Crystals of taka-amylase A, a cornerstone of protein chemistry in Japan.

IF 4.4 3区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES Proceedings of the Japan Academy. Series B, Physical and Biological Sciences Pub Date : 2024-01-01 DOI:10.2183/pjab.100.027
Saburo Aimoto, Naoto Minamino, Takeshi Ishimizu, Masami Kusunoki
{"title":"Crystals of taka-amylase A, a cornerstone of protein chemistry in Japan.","authors":"Saburo Aimoto, Naoto Minamino, Takeshi Ishimizu, Masami Kusunoki","doi":"10.2183/pjab.100.027","DOIUrl":null,"url":null,"abstract":"<p><p>In 1935, Shiro Akabori began research on the preparation of taka-amylase A with a purity suitable for chemical research, with the intention of elucidating the chemical nature of the enzyme. He succeeded in developing a method to efficiently obtain crystallized taka-amylase A from Aspergillus oryzae. Using crystallized taka-amylase A as the starting material, a series of studies were conducted to determine its amino acid composition and sequence, sugar chain structure, and three-dimensional structure. Based on these results, the molecular structure and catalytic mechanism of taka-amylase A were elucidated. The scientific achievements from research on taka-amylase A significantly enhanced Japan's capabilities in protein research, represented by the fact that taka-amylase A was the first amylase in the world for which both chemical and crystallographic structures were elucidated.</p>","PeriodicalId":20707,"journal":{"name":"Proceedings of the Japan Academy. Series B, Physical and Biological Sciences","volume":"100 8","pages":"429-445"},"PeriodicalIF":4.4000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11535007/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of the Japan Academy. Series B, Physical and Biological Sciences","FirstCategoryId":"103","ListUrlMain":"https://doi.org/10.2183/pjab.100.027","RegionNum":3,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
引用次数: 0

Abstract

In 1935, Shiro Akabori began research on the preparation of taka-amylase A with a purity suitable for chemical research, with the intention of elucidating the chemical nature of the enzyme. He succeeded in developing a method to efficiently obtain crystallized taka-amylase A from Aspergillus oryzae. Using crystallized taka-amylase A as the starting material, a series of studies were conducted to determine its amino acid composition and sequence, sugar chain structure, and three-dimensional structure. Based on these results, the molecular structure and catalytic mechanism of taka-amylase A were elucidated. The scientific achievements from research on taka-amylase A significantly enhanced Japan's capabilities in protein research, represented by the fact that taka-amylase A was the first amylase in the world for which both chemical and crystallographic structures were elucidated.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
日本蛋白质化学的基石--高淀粉酶 A 的晶体。
1935 年,赤堀史郎开始研究如何制备纯度适合化学研究的高淀粉酶 A,目的是阐明这种酶的化学本质。他成功地开发出一种从黑曲霉中高效获取结晶高淀粉酶 A 的方法。以结晶的高淀粉酶 A 为起始材料,进行了一系列研究,以确定其氨基酸组成和序列、糖链结构和三维结构。在此基础上,阐明了高卡淀粉酶 A 的分子结构和催化机理。高淀粉酶 A 是世界上第一个同时阐明了化学结构和晶体结构的淀粉酶,由此可见,高淀粉酶 A 研究取得的科研成果大大提高了日本在蛋白质研究方面的能力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
CiteScore
6.60
自引率
0.00%
发文量
26
审稿时长
>12 weeks
期刊介绍: The Proceedings of the Japan Academy Ser. B (PJA-B) is a scientific publication of the Japan Academy with a 90-year history, and covers all branches of natural sciences, except for mathematics, which is covered by the PJA-A. It is published ten times a year and is distributed widely throughout the world and can be read and obtained free of charge through the world wide web.
期刊最新文献
Incorporation of photosynthetically active algal chloroplasts in cultured mammalian cells towards photosynthesis in animals. Cloning of human Type I interferon cDNAs. Origin of an orbiting star around the galactic supermassive black hole. Changes in the expression of mexB, mexY, and oprD in clinical Pseudomonas aeruginosa isolates. Complementary use of visual and olfactory cues to assess capture of Bactrocera dorsalis (Hendel): Implementation and field verification via an IoT-based automatic monitoring system.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1