Synthesis and conformational analysis of the repeating units of bacterial spore peptidoglycan

Keglević, Dina; Kojić‐Prodić, Biserka; Tomišić, Zrinka Banić

doi:10.1016/s0008-6215(03)00067-3

Cited by 4 publications

(2 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although total synthesis of a peptidoglycan dimer (GlcNAc–MurNAc) has recently been described [31], the pure tetramer, which PdaA requires for activity [8,12], is not available in the quantities and purity required for crystallographic and enzymological studies. We have tried to approach a PdaA–substrate complex by soaking studies with short chitooligosaccharides and the monomers GlcNAc, GlcN, MurNAc and Mur.…”

Section: Resultsmentioning

confidence: 99%

Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N‐acetyl‐glucosamine

Blair

Aalten

2004

FEBS Letters

View full text Add to dashboard Cite

Family 4 carbohydrate esterases deacetylate polymeric carbohydrate substrates such as chitin, acetyl xylan and peptidoglycan. Although some of these enzymes have recently been enzymologically characterised, neither their structure nor their reaction mechanism has been defined. Sequence conservation in this family has pointed to a conserved core, termed the NodB homology domain. We describe the cloning, purification and 1.9 A crystal structure of PdaA, a peptidoglycan deacetylase from Bacillus subtilis. The enzyme assumes a fold related to a ðb=aÞ 8 barrel, with a long groove on the surface of the protein that harbours all conserved residues. A complex with the substrate analogue N-acetyl-glucosamine was refined to 2.25 A resolution, revealing interactions of an aspartic acid and three histidines, all conserved in the NodB homology domain, with the ligand. The PdaA structure provides a template for interpreting the wealth of sequence data on family 4 carbohydrate esterases in a structural context and represents a first step towards understanding the reaction mechanism of this family of enzymes.

show abstract

Section: Resultsmentioning

confidence: 99%

Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N‐acetyl‐glucosamine

Blair

Aalten

2004

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…Selected examples of N ‐Phth‐protected glucosamine donors and glycosylations using various acceptor moieties are shown in Table 2. Glycosylations using N ‐Phth trichloroacetimidates are usually carried out in dichloromethane and can be promoted by catalytic amounts of trimethylsilyl trifluoromethanesulfonate (TMSOTf)14, 16, 17, 18 or AgOTf20 (Table 2, entries 1–3) as well as BF 3 ⋅OEt 2 14b. N ‐Phth thioglycoside donors like STol,15 SPh,21 SEt,22 S i Pr,23 and S‐benzoxazolyl (S‐Box)3 can be activated by NIS/TfOH,22, 24 NIS/TESOTf,21 or AgOTf in the presence of PTSCl ( p ‐toluenesulfonyl chloride) (Table 2, entry 4),15a NIS/TMSOTf (Table 2, entries 5 and 6),15b, 23 BSP/Tf 2 O/DTBMP (Table 2, entry 7), [25] or MeOTf 3.…”

Section: The N‐phthaloyl Groupmentioning

confidence: 99%

Stereoselective Glycosylation of Glucosamine: The Role of the N‐Protecting Group

Enugala

Carvalho

Pires

et al. 2012

Chemistry An Asian Journal

View full text Add to dashboard Cite

Oligosaccharides and glycoconjugates play an important role in biological processes. The use of these complex polymers as biocompatible materials for medicinal applications as well as therapeutic agents for the treatment of several diseases has attracted considerable interest. However, these investigations require large and pure amounts of glycostructures. Glucosamine is one of the major building blocks of these highly important glycoconjugates. Recently, considerable synthetic efforts have been devoted to improving stereoselective glycosylation. In this Focus review, the role of the amine protecting group in the outcome of the glucosamine glycosylation reaction is highlighted.

show abstract

Combining Computational Chemistry and Crystallography for a Better Understanding of the Structure of Cellulose

French

2012

Advances in Carbohydrate Chemistry and Biochemistry

View full text Add to dashboard Cite

Synthesis and conformational analysis of the repeating units of bacterial spore peptidoglycan

Cited by 4 publications

References 20 publications

Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N‐acetyl‐glucosamine

Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N‐acetyl‐glucosamine

Stereoselective Glycosylation of Glucosamine: The Role of the N‐Protecting Group

Combining Computational Chemistry and Crystallography for a Better Understanding of the Structure of Cellulose

Contact Info

Product

Resources

About