Document Detail

Channeling of ammonia in glucosamine-6-phosphate synthase.
MedLine Citation:
PMID:  11700065     Owner:  NLM     Status:  MEDLINE    
Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.
A Teplyakov; G Obmolova; B Badet; M A Badet-Denisot
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular biology     Volume:  313     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-08     Completed Date:  2001-12-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1093-102     Citation Subset:  IM    
Copyright Information:
Copyright 2001 Academic Press.
European Molecular Biology Laboratory, Notkestr. 85, D-22603 Hamburg, Germany.
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MeSH Terms
Ammonia / metabolism*
Binding Sites
Crystallography, X-Ray
Escherichia coli / enzymology*
Glutaminase / chemistry,  metabolism
Glutamine / metabolism
Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / chemistry*,  metabolism*
Isomerases / chemistry,  metabolism
Models, Molecular
Multienzyme Complexes / chemistry,  metabolism
Nitrogen / metabolism
Protein Structure, Quaternary
Protein Structure, Tertiary
Structure-Activity Relationship
Reg. No./Substance:
0/Multienzyme Complexes; 0/Solvents; 56-85-9/Glutamine; 7664-41-7/Ammonia; 7727-37-9/Nitrogen; EC Transaminase (Isomerizing); EC; EC 5.-/Isomerases

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