English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Absolute stereochemistry of flavins in enzyme-catalyzed reactions

Manstein, D. J., Pai, E. F., Schopfer, L. M., & Massey, V. (1986). Absolute stereochemistry of flavins in enzyme-catalyzed reactions. Biochemistry, 25(22), 6807-6816. doi:10.1021/bi00370a012.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
Biochem_25_1986_6807.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
Biochem_25_1986_6807.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Locator:
https://doi.org/10.1021/bi00370a012 (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Manstein, Dietmar J.1, 2, Author              
Pai, Emil F.2, Author              
Schopfer, Lawrence M., Author
Massey, Vincent, Author
Affiliations:
1Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: The 8-demethyl-8-hydroxy-5-deaza-5-carba analogues of FMN and FAD have been synthesized. Several apoproteins of flavoenzymes were successfully reconstituted with these analogues. This and further tests established that these analogues could serve as general probes for flavin stereospecificity in enzyme-catalyzed reactions. The method used by us involved stereoselective introduction of label on one enzyme combined with transfer to and analysis on a second enzyme. Using as a reference glutathione reductase from human erythrocytes for which the absolute stereochemistry of catalysis is known from X-ray studies [Pai, E. F., & Schulz, G. E. (1983) J. Biol. Chem. 258, 1752-1758], we were able to determine the absolute stereospecificities of other flavoenzymes. We found that glutathione reductase (NADPH), general acyl-CoA dehydrogenase (acyl-CoA), mercuric reductase (NADPH), thioredoxin reductase (NADPH), p-hydroxybenzoate hydroxylase (NADPH), melilotate hydroxylase (NADH), anthranilate hydroxylase (NADPH), and glucose oxidase (glucose) all use the re face of the flavin ring when interacting with the substrates given in parentheses.

Details

show
hide
Language(s): eng - English
 Dates: 1986-04-281986-07-101986-11-04
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 25 (22) Sequence Number: - Start / End Page: 6807 - 6816 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103