnol.13。
  • DOI:
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    0
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  • 通讯作者:
Toru Nagasawa: "Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1" Archives of Microbiology.
Toru Nagasawa:“大肠杆菌 D-半胱氨酸脱硫酶与恶臭假单胞菌 CR 1-1 的 3-氯-D-丙氨酸脱氢氯化酶的生理比较”微生物学档案。
  • DOI:
  • 发表时间:
  • 期刊:
  • 影响因子:
    0
  • 作者:
  • 通讯作者:
長沢透: 日本農芸化学会誌. 61. 165-174 (1987)
长泽彻:日本农业化学学会杂志 61. 165-174 (1987)。
  • DOI:
  • 发表时间:
  • 期刊:
  • 影响因子:
    0
  • 作者:
  • 通讯作者:
Toru Nagasawa: European Journal of Biochemistry. 153. 541-551 (1985)
长泽彻:欧洲生物化学杂志。
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    0
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NAGASAWA Toru其他文献

Association between Job Stress and Number of Physical Symptoms among Female Nurses of Medical-university-affiliated Hospitals
医科大学附属医院女护士工作压力与躯体症状数的相关性
  • DOI:
    10.1265/jjh.73.388
  • 发表时间:
    2018
  • 期刊:
  • 影响因子:
    0
  • 作者:
    YOSHIOKA Nozomi;NOMURA Kyoko;ASAYAMA Kei;TAKENOSHITA Shinichi;NAGASAWA Toru;NAKATA Yoshinori;HIRAIKE Haruko;SASAMORI Yukifumi;TSUCHIYA Akiko;OHKUBO Takayoshi;OKINAGA Hiroko
  • 通讯作者:
    OKINAGA Hiroko

NAGASAWA Toru的其他文献

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{{ truncateString('NAGASAWA Toru', 18)}}的其他基金

Library construction of decarboxylases catalyzing carbon dioxide fixation and their application for the production of various aromatic carboxylic acids
催化二氧化碳固定的脱羧酶文库构建及其在多种芳香族羧酸生产中的应用
  • 批准号:
    21580091
  • 财政年份:
    2009
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
Studies on Kolbe・Schmitt Reaction catalyzed by microbial decarboxylases and its application for the production of aromatic hydroxy carboxylic acids
微生物脱羧酶催化科尔贝·施密特反应及其在芳香族羟基羧酸生产中的应用研究
  • 批准号:
    19580087
  • 财政年份:
    2007
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
Highly functional utilization of surplus renewable resources through microbial regio-specific hydroxylation
通过微生物区域特异性羟基化对剩余可再生资源进行高度功能化利用
  • 批准号:
    14560062
  • 财政年份:
    2002
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
Findinf of novel decarboxylases which catalyzes carbon dioxide fixation and establishment of the precise conversion techniques of carbon dioxide
催化二氧化碳固定的新型脱羧酶的发现及二氧化碳精准转化技术的建立
  • 批准号:
    12559003
  • 财政年份:
    2000
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Construction of library of useful nitrile hydratase for various industrial needs
构建适合各种工业需求的有用腈水合酶库
  • 批准号:
    11660080
  • 财政年份:
    1999
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
The novel hydroxylation reaction of nicotinic acid catalyzed by the cooperation of yeat and bacteria
酵母与细菌协同催化烟酸羟基化反应
  • 批准号:
    09660093
  • 财政年份:
    1997
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
Enzymatic synthesis of an important building block for the new nicotinyl pesticides
新型烟基农药重要组成部分的酶法合成
  • 批准号:
    07556025
  • 财政年份:
    1995
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Scientific Research (A)
New Function of Halohydrin Epoxidase and Its Application of the Synthesis of Chiral Building Block.
卤代醇环氧化酶的新功能及其在手性构件合成中的应用。
  • 批准号:
    05660088
  • 财政年份:
    1993
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for General Scientific Research (C)
Studies on the cofactors and reaction mechanisms of nitrile hydratase which is useful for the synthesis of amides
用于酰胺合成的腈水合酶的辅因子和反应机制的研究
  • 批准号:
    02660114
  • 财政年份:
    1990
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for General Scientific Research (C)
Develop a new technique for measuring tongue and mandibular movement
开发测量舌头和下颌运动的新技术
  • 批准号:
    63870075
  • 财政年份:
    1988
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Grant-in-Aid for Developmental Scientific Research

相似海外基金

Sulfur amino acid metabolism in plants and bacteria: enzymology and gene regulation of cystahionine gamma-synthase and o-acetylserine sulfhydrylase
植物和细菌中的硫氨基酸代谢:胱硫醚γ-合酶和邻乙酰丝氨酸硫化氢解酶的酶学和基因调控
  • 批准号:
    298269-2004
  • 财政年份:
    2008
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Discovery Grants Program - Individual
Sulfur amino acid metabolism in plants and bacteria: enzymology and gene regulation of cystahionine gamma-synthase and o-acetylserine sulfhydrylase
植物和细菌中的硫氨基酸代谢:胱硫醚γ-合酶和邻乙酰丝氨酸硫化氢解酶的酶学和基因调控
  • 批准号:
    298269-2004
  • 财政年份:
    2007
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Discovery Grants Program - Individual
Sulfur amino acid metabolism in plants and bacteria: enzymology and gene regulation of cystahionine gamma-synthase and o-acetylserine sulfhydrylase
植物和细菌中的硫氨基酸代谢:胱硫醚γ-合酶和邻乙酰丝氨酸硫化氢解酶的酶学和基因调控
  • 批准号:
    298269-2004
  • 财政年份:
    2006
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Discovery Grants Program - Individual
Sulfur amino acid metabolism in plants and bacteria: enzymology and gene regulation of cystahionine gamma-synthase and o-acetylserine sulfhydrylase
植物和细菌中的硫氨基酸代谢:胱硫醚γ-合酶和邻乙酰丝氨酸硫化氢解酶的酶学和基因调控
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    298269-2004
  • 财政年份:
    2005
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Discovery Grants Program - Individual
Sulfur amino acid metabolism in plants and bacteria: enzymology and gene regulation of cystahionine gamma-synthase and o-acetylserine sulfhydrylase
植物和细菌中的硫氨基酸代谢:胱硫醚γ-合酶和邻乙酰丝氨酸硫化氢解酶的酶学和基因调控
  • 批准号:
    298269-2004
  • 财政年份:
    2004
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Discovery Grants Program - Individual
Mechanism of the B6 Enzyme, O-Acetylserine Sulfhydrylase
B6 酶 O-乙酰丝氨酸硫酸化酶的机制
  • 批准号:
    9729609
  • 财政年份:
    1998
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Continuing Grant
Mechanism of the B6 Enzyme O-Acetylserine Sulfhydrylase
B6 酶 O-乙酰丝氨酸硫酸化酶的机制
  • 批准号:
    8812701
  • 财政年份:
    1989
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Continuing Grant
Mechanism of the B6 Enzyme O-Acetylserine Sulfhydrylase
B6 酶 O-乙酰丝氨酸硫酸化酶的机制
  • 批准号:
    8912053
  • 财政年份:
    1989
  • 资助金额:
    $ 1.22万
  • 项目类别:
    Continuing Grant
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