Enzymes in carbohydrate synthesis. Lipase-catalyzed selective acylation and deacylation of furanose and pyranose derivatives

Hennen, William J.; Sweers, H. M.; Wang, Yi Fong; Wong, Chi Huey

doi:10.1021/jo00256a008

Cited by 192 publications

(51 citation statements)

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“…The required methyl 5-phosphoribofuranoside 2a was prepared from known methyl ribofuranoside [15] (Scheme 4) by phosphitylation of this compound with dibenzyloxydiisopropylaminophosphane, in the presence of tetrazole as a catalyst, and subsequent oxidation with tert-butylhydroperoxide to give the phosphorous triester derivative 5. Hydrogenolytic O-debenzylation followed by triethylamine addition furnished triethylammonium salt 6, which upon ion exchange led to the corresponding phosphorous acid monoester 2a.…”

Section: Eur J Org Chem 2000 1467ϫ1482 1468mentioning

confidence: 99%

Base- and Sugar-Modified Cytidine MonophosphateN-Acetylneuraminic Acid (CMP-Neu5Ac) Analogues - Synthesis and Studies with α(2-6)-Sialyltransferase from Rat Liver

et al. 2000

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The reaction of sialyl phosphites 1, 22a‐d, 28, 39, and 45 with acyl‐protected riboside 5‐phosphorous acids 2a,b and 23 directly furnished, without addition of a catalyst, under phosphite/phosphate exchange the corresponding β‐configured sialyl riboside monophosphates 3a,b, 24a‐d, 29, 46, and 47. The synthesis of the starting materials, formation of the products, and their treatment with sodium methanolate in methanol and subsequent hydrolysis of the sialic acid ester moiety to provide the unprotected target molecules 4a,b, 25a‐d, 30, 48, and 49 is described. Investigations with α(2‐6)‐sialyltransferase from rat liver showed that base replacement in CMP‐Neu5Ac (4a,b) is not tolerated by the enzyme but that modifications of the 5‐, 8‐, or 9‐position of the neuraminic acid residue (25a‐d, 30, 48, 49) are tolerated.

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Section: Eur J Org Chem 2000 1467ϫ1482 1468mentioning

confidence: 99%

Base- and Sugar-Modified Cytidine MonophosphateN-Acetylneuraminic Acid (CMP-Neu5Ac) Analogues - Synthesis and Studies with α(2-6)-Sialyltransferase from Rat Liver

et al. 2000

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“…The purification also proved to be rather difficult as the products and the acetylated hydrazine species showed similar polarities and solubilities. Reaction of 11 with benzylamine, 14 methanolic ammonia and porcine pancreas lipase 15 , respectively did not show any conversion. On the other hand the use of sodium methoxide or potassium carbonate led to an unwanted solvolysis of both acetate moieties in 11 even at 0 °C.…”

Section: Resultsmentioning

confidence: 92%

Preparation of (2R)-2-acetoxy-D-forosamine for the total synthesis of spinosyns

Tietze¹,

Böhnke²,

Brasche³

2006

Arkivoc

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“…The St. lividans AcXE displays a different regioselectivity for deacetylation of methyl glycosides in comparison to lipases used for carbohydrate deacetylation [9][10][11][12][13]. The deacetylation regioselectivity for positions 2 and 3 is complementary to the regioselectivity of most other deacetylating enzymes, which mainly release acetyl groups from position 4 in xylopyranosides [13] and position 6 in hexopyranosides [14].…”

Section: Discussionmentioning

confidence: 99%

Substrate specificity and mode of action of acetylxylan esterase from Streptomyces lividans

et al. 1996

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The substrate specificity of purified acetylxylan esterase (AcXE) from Streptomyces lividans was investigated on partially and fully acetylated methyl glycopyranosides. The enzyme exhibited deacetylation regioselectivity on model compounds which provided insights pertaining to its function in acetyixylan degradation. The enzyme catalyzed double deacetylation of methyl 2,3,4-tri-O-acetyl-l~-l)-xylopyranoside and methyl 2,3,4,6-tetra-O-acetyl-~o-glucopyranoside at positions 2 and 3. Two methyl xylopyranoside diacetates, which had a free hydroxyl group at position 2 or 3, i.e. the derivatives that most closely mimic monoacetylated xylopyranosyl residues in acetylxylan, were deacetylated 1 to 2 orders of magnitude faster than methyl 2,3,4-tri-O-acetyi-~o-xylopyranoside and methyl 2,3-di-O-acetyl-~D-xylopyranoside. These observations explain the double deacetylation. The second acetyl group is released immediately after the first one is removed from the fully acetylated methyl ~o-xylo-and -glucopyranoside. The results suggest that in acetylxylan degradation the enzyme rapidly deacetylates monoacetylated xylopyranosyl residues, but attacks doubly acetylated residues much more slowly. Evidence is also presented that the St. lividans enzyme could be the first real substrate-specific AcXE.

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Enzymes in carbohydrate synthesis. Lipase-catalyzed selective acylation and deacylation of furanose and pyranose derivatives

Cited by 192 publications

References 1 publication

Base- and Sugar-Modified Cytidine MonophosphateN-Acetylneuraminic Acid (CMP-Neu5Ac) Analogues - Synthesis and Studies with α(2-6)-Sialyltransferase from Rat Liver

Base- and Sugar-Modified Cytidine MonophosphateN-Acetylneuraminic Acid (CMP-Neu5Ac) Analogues - Synthesis and Studies with α(2-6)-Sialyltransferase from Rat Liver

Preparation of (2R)-2-acetoxy-D-forosamine for the total synthesis of spinosyns

Substrate specificity and mode of action of acetylxylan esterase from Streptomyces lividans

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