Document Detail

Biosynthesis of UDP-glucuronic acid and UDP-galacturonic acid in Bacillus cereus subsp. cytotoxis NVH 391-98.
MedLine Citation:
PMID:  22023070     Owner:  NLM     Status:  MEDLINE    
The food borne pathogen Bacillus cereus produces uronic acid-containing glycans that are secreted in a shielding biofilm environment, and certain alkaliphilic Bacillus deposit uronate-glycan polymers in the cell wall when adapting to alkaline environments. The source of these acidic sugars is unknown and, in the present study, we describe the functional identification of an operon in Bacillus cerues subsp. cytotoxis NVH 391-98 that comprises genes involved in the synthesis of UDP-uronic acids in Bacillus spp. Within the operon, a UDP-glucose 6-dehydrogenase converts UDP-glucose in the presence of NAD(+) to UDP-glucuronic acid and NADH, and a UDP-GlcA 4-epimerase (UGlcAE) converts UDP-glucuronic acid to UDP-galacturonic acid. Interestingly, in vitro, both enzymes can utilize the TDP-sugar forms as well, albeit at lower catalytic efficiency. Unlike most of the very few bacterial 4-epimerases that have been characterized, which are promiscuous, the B. cereus UGlcAE enzyme is very specific and cannot use UDP-glucose, UDP-N-acetylglucosamine, UDP-N-acetylglucosaminuronic acid or UDP-xylose as substrates. Size exclusion chromatography suggests that UGlcAE is active as a monomer, unlike the dimeric form of plant enzymes; the Bacillus UDP-glucose 6-dehydrogenase is also found as a monomer. Phylogenic analysis further suggests that the Bacillus UGlcAE may have evolved separately from other bacterial and plant epimerases. Our results provide insight into the formation and function of uronic acid-containing glycans in the lifecycle of B. cereus and related species containing homologous operons, as well as a basis for determining the importance of these acidic glycans. We also discuss the ability to target UGlcAE as a drug candidate.
Bryan Broach; Xiaogang Gu; Maor Bar-Peled
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-11-11
Journal Detail:
Title:  The FEBS journal     Volume:  279     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2011-12-15     Completed Date:  2012-01-31     Revised Date:  2014-09-08    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  100-12     Citation Subset:  IM    
Copyright Information:
© 2011 The Authors Journal compilation © 2011 FEBS.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/HM581979;  HM581980
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MeSH Terms
Bacillus cereus / genetics,  metabolism*
Carbohydrate Epimerases / genetics*,  metabolism*
Cell Wall / metabolism
Chromatography, High Pressure Liquid
Cloning, Molecular
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Operon / genetics*
Recombinant Proteins / genetics,  isolation & purification,  metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substrate Specificity
Uridine Diphosphate Glucuronic Acid / metabolism*
Uridine Diphosphate Sugars / metabolism*
Grant Support
Reg. No./Substance:
0/Recombinant Proteins; 0/Uridine Diphosphate Sugars; 2616-64-0/Uridine Diphosphate Glucuronic Acid; 50722-58-2/UDP-galacturonic acid; EC 5.1.3.-/Carbohydrate Epimerases

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

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