Binding Site of Cerulenin in Fatty Acid Synthetase1 (original) (raw)
Journal Article
,
*
Institute of Applied Microbiology, The University of Tokyo
Bunkyo-ku, Tokyo 113
Search for other works by this author on:
,
**
Department of Biology, College of Arts and Sciences, The University of Tokyo
Meguro-ku, Tokyo 153
2 To whom correspondence should be addressed.
Search for other works by this author on:
,
***
The Kitasato Institute, Shirogane
Minato-ku, Tokyo 108
Search for other works by this author on:
,
***
The Kitasato Institute, Shirogane
Minato-ku, Tokyo 108
Search for other works by this author on:
,
***
The Kitasato Institute, Shirogane
Minato-ku, Tokyo 108
Search for other works by this author on:
*
Institute of Applied Microbiology, The University of Tokyo
Bunkyo-ku, Tokyo 113
Search for other works by this author on:
Received:
05 December 1988
Cite
Hiroshi Funabashi, Akihiko Kawaguchi, Hiroshi Tomoda, Satoshi Ömura, Shigenobu Okuda, Shigeo Iwasaki, Binding Site of Cerulenin in Fatty Acid Synthetase, The Journal of Biochemistry, Volume 105, Issue 5, May 1989, Pages 751–755, https://doi.org/10.1093/oxfordjournals.jbchem.a122739
Close
Navbar Search Filter Mobile Enter search term Search
Abstract
An antibiotic cerulenin, (2_R_, 3_S_)-2,3-epoxy-4-oxo-7,10-trans, _trans_-dodecadienamide, irreversibly inhibits fatty acid synthetase from Saccharomyces cerevisiae. Three moles of cerulenin were bound to 1 mol of the enzyme with concomitant loss of its activity. Pretreatment of the enzyme with iodoacetamide reduced the amount of cerulenin bound to the enzyme. Since iodoacetamide is known to specifically bind to the cysteine residue on the condensing reaction domain, cerulenin is considered to bind to the same domain. Tryptic digestion of the [3H]cerulenin-treated enzyme gave a radioactive peptide; its amino acid composition was Asx 1, Thr 1, Ser 1, Glx 2, Pro 1, Gly 1, Ala 1, Val 1, lle 1, and Leu 2. This composition included all the amino acids of the condensing reaction site (Thr-Pro-Val-Gly-Ala-Cys) previously reported by Kresze et al. (Eur. J. Biochem, 79, 181 [1977]) except for Cys. When the enzyme was treated with [3H]cerulenin and digested successively with trypsin and carboxypeptidase P, a [3H]cerulenin-cysteine adduct was isolated as the sole product. This was identified with the adduct chemically synthesized from non-labeled cerulenin and cysteine, and its structure was elucidated by 1H-, 13C-NMR, and fast atom bombardment mass spectrometry. These results indicate that cerulenin, forming a hydroxylactam ring, reacts at its epoxide carbon (C-2 position) with the SH-group of the cysteine residue in the condensing reaction domain of yeast fatty acid synthetase.
This content is only available as a PDF.
© 1989 BY THE JOURNAL OF BIOCHEMISTRY
You do not currently have access to this article.
Personal account
- Sign in with email/username & password
- Get email alerts
- Save searches
- Purchase content
- Activate your purchase/trial code
- Add your ORCID iD
Get help with access
Institutional access
Access to content on Oxford Academic is often provided through institutional subscriptions and purchases. If you are a member of an institution with an active account, you may be able to access content in one of the following ways:
IP based access
Typically, access is provided across an institutional network to a range of IP addresses. This authentication occurs automatically, and it is not possible to sign out of an IP authenticated account.
Sign in through your institution
Choose this option to get remote access when outside your institution. Shibboleth/Open Athens technology is used to provide single sign-on between your institution’s website and Oxford Academic.
- Click Sign in through your institution.
- Select your institution from the list provided, which will take you to your institution's website to sign in.
- When on the institution site, please use the credentials provided by your institution. Do not use an Oxford Academic personal account.
- Following successful sign in, you will be returned to Oxford Academic.
If your institution is not listed or you cannot sign in to your institution’s website, please contact your librarian or administrator.
Sign in with a library card
Enter your library card number to sign in. If you cannot sign in, please contact your librarian.
Society Members
Society member access to a journal is achieved in one of the following ways:
Sign in through society site
Many societies offer single sign-on between the society website and Oxford Academic. If you see ‘Sign in through society site’ in the sign in pane within a journal:
- Click Sign in through society site.
- When on the society site, please use the credentials provided by that society. Do not use an Oxford Academic personal account.
- Following successful sign in, you will be returned to Oxford Academic.
If you do not have a society account or have forgotten your username or password, please contact your society.
Sign in using a personal account
Some societies use Oxford Academic personal accounts to provide access to their members. See below.
Personal account
A personal account can be used to get email alerts, save searches, purchase content, and activate subscriptions.
Some societies use Oxford Academic personal accounts to provide access to their members.
Viewing your signed in accounts
Click the account icon in the top right to:
- View your signed in personal account and access account management features.
- View the institutional accounts that are providing access.
Signed in but can't access content
Oxford Academic is home to a wide variety of products. The institutional subscription may not cover the content that you are trying to access. If you believe you should have access to that content, please contact your librarian.
Institutional account management
For librarians and administrators, your personal account also provides access to institutional account management. Here you will find options to view and activate subscriptions, manage institutional settings and access options, access usage statistics, and more.
Purchase
Short-term Access
To purchase short-term access, please sign in to your personal account above.
Don't already have a personal account? Register
Binding Site of Cerulenin in Fatty Acid Synthetase1 - 24 Hours access
EUR €39.00
GBP £34.00
USD $42.00
Rental
This article is also available for rental through DeepDyve.
Citations
Views
Altmetric
Metrics
Total Views 67
9 Pageviews
58 PDF Downloads
Since 12/1/2016
Month: | Total Views: |
---|---|
December 2016 | 1 |
January 2017 | 2 |
February 2017 | 1 |
July 2017 | 2 |
August 2017 | 2 |
November 2017 | 4 |
March 2018 | 2 |
April 2018 | 2 |
May 2018 | 1 |
July 2018 | 1 |
May 2019 | 2 |
November 2019 | 3 |
January 2020 | 1 |
February 2020 | 1 |
August 2020 | 1 |
January 2021 | 5 |
March 2021 | 1 |
June 2021 | 1 |
September 2021 | 2 |
October 2021 | 1 |
November 2021 | 2 |
December 2021 | 2 |
January 2022 | 1 |
May 2022 | 2 |
July 2022 | 1 |
November 2022 | 2 |
December 2022 | 2 |
March 2023 | 1 |
April 2023 | 1 |
July 2023 | 1 |
August 2023 | 2 |
October 2023 | 2 |
November 2023 | 4 |
December 2023 | 1 |
March 2024 | 1 |
April 2024 | 4 |
May 2024 | 1 |
June 2024 | 1 |
Citations
170 Web of Science
×
Email alerts
Citing articles via
More from Oxford Academic