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Acyl Donors (acyl + donor)
Selected AbstractsCyanide-Catalyzed Additions of Acyl Phosphonates to Aldehydes: A New Acyl Donor for Benzoin-Type ReactionsADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 9 2005Abstract Acyl phosphonates have been utilized as new acyl donors for cyanide-catalyzed benzoin-type reactions. Cyanation of acyl phosphonates, followed by a [1,2]-phosphoryl migration generates the active acyl anion intermediate. The presumed (cyano)phosphate anion reacts with a variety of aryl aldehydes to yield phosphate ester-protected, unsymmetrical benzoins in good to excellent yields. The unsymmetrical benzoin product can be obtained after deprotection of the phosphate ester with an aqueous amine solution. [source] Removal of the Acyl Donor Residue Allows the Use of Simple Alkyl Esters as Acyl Donors for the Dynamic Kinetic Resolution of Secondary Alcohols.CHEMINFORM, Issue 38 2005Gerard K. M. Verzijl Abstract For Abstract see ChemInform Abstract in Full Text. [source] Palladium-Catalyzed Carboacylation of Alkenes by Using Acylchromates as Acyl Donors.CHEMINFORM, Issue 24 2005Motoki Yamane No abstract is available for this article. [source] Improved Synthesis and Isolation of 2,- O -Methyladenosine: Effective and Scalable Enzymatic Separation of 2,/3,- O -Methyladenosine RegioisomersEUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 19 2009Saúl Martínez-Montero Abstract An efficient separation of a mixture of 2,/3,- O -methyladenosine regioisomers (1 + 2; 1:1) has been developed by selective enzymatic acylation using immobilized Pseudomonas cepacia lipase (PSL-C) in combination with acetonoxime levulinate as acyl donor. The 3,-hydroxy group of 2,- O -methyladenosine (1) was acylated with high selectivity (ca. 70,%), whereas an equal amount of 3,- O -methyladenosine (2) in the same solution resulted in minor acylation of 5,-hydroxy group (ca. 8,%). The differential behavior of both regioisomers towards enzymatic acylation allowed to develop a separation protocol. Upon extraction of the acylated products, the 3,- O -methyladenosine was isolated in 81,% yield and 97,% purity from the aqueous layer. Hydrolysis of acylated products in organic layer furnished 2,- O -methyladenosine in 67,% yield and 99,% purity. The separation process was successfully applied to the crude reaction mixture of methylated products (ca. 3:1 of 1/2) on 5-g scale. We also report on the use of methyl p -toluenesulfonate as a safe reagent for 2,- O -methylation of adenosine.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009) [source] Kinetic Analysis of L -Carnosine Formation by ,-AminopeptidasesADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 2-3 2010Tobias Heck Abstract The ,,,-dipeptide L -carnosine occurs in high concentrations in long-lived innervated mammalian tissues and is widely sold as a food additive. On a large scale L -carnosine is produced by chemical synthesis procedures. We have established two aqueous enzymatic reaction systems for the preparation of L -carnosine using the dissolved bacterial ,-aminopeptidases DmpA from Ochrobactrum anthropi and BapA from Sphingosinicella xenopeptidilytica as catalysts and investigated the kinetics of the enzyme-catalyzed peptide couplings. DmpA catalyzed the formation of L -carnosine from C-terminally activated ,-alanine derivatives (acyl donor) and L -histidine (acyl acceptor) in an aqueous reaction mixture at pH,10 with high catalytic rates (Vmax=19.2,,mol,min,1 per mg of protein, kcat=12.9,s,1), whereas Vmax in the BapA-catalyzed coupling reaction remained below 1.4,,mol,min,1 per mg of protein (kcat=0.87,s,1). Although the equilibrium of this reaction lies on the side of the hydrolysis products, the reaction is under kinetic control and L -carnosine temporarily accumulated to concentrations that correspond to yields of more than 50% with respect to the employed acyl donor. However, competing nucleophiles caused unwanted hydrolysis and coupling reactions that led to decreased product yield and to formation of various peptidic by-products. The substitution of L -histidine for L -histidine methyl ester as acyl acceptor shifted the pKa of the amino functionality from 9.25 to 6.97, which caused a drastic reduction in the amount of coupling by-products in an aqueous reaction system at pH,8. [source] Combined Chemical-Enzymatic Assembly of Aminoglycoside Derivatives with N-1-AHB Side ChainADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 11-12 2008Igor Nudelman Abstract A series of unprotected pseudo-disaccharides and pseudo-trisaccharides of 2-deoxystreptamine-containing aminoglycosides have been selectively acylated at the N-1 position with the valuable (S)-4-amino-2-hydroxybutanoyl (AHB) pharmacophore by using the recombinant BtrH and BtrG enzymes from butirosin biosynthesis in combination with a synthetic acyl donor. The process was optimized by performing two enzymatic steps in a sequential manner without purification of the intermediate product. [source] Kinetic Resolution of 1-Biaryl- and 1-(Pyridylphenyl)alkan-1-ols Catalysed by the Lipase B from Candida antarcticaADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 5 2005Robert Kourist Abstract Lipase B from Candida antarctica (CAL-B) catalyses the highly enantioselective (E>200) transesterification of some 1-biaryl-2-yl-, -3-yl-, and -4-ylethanols and -propan-1-ols, as well as 1-(o -, m -, and p -pyridylphenyl)ethanols, 6, with vinyl acetate, Kazlauskas' rule being obeyed in all cases. meta and para -Substituted substrates were transformed within several hours (conversion degree ranging from 23,50%), reaction rates for propan-1-ol derivatives being slower than those for ethanol derivatives. Transesterifications of ortho -substituted alcohols took several days and were accompanied by a chemoenzymatic side reaction: the formation of another acetate derived from the hemiacetal between 6 and acetaldehyde coming from vinyl acetate. This side reaction was suppressed in the presence of isopropenyl acetate as acyl donor, conversion degrees for transesterification ranging from 20,40% after ten days (E>200). The usefulness of (R)- 6p as ligand in the asymmetric addition of diethylzinc to benzaldehyde was also demonstrated. [source] Esterification of n -butyric acid with n -butyl alcohol and transesterification of (R,,S)-phenylethanol by lipase immobilized on cellulose acetate,TiO2 gel fibreJOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 1 2002Yuko Ikeda Abstract Lipase (EC 3.1.1.3) was immobilized on cellulose acetate,TiO2 gel fibre by the sol,gel method. The immobilized lipases were used for esterification of n -butyric acid with n -butyl alcohol and enantioselective acylation of (R, S)-phenylethanol using vinyl acetate as an acyl donor. Compared with native lipase, the activity of the immobilized lipase was stable and relatively unaffected by the water content of the solvent and the substrate concentration. The data indicate that the lipases are immobilized on the fibre surface and that enzyme activity is influenced by bound water. However, the thermal reactivity and enantioselectivity of the immobilized lipase were less than those of native lipase. This may not reflect thermal inactivation of the enzyme but rather significant thermal contraction of the gel fibre by cellulose crystallization, resulting in liberation of bound water and a decrease in the amount of enzyme which is available for the reaction. Copyright © 2001 Society of Chemical Industry [source] Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT foldACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 11 2008Matthew W. Vetting Gene rv0802c from Mycobacterium tuberculosis encodes a 218-amino-acid protein and is annotated as a hypothetical protein with homology to GCN5-related N -acetyltransferases. The structure of Rv0802c was determined in an unliganded form to 2.0,Ĺ resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+:citrate2 complex. The structure confirms that Rv0802c exhibits the GCN5-related N -acetyltransferase fold and revealed a tetramer composed of a dimer of dimers with approximate 222 symmetry. In addition, a bound acetate ion indicated that Rv0802c may utilize a unique acyl donor for the family. The subsequent determination of the structure of Rv0802c in complex with succinyl-CoA to 2.3,Ĺ resolution suggests that Rv0802c is the first known GCN5-related N -acetyltransferase family member to utilize succinyl-CoA as a substrate. [source] An Inverse Substrate Orientation for the Regioselective Acylation of 3,,5,-Diaminonucleosides Catalyzed by Candida antarctica lipase B?CHEMBIOCHEM, Issue 8 2005Iván Lavandera Dr. Abstract Candida antarctica lipase B (CAL-B) catalyzes the regioselective acylation of natural thymidine with oxime esters and also the regioselective acylation of an analogue, 3,,5,-diamino-3,,5,-dideoxythymidine with nonactivated esters. In both cases, acylation favors the less hindered 5,-position over the 3,-position by upto 80-fold. Computer modeling of phosphonate transition-state analogues for the acylation of thymidine suggests that CAL-B favors acylation of the 5,-position because this orientation allows the thymine ring to bind in a hydrophobic pocket and forms stronger key hydrogen bonds than acylation of the 3,-position. On the other hand, computer modeling of phosphonamidate analogues of the transition states for acylation of either the 3,- or 5,-amino groups in 3,,5,-diamino-3,,5,-dideoxythymidine shows similar orientations and hydrogen bonds and, thus, does not explain the high regioselectivity. However, computer modeling of inverse structures, in which the acyl chain binds in the nucleophile pocket and vice versa, does rationalize the observed regioselectivity. The inverse structures fit the 5,-, but not the 3,-intermediate thymine ring, into the hydrophobic pocket, and form a weak new hydrogen bond between the O-2 carbonyl atom of the thymine and the nucleophile amine only for the 5,-intermediate. A water molecule might transfer a proton from the ammonium group to the active-site histidine. As a test of this inverse orientation, we compared the acylation of thymidine and 3,,5,-diamino-3,,5,-dideoxythymidine with butyryl acyl donors and with isosteric methoxyacetyl acyl donors. Both acyl donors reacted at equal rates with thymidine, but the methoxyacetyl acyl donor reacted four times faster than the butyryl acyl donor with 3,,5,-diamino-3,,5,-dideoxythymidine. This faster rate is consistent with an inverse orientation for 3,,5,-diamino-3,,5,-dideoxythymidine, in which the ether oxygen atom of the methoxyacetyl group can form a similar hydrogen bond to the nucleophilic amine. This combination of modeling and experiments suggests that such lipase-catalyzed reactions of apparently close substrate analogues like alcohols and amines might follow different pathways. [source] Chemoenzymatic synthesis and properties of Schiff bases containing (R)-1-(9-anthryl)ethylamineCHIRALITY, Issue 8 2002Marin Roje Abstract Racemic 1-(9-anthryl)ethylamine (10), obtained in 70% overall yield from commercial 9-cyanoanthracene, was kinetically resolved by the Candida antarctica A lipase-catalyzed acetylation with isopropyl acetate as acyl donor, affording (R)-(+)- 10 with 95.8% enantiomeric excess (e.e.) (E- value 43.5), which afforded Schiff bases (R)- 4 and(R)- 8.1H-NMR, CD, and MM2 calculations offer a consistent picture of the conformational properties of these potential ligands and an explanation for the limited enhancement of enantioselectivity in cyclopropanation of styrene by their Cu(I) complexes, as compared with previously studied ligands in this series. Chirality 14:625,631, 2002. © 2002 Wiley-Liss, Inc. [source] Phylogenetic analysis of condensation domains in the nonribosomal peptide synthetasesFEMS MICROBIOLOGY LETTERS, Issue 1 2005Niran Roongsawang Abstract Condensation (C) domains in the nonribosomal peptide synthetases are capable of catalyzing peptide bond formation between two consecutively bound various amino acids. C-domains coincide in frequency with the number of peptide bonds in the product peptide. In this study, a phylogenetic approach was used to investigate structural diversity of bacterial C-domains. Phylogenetic trees show that the C-domains are clustered into three functional groups according to the types of substrate donor molecules. They are l -peptidyl donors, d -peptidyl donors, and N -acyl donors. The fact that C-domain structure is not subject to optical configuration of amino acid acceptor molecules supports an idea that the conversion from l to d -form of incorporating amino acid acceptor occurs during or after peptide bond formation. l -peptidyl donors and d -peptidyl donors are suggested to separate before separating the lineage of Gram-positive and Gram-negative bacteria in the evolution process. [source] Cyanide-Catalyzed Additions of Acyl Phosphonates to Aldehydes: A New Acyl Donor for Benzoin-Type ReactionsADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 9 2005Abstract Acyl phosphonates have been utilized as new acyl donors for cyanide-catalyzed benzoin-type reactions. Cyanation of acyl phosphonates, followed by a [1,2]-phosphoryl migration generates the active acyl anion intermediate. The presumed (cyano)phosphate anion reacts with a variety of aryl aldehydes to yield phosphate ester-protected, unsymmetrical benzoins in good to excellent yields. The unsymmetrical benzoin product can be obtained after deprotection of the phosphate ester with an aqueous amine solution. [source] The ,-lactam-sensitive d,d -carboxypeptidase activity of Pbp4 controls the l,d and d,d transpeptidation pathways in Corynebacterium jeikeiumMOLECULAR MICROBIOLOGY, Issue 3 2009Marie Lavollay Summary Corynebacterium jeikeium is an emerging nosocomial pathogen responsible for vascular catheters infections, prosthetic endocarditis and septicemia. The treatment of C. jeikeium infections is complicated by the multiresistance of clinical isolates to antibiotics, in particular to ,-lactams, the most broadly used class of antibiotics. To gain insight into the mechanism of ,-lactam resistance, we have determined the structure of the peptidoglycan and shown that C. jeikeium has the dual capacity to catalyse formation of cross-links generated by transpeptidases of the d,d and l,d specificities. Two ampicillin-insensitive cross-linking enzymes were identified, LdtCjk1, a member of the active site cysteine l,d -transpeptidase family, and Pbp2c, a low-affinity class B penicillin-binding protein (PBP). In the absence of ,-lactam, the PBPs and the l,d -transpeptidase contributed to the formation of 62% and 38% of the cross-links respectively. Although LdtCjk1 and Pbp2C were not inhibited by ampicillin, the participation of the l,d -transpeptidase to peptidoglycan cross-linking decreased in the presence of the drug. The specificity of LdtCjk1 for acyl donors containing a tetrapeptide stem accounts for this effect of ampicillin since the essential substrate of LdtCjk1 was produced by an ampicillin-sensitive d,d -carboxypeptidase (Pbp4Cjk). Acquisition and mutational alterations of pbp2C accounted for high-level ,-lactam resistance in C. jeikeium. [source] Overexpression of the apple alcohol acyltransferase gene alters the profile of volatile blends in transgenic tobacco leavesPHYSIOLOGIA PLANTARUM, Issue 3 2008Dapeng Li Alcohol acyltransferases (AATs) are key enzymes in ester biosynthesis. Previous studies have found that AAT may be a stress-related gene. To investigate further the function of the apple alcohol acyltransferase gene (MdAAT2), transgenic tobacco plants overexpressing MdAAT2 were generated. Gas chromatography,mass spectroscopy analysis showed that the volatile blends were altered in these transgenic tobacco leaves. Although no apple-fruity volatile esters were detected in transgenic tobacco leaves, methyl caprylate, methyl caprate, and methyl dodecanoate were newly generated, and the concentrations of methyl benzoate and methyl tetradecanoate were significantly increased, suggesting that MdAAT2 may use medium-chain fatty acyl CoA and benzoyl-CoA as acyl donors together with methanol acceptors as substrates. Surprisingly, the concentrations of linalool were significantly increased in transgenic tobacco leaves, which may mediate the repellent effect on Myzus persicae (Sulzer) aphids. Using methyl jasmonate (MeJA) and wounding treatments, we found that MdAAT2 may substitute for the partial ability of MeJA to induce the production of linalool in transgenic plants. These data suggest that MdAAT2 may be involved in the response to the MeJA signal and may play a role in the response to biotic and abiotic stress. [source] Recognition of acyl donors by lipase CAL-B in the acylation of 6-azauridineBIOTECHNOLOGY PROGRESS, Issue 3 2009Zhao-Yu Wang Abstract CAL-B-catalyzed synthesis of different 5,-O-monoester derivatives of 6-azauridine via a one-step highly regioselective enzymatic acylation route was successfully performed for the first time. The effects of some crucial factors on the enzymatic undec-10-enoylation of 6-azauridine were examined. The optimal reaction medium, molar ratio of 6-azauridine to vinyl undec-10-enoate and reaction temperature were found to be anhydrous acetone, 1:3 and 50°C, under which the reaction rate, the substrate conversion and the regioselectivity were 22.3 mM/h, 99.0% and 99.0%, respectively. In addition, the enzyme recognition of acyl donors was investigated. The results showed that the enzyme activity varied widely with different acyl donors owing to the specific structure of the lipase active site and the acyl donors. 5,-O-Monoesters of 6-azauridine were achieved exclusively with all the acyl donors tested. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009 [source] An Inverse Substrate Orientation for the Regioselective Acylation of 3,,5,-Diaminonucleosides Catalyzed by Candida antarctica lipase B?CHEMBIOCHEM, Issue 8 2005Iván Lavandera Dr. Abstract Candida antarctica lipase B (CAL-B) catalyzes the regioselective acylation of natural thymidine with oxime esters and also the regioselective acylation of an analogue, 3,,5,-diamino-3,,5,-dideoxythymidine with nonactivated esters. In both cases, acylation favors the less hindered 5,-position over the 3,-position by upto 80-fold. Computer modeling of phosphonate transition-state analogues for the acylation of thymidine suggests that CAL-B favors acylation of the 5,-position because this orientation allows the thymine ring to bind in a hydrophobic pocket and forms stronger key hydrogen bonds than acylation of the 3,-position. On the other hand, computer modeling of phosphonamidate analogues of the transition states for acylation of either the 3,- or 5,-amino groups in 3,,5,-diamino-3,,5,-dideoxythymidine shows similar orientations and hydrogen bonds and, thus, does not explain the high regioselectivity. However, computer modeling of inverse structures, in which the acyl chain binds in the nucleophile pocket and vice versa, does rationalize the observed regioselectivity. The inverse structures fit the 5,-, but not the 3,-intermediate thymine ring, into the hydrophobic pocket, and form a weak new hydrogen bond between the O-2 carbonyl atom of the thymine and the nucleophile amine only for the 5,-intermediate. A water molecule might transfer a proton from the ammonium group to the active-site histidine. As a test of this inverse orientation, we compared the acylation of thymidine and 3,,5,-diamino-3,,5,-dideoxythymidine with butyryl acyl donors and with isosteric methoxyacetyl acyl donors. Both acyl donors reacted at equal rates with thymidine, but the methoxyacetyl acyl donor reacted four times faster than the butyryl acyl donor with 3,,5,-diamino-3,,5,-dideoxythymidine. This faster rate is consistent with an inverse orientation for 3,,5,-diamino-3,,5,-dideoxythymidine, in which the ether oxygen atom of the methoxyacetyl group can form a similar hydrogen bond to the nucleophilic amine. This combination of modeling and experiments suggests that such lipase-catalyzed reactions of apparently close substrate analogues like alcohols and amines might follow different pathways. [source] Solid-Phase Synthesis of Peptide and Glycopeptide Thioesters through Side-Chain-Anchoring StrategiesCHEMISTRY - A EUROPEAN JOURNAL, Issue 12 2008Simon Ficht Dr. Abstract An efficient new strategy for the synthesis of peptide and glycopeptide thioesters is described. The method relies on the side-chain immobilization of a variety of Fmoc-amino acids, protected at their C-termini, on solid supports. Once anchored, peptides were constructed using solid-phase peptide synthesis according to the Fmoc protocol. After unmasking the C-terminal carboxylate, either thiols or amino acid thioesters were coupled to afford, after cleavage, peptide and glycopeptide thioesters in high yields. Using this method a significant proportion of the proteinogenic amino acids could be incorporated as C-terminal amino acid residues, therefore providing access to a large number of potential targets that can serve as acyl donors in subsequent ligation reactions. The utility of this methodology was exemplified in the synthesis of a 28 amino acid glycopeptide thioester, which was further elaborated to an N-terminal fragment of the glycoprotein erythropoietin (EPO) by native chemical ligation. [source] | |||||||||||||