Enzymatic synthesis of carnosine derivatives catalysed by Burkholderia cepacia lipase

D’Arrigo, Paola; Kanerva, Liisa T.; Li, Xiangguo; Saraceno, Caterina; Servi, Stefano De; Tessaro, Davide

doi:10.1016/j.tetasy.2009.05.040

Cited by 14 publications

(4 citation statements)

References 22 publications

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“…For these reasons, the interest in the synthesis of carnosine derivatives with therapeutic properties but with greater biological stability has increased (Cacciatore et al, ). D'Arrigo et al () studied the synthesis of analogs of carnosine by forming a peptide bond between a β‐lactam and an alpha‐amino protected acid. The reaction was catalyzed by Lipase PS‐D (Figure b).…”

Section: Synthesis Of Drugsmentioning

confidence: 99%

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Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Sánchez

Tonetto

Ferreira

2017

Biotech & Bioengineering

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The lipase from Burkholderia cepacia, formerly known as Pseudomonas cepacia lipase, is a commercial enzyme in both soluble and immobilized forms widely recognized for its thermal resistance and tolerance to a large number of solvents and short-chain alcohols. The main applications of this lipase are in transesterification reactions and in the synthesis of drugs (because of the properties mentioned above). This review intends to show the features of this enzyme and some of the most relevant aspects of its use in different synthesis reactions. Also, different immobilization techniques together with the effect of various compounds on lipase activity are presented. This lipase shows important advantages over other lipases, especially in reaction media including solvents or reactions involving short-chain alcohols.

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Section: Synthesis Of Drugsmentioning

confidence: 99%

“…a) Structure of the dipeptide carnosine. b) Mechanism of lipase‐catalysed dipeptide formation (D'Arrigo et al, )…”

Section: Synthesis Of Drugsmentioning

confidence: 99%

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Sánchez

Tonetto

Ferreira

2017

Biotech & Bioengineering

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“…1 H NMR (400 MHz, CDCl 3 ) δ: 7.28-7.16 (m, 5H), 5.1 (s, 2H), 3.44-3.4 (t, J = 5.3, 2H), 2.85-2.81(t, J = 5.3, 2H). 13 34 (5). 2-Azetidinone (72 mg, 1 mmol) and DMAP (12.2 mg, 0.1 mmol) were dissolved in acetonitrile (5 mL) at 0 °C.…”

Section: Synthesis 1-[(4-methylphenylmentioning

confidence: 99%

N-Activated β-lactams as versatile reagents for acyl carrier protein labeling

et al. 2012

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Acyl carrier proteins are critical components of fatty acid and polyketide biosynthesis. Their primary function is to shuttle intermediates between active sites via a covalently bound phosphopantetheine arm. Small molecules capable of acylating this prosthetic group will provide a simple and reversible means of introducing novel functionality onto carrier protein domains. A series of N-activated β-lactams are prepared to examine site-specific acylation of the phosphopantetheine-thiol. In general, β-lactams are found to be significantly more reactive than our previously studied β-lactones. Selectivity for the holo over apo-form of acyl carrier proteins is demonstrated indicating that only the phosphopantetheine-thiol is modified. Incorporation of an N-propargyloxycarbonyl group provides an alkyne handle for conjugation to fluorophores and affinity labels. The utility of these groups for mechanistic interrogation of a critical step in polyketide biosynthesis is examined through comparison to traditional probes. In all, we expect the probes described in this study to serve as valuable and versatile tools for mechanistic interrogation of fatty acid, polyketide, and nonribosomal peptide biosynthesis.

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“…Lipases accept a wide range of substrates in the different types of reactions they catalyse (e.g., hydrolysis, alcoholysis, aminolysis, interesterification and Michael addition),1,3 and they also show a high stability and diversity. They have also been used as cheap regio‐ and enantioselective ring‐opening catalysts of β‐lactams in the preparation of β‐amino acids1 and their esters4a and amides, which could then be used, for example, in the synthesis of β‐dipeptides 4b,4c. Instances of the catalytic cleavage of amides by lipases are rare, and are mostly restricted to Candida antarctica lipases; a number of serine proteases readily fulfil this function 5.…”

Section: Introductionmentioning

confidence: 99%

Regio‐ and Stereoselective Lipase‐Catalysed Acylation of Methyl α‐D‐Glycopyranosides with Fluorinated β‐Lactams

2014

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Burkholderia cepacia lipase (lipase PS‐D) catalysed acylation with 3,3‐difluoro‐4‐phenyl‐, ‐thiophen‐3‐yl‐ and ‐4‐pyridylazetidin‐2‐ones was examined for the formation of N‐Boc‐protected 6‐O‐acylated sugar–β‐amino acid conjugates from methyl α‐D‐galacto‐, ‐gluco‐ and mannopyranosides and Boc2O. The 6‐O‐acylated glycopyranoside–β‐amino acid conjugates were isolated and characterized. The low solubility of the gluco‐ and mannopyranosides and the high reactivity of the pyridylazetidinone restricted product formation. Activation of the β‐lactam ring by the presence of fluorine substituents was shown to be necessary for the enzymatic acylation reaction. The (S)‐enantiomers of the racemic β‐lactam substrates reacted with the sugars.

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Enzymatic synthesis of carnosine derivatives catalysed by Burkholderia cepacia lipase

Cited by 14 publications

References 22 publications

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

N-Activated β-lactams as versatile reagents for acyl carrier protein labeling

Regio‐ and Stereoselective Lipase‐Catalysed Acylation of Methyl α‐D‐Glycopyranosides with Fluorinated β‐Lactams

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