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首页> 外文期刊>The Journal of Antibiotics: An International Journal >Amide compound synthesis by adenylation domain of bacillibactin synthetase
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Amide compound synthesis by adenylation domain of bacillibactin synthetase

机译：氨基酰胺化合物的氨基酰胺酰胺酰胺合成酶的酰胺化合物合成

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摘要

The adenylation domain of nonribosomal peptide synthetase (NRPS) is responsible for the selective substrate recognition and its activation (as an acyl-O-AMP intermediate) during ATP consumption. DhbE, a stand-alone adenylation domain, acts on an aromatic acid, 2,3-dihydroxybenzoic acid (DHB). This activation is the initial step of the synthesis of bacillibactin that is a high-affinity small-molecule iron chelator also termed siderophore. Subsequently, the activated DHB is transferred and attached covalently to a peptidyl carrier protein domain via a thioester bond. Adenylation domains belong to the superfamily of adenylate-forming enzymes including acetyl-CoA synthetase, acyl-CoA synthetase and firefly luciferase. We previously reported a novel N-acylation reaction for an acyl-CoA synthetase (AcsA) that originally catalyzes the formation of a thioester bond between an acid and CoA, yielding acyl-CoA. This novel reaction was also confirmed for acetyl-CoA synthetase and firefly luciferase, but not yet for an adenylation domain. Here, we for the first time demonstrated the synthesis of N-acyl-L-cysteine by a stand-alone adenylation domain, DhbE. When DHB and L-cysteine were used as substrates of DhbE, N-DHB-L-cysteine was formed. A V-max value of 0.0156 +/- 0.0008 units mg(-1) and K-m values of 150 +/- 18.3 mm for L-cysteine and 0.0579 +/- 0.0260 mm for DHB were obtained in this novel reaction. Furthermore, DhbE synthesized N-benzoyl-L-cysteine when benzoic acid and L-cysteine were used as substrates. Through the N-acylation reaction of DhbE, we also succeeded in the synthesis of N-aromatic acyl compounds that have never previously been reported to be produced by this enzymatic method.
机译：非纤维素肽合成酶（NRPS）的腺化结构域是在ATP消耗期间选择性底物识别及其活化（作为酰基-O-AMP中间体）的原因。 DHBE，一种独立的腺苷酸域，作用于芳香酸，2,3-二羟基苯甲酸（DHB）。这种活化是合成Bacillibactin的初始步骤，其是一种高亲和力的小分子铁螯合剂，也称为载体。随后，通过硫酯键将活化的DHB转移并与肽基载体蛋白质结构溶液共价连接。腺苷酸化结构域属于腺苷酸形成酶的超家族，包括乙酰-COA合成酶，酰基-CoA合成酶和萤火虫荧光素酶。我们之前报道了一种新的N-酰化反应，其用于酰基-CoA合成酶（ACSA），其最初催化酸和柯等之间形成硫酯键，得到酰基-COA。该新型反应还证实了乙酰-CoA合成酶和萤火虫荧光素酶，但尚未用于腺苷酸化结构域。在这里，我们首次证明了通过独立的腺苷酸域，DHBE的合成N-酰基-1-半胱氨酸。当使用DHB和L-半胱氨酸作为DHBE的底物时，形成N-DHB-L-半胱氨酸。在这种新的反应中获得了L-半胱氨酸的0.0156 +/- 0.0008单元Mg（-1）和150 +/- 18.3mm的0.0156 +/- 0.0008单位的V-max值和k-m值为DHB的0.0579 +/- 0.0260mm。此外，当使用苯甲酸和L-半胱氨酸作为基质时，DHBE合成N-苯甲酰基半胱氨酸。通过DHBE的N-酰化反应，我们也成功地合成了从未申报过的酶法生产的N-芳族酰基化合物。

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    Abe Tomoko; Hashimoto Yoshiteru; Sugimoto Sayaka; Kobayashi Kenta; Kumano Takuto; Kobayashi Michihiko;

  • 作者单位

    Univ Tsukuba Grad Sch Life &

    Environm Sci Inst Appl Biochem 1-1-1 Tennodai Tsukuba Ibaraki;

    Univ Tsukuba Grad Sch Life &

    Environm Sci Inst Appl Biochem 1-1-1 Tennodai Tsukuba Ibaraki;

    Univ Tsukuba Grad Sch Life &

    Environm Sci Inst Appl Biochem 1-1-1 Tennodai Tsukuba Ibaraki;

    Tokyo Denki Univ Sch Sci &

    Engn Div Life Sci &

    Engn Saitama Japan;

    Univ Tsukuba Grad Sch Life &

    Environm Sci Inst Appl Biochem 1-1-1 Tennodai Tsukuba Ibaraki;

    Univ Tsukuba Grad Sch Life &

    Environm Sci Inst Appl Biochem 1-1-1 Tennodai Tsukuba Ibaraki;

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  • 正文语种 eng
  • 中图分类 药学;
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