Document Detail

Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis.
MedLine Citation:
PMID:  15839685     Owner:  NLM     Status:  MEDLINE    
The doubly functional aminotransferase BtrS in the 2-deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruption study clearly showed that BtrS is involved, in addition to the previously confirmed first transamination, in the second transamination as well. This dual function of BtrS for the DOS biosynthesis was further confirmed by the structural determination of the reverse reaction product from DOS. Enantiospecific formation of the reverse reaction product from DOS clearly showed that BtrS distinguishes the enantiotopic amino groups of DOS, but in contrast, both enantiomers of 2-deoxy-scyllo-inosose (DOI) were efficiently accepted by BtrS to give a racemic product. This unique stereochemical recognition of DOI chirality and DOS prochirality by BtrS is mechanistically explained by a specific hydrogen-bond donating force in the enzyme active site as a particular feature of this doubly functional enzyme.
Kenichi Yokoyama; Fumitaka Kudo; Mieko Kuwahara; Kousuke Inomata; Hideyuki Tamegai; Tadashi Eguchi; Katsumi Kakinuma
Related Documents :
6441185 - Oxidation of prostacyclin and its analogs by three 15-hydroxyprostaglandin dehydrogenases.
20888835 - Gradual adaptive changes of a protein facing high salt concentrations.
19767425 - Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigatio...
17115705 - A monofunctional and thermostable prephenate dehydratase from the archaeon methanocaldo...
3818665 - Golgi endo-alpha-d-mannosidase from rat liver, a novel n-linked carbohydrate unit proce...
39755 - The kinetics of a purified form of 3-deoxy-d-arabino heptulosonate-7-phosphate synthase...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  127     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-04-20     Completed Date:  2005-07-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5869-74     Citation Subset:  IM    
Department of Chemistry and the Department of Chemistry and Materials Science, Tokyo Institute of Technology, 2-12-1 O-okayama, Meguro-ku, Tokyo 152-8551, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Bacillus / enzymology,  genetics
Binding Sites
Escherichia coli / enzymology,  genetics
Glutamine / metabolism
Hexosamines / biosynthesis*
Hydrogen Bonding
Inositol / analogs & derivatives*,  metabolism
Nuclear Magnetic Resonance, Biomolecular
Recombinant Proteins / biosynthesis,  genetics,  metabolism
Transaminases / genetics,  metabolism*
Reg. No./Substance:
0/Hexosamines; 0/Recombinant Proteins; 2037-48-1/2-deoxystreptamine; 56-85-9/Glutamine; 61914-09-8/2-deoxyinosose; 6917-35-7/Inositol; EC 2.6.1.-/Transaminases

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

Previous Document:  A designed synthetic analogue of 4-OT is specific for a non-natural substrate.
Next Document:  Inclusion of cut and as-grown single-walled carbon nanotubes in the helical superstructure of schizo...