Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ohnuma, S.-i.
Right arrow Articles by Nishino, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohnuma, S.-i.
Right arrow Articles by Nishino, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1998, Vol. 123, No. 6 1036-1040
© 1998 Japanese Biochemical Society

research-article

Recognition of Allylic Substrates in Sulfolobus acidocaldarius Geranylgeranyl Diphosphate Synthase: Analysis Using Mutated Enzymes and Artificial Allylic Substrates1

Shin-ichi Ohnuma*,2,3, Hisashi Hemmi*, Tanetoshi Koyama{dagger}, Kyozo Ogura{dagger} and Tokuzo Nishino*,2

*Department of Biochemistry and Engineering, Tohoku University Aoba Aramaki 07, Aoba-ku, Sendai 980-8579
{dagger}Institute for Chemical Reaction Science, Tohoku University Sendai 980-8577

2To whom correspondence should be addressed.

We examined the substrate specificity of two mutated geranylgeranyl diphosphate synthases, I-9 and I-11, with respect to several artificial substrates. These mutated enzymes have replacements in the amino acid sequences from positions 170 to 173, which are thought to be a part of the putative substrate binding region. The wild-type enzyme catalyzes the condensation of IPP with a series of (2E)-3-methyl-2-alkenyl diphosphates to give products with carbon numbers between 14 and 21. On the other hand, the mutated enzymes show lower activities for artificial substrates with short alkyl chains than those of the wild-type enzyme though the carbon numbers of the products are similar to those in the case of the wild-type. The mutated enzyme I-11 never accepts artificial substrates shorter than C8. Analysis of additional mutated enzymes revealed that the characteristics of the mutated enzymes arise from a few substitutions within positions 171 to 173. These results indicate that the amino acids in the positions 171 to 173 of the geranylgeranyl diphosphate synthase from Sulfolobus acidocaldarius are involved in recognition of short allylic substrates, such as dimethylallyl diphosphate, but not in recognition of the chain length of the products.

1This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan.

3Present address: Department of Anatomy, University of Cambridge, Downing Street, Cambridge CB2 3DY, England.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Microbiol. Mol. Biol. Rev.Home page
D. Umeno, A. V. Tobias, and F. H. Arnold
Diversifying Carotenoid Biosynthetic Pathways by Directed Evolution
Microbiol. Mol. Biol. Rev., March 1, 2005; 69(1): 51 - 78.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
D. Umeno, A. V. Tobias, and F. H. Arnold
Evolution of the C30 Carotenoid Synthase CrtM for Function in a C40 Pathway
J. Bacteriol., December 1, 2002; 184(23): 6690 - 6699.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.