Document Detail

Molecular analysis of cis-prenyl chain elongating enzymes.
MedLine Citation:
PMID:  12636086     Owner:  NLM     Status:  MEDLINE    
Recent isolation of the gene for an undecaprenyl diphosphate synthase has disclosed the structures of many kinds of cis-prenyl chain elongating enzymes. Not only the primary structure but also the crystal structure of the cis-prenyltransferase is totally different from those of trans-prenyl chain elongating enzymes. This review covers up to February 2002 and contains 72 references.
Yugesh Kharel; Tanetoshi Koyama
Related Documents :
9634796 - Transgenic canola and soybean seeds with increased lysine.
17697396 - Type i and type ii fatty acid biosynthesis in eimeria tenella: enoyl reductase activity...
17971446 - A heat shock protein 90 binding domain in endothelial nitric-oxide synthase influences ...
18389076 - Influence of c-peptide on glucose utilisation.
20349926 - Surface investigation on biomimetic materials to control cell adhesion: the case of rgd...
11504566 - The fission yeast cop9/signalosome is involved in cullin modification by ubiquitin-rela...
Publication Detail:
Type:  Comparative Study; Journal Article; Review    
Journal Detail:
Title:  Natural product reports     Volume:  20     ISSN:  0265-0568     ISO Abbreviation:  Nat Prod Rep     Publication Date:  2003 Feb 
Date Detail:
Created Date:  2003-03-14     Completed Date:  2003-07-08     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8502408     Medline TA:  Nat Prod Rep     Country:  England    
Other Details:
Languages:  eng     Pagination:  111-8     Citation Subset:  IM    
Institute Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Alkyl and Aryl Transferases* / chemistry,  genetics,  metabolism
Amino Acid Sequence
Biological Factors / chemistry,  metabolism
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Protein Conformation
Sequence Homology, Amino Acid
Transferases* / analysis,  chemistry,  genetics,  metabolism
Reg. No./Substance:
0/Biological Factors; EC 2.-/Transferases; EC 2.5.-/Alkyl and Aryl Transferases; EC 2.5.1.-/cis-prenyl transferase; EC pyrophosphate synthetase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  The chalcone synthase superfamily of type III polyketide synthases.
Next Document:  The biosynthesis of shikimate metabolites.