T. Kawamura, S. Takanawa, H. Ashida, S. Muranaka, A. Murota, S. Kota, A. Maeda, R. Hashimoto, E. Matsui, K. Takayama
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In particular, we focused on melanin synthesis inhibition and used the water-soluble fraction of <i>Curtobacterium</i> and the melanin synthase in vitro human tyrosinase activity assay to examine its inhibitory effects on monophenolase activity, which converts Tyr to L-3,4-dihydroxyphenylalanine (L-DOPA), and diphenolase activity, which uses L-DOPA as a substrate to produce L-dopaquinone. The results demonstrated that the water-soluble fraction of bacterial secretion inhibited monophenolase activity but not diphenolase activity. Additionally, we discovered a compound with the molecular weight of approximately 379.2 Da and the tyrosinase inhibitory effect in which two protons were bound in the absence of copper ions and copper ions were bound instead when they were present in the water-soluble fraction of the bacterial secretion. Since the enzymatic activity of tyrosinase is copper ion-dependent, <i>Curtobacterium</i> may be able to suppress the browning caused by the copper-binding compound-induced oxidation of phenols, such as Tyr, allowing it to express a bright flash-yellow color.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0000,"publicationDate":"2024-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"How Does Curtobacterium Produce a Bright Flash-Yellow Color?\",\"authors\":\"T. Kawamura, S. Takanawa, H. Ashida, S. Muranaka, A. Murota, S. Kota, A. Maeda, R. Hashimoto, E. Matsui, K. Takayama\",\"doi\":\"10.1134/S0003683823602895\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><i>Curtobacterium</i>, a bright flash-yellow color-producing bacterium, has been isolated from the body fluid of the pupae of <i>Graphium sarpedon</i>. 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引用次数: 0
摘要
摘要 从石斑鱼蛹的体液中分离出了一种能产生明亮闪光黄色的细菌--龟裂菌。通过几项实验,确定了这种细菌表现出鲜艳颜色的三种机制。第一种是黄色色素沉着造成的;第二种是由于一种吸收蓝光并发出绿色荧光的物质造成的;第三种是通过抑制黑色素合成来排除褐色的过程。其中,我们以黑色素合成抑制为研究重点,利用杯状杆菌的水溶性部分和黑色素合成酶体外人体酪氨酸酶活性测定法,研究其对将Tyr转化为L-3,4-二羟基苯丙氨酸(L-DOPA)的单苯酚酶活性和以L-DOPA为底物生成L-多巴醌的二苯酚酶活性的抑制作用。结果表明,细菌分泌物中的水溶性部分能抑制单苯酚酶的活性,但不能抑制二苯酚酶的活性。此外,我们还发现了一种分子量约为 379.2 Da 的化合物,它具有抑制酪氨酸酶的作用,在没有铜离子的情况下,该化合物与两个质子结合,而当铜离子存在于细菌分泌物的水溶性部分时,则与之结合。由于酪氨酸酶的酶活性依赖于铜离子,因此龟毛杆菌可能能够抑制铜结合化合物诱导的酚类(如 Tyr)氧化引起的褐变,使其表现出明亮的闪黄色。
How Does Curtobacterium Produce a Bright Flash-Yellow Color?
Curtobacterium, a bright flash-yellow color-producing bacterium, has been isolated from the body fluid of the pupae of Graphium sarpedon. Several experiments were conducted to identify three mechanisms by which this bacterium expresses a vibrant color. The first is caused by yellow pigmentation; the second is due to a substance that absorbs blue light and emits green fluorescence; and the third is a process that excludes brownish colors by inhibiting melanin synthesis. In particular, we focused on melanin synthesis inhibition and used the water-soluble fraction of Curtobacterium and the melanin synthase in vitro human tyrosinase activity assay to examine its inhibitory effects on monophenolase activity, which converts Tyr to L-3,4-dihydroxyphenylalanine (L-DOPA), and diphenolase activity, which uses L-DOPA as a substrate to produce L-dopaquinone. The results demonstrated that the water-soluble fraction of bacterial secretion inhibited monophenolase activity but not diphenolase activity. Additionally, we discovered a compound with the molecular weight of approximately 379.2 Da and the tyrosinase inhibitory effect in which two protons were bound in the absence of copper ions and copper ions were bound instead when they were present in the water-soluble fraction of the bacterial secretion. Since the enzymatic activity of tyrosinase is copper ion-dependent, Curtobacterium may be able to suppress the browning caused by the copper-binding compound-induced oxidation of phenols, such as Tyr, allowing it to express a bright flash-yellow color.
期刊介绍:
Applied Biochemistry and Microbiology is an international peer reviewed journal that publishes original articles on biochemistry and microbiology that have or may have practical applications. The studies include: enzymes and mechanisms of enzymatic reactions, biosynthesis of low and high molecular physiologically active compounds; the studies of their structure and properties; biogenesis and pathways of their regulation; metabolism of producers of biologically active compounds, biocatalysis in organic synthesis, applied genetics of microorganisms, applied enzymology; protein and metabolic engineering, biochemical bases of phytoimmunity, applied aspects of biochemical and immunochemical analysis; biodegradation of xenobiotics; biosensors; biomedical research (without clinical studies). Along with experimental works, the journal publishes descriptions of novel research techniques and reviews on selected topics.