A Stereoselective Inverting <i>sec</i>-Alkylsulfatase for the Deracemization of <i>sec</i>-Alcohols

Schöber, Markus; Gadler, Petra; Knaus, Tanja; Kayer, Heidemarie; Birner-Grünberger, Ruth; Gülly, Christian; Macheroux, Peter; Wagner, Ulrike; Faber, Kurt

doi:10.1021/ol201635y

Cited by 34 publications

(70 citation statements)

References 24 publications

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“…The latter can be chemically hydrolyzed to (S)-secondary alcohols, so that a single (S)-configurated product with up to >99% e.e. results (Figure 6) (65).…”

Section: Novel Biocatalysts Through Finding New Reactionsmentioning

confidence: 89%

See 1 more Smart Citation

Biocatalysis: A Status Report

Bommarius

2015

Annu. Rev. Chem. Biomol. Eng.

136

101

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This review describes the status of the fields of biocatalysts and enzymes, as well as existing drawbacks, and recent advances in the areas deemed to represent drawbacks. Although biocatalysts are often highly active and extremely selective, there are still drawbacks associated with biocatalysis as a generally applicable technique: the lack of designability of biocatalysts; their limits of stability; and the insufficient number of well-characterized, ready-to-use biocatalysts. There has been significant progress on the following fronts: (a) novel protein engineering tools, both experimental and computational, have significantly enhanced the toolbox for biocatalyst development. (b) The deactivation of biocatalysts under various stresses can be described quantitatively via rational models. There are several cases of spectacular leaps of stabilization after accumulating all stabilizing mutations found in earlier rounds. The concept that stabilization against one type of stress commonly also stabilizes against other types of stress is now experimentally considerably better founded than a few years ago.

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“…The latter can be chemically hydrolyzed to (S)-secondary alcohols, so that a single (S)-configurated product with up to >99% e.e. results (Figure 6) (65).…”

Section: Novel Biocatalysts Through Finding New Reactionsmentioning

confidence: 89%

“…Recently, employing a mixture of inverting and retaining stereocomplementary sulfatases acting Enantiocomplementary synthesis of (S)-secondary alcohols. Reproduced from Schober et al (65), copyright 2011 ACS.…”

Section: Novel Biocatalysts Through Finding New Reactionsmentioning

confidence: 99%

Biocatalysis: A Status Report

Bommarius

2015

Annu. Rev. Chem. Biomol. Eng.

136

101

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“…The latter can be then transformed into the (S)-alcohols by chemical deprotection under acidic conditions. [125] In a later study, the same authors investigated the scope of this enzyme finding that it showed good stereoselectivity in the hydrolysis of a variety of sulfate esters such as aromatic, olefinic and acetylenic sulfates, especially when bearing two groups of different size. Moreover, the addition of DMSO (20% v/v) proved to be very convenient in order to obtain better enantioselectivities.…”

Section: Scheme 21mentioning

confidence: 99%

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Díaz‐Rodríguez¹,

Lavandera

Gotor³

2015

CGC

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Abstract. In recent years the usefulness of enzymatic systems to obtain a single stereoisomerically pure compound starting from a racemate has been expanded. Moreover, current advances in protein engineering, molecular biology and modeling tools are the basis to improve the catalytic properties of enzymes to face novel synthetic challenges. Also, medium engineering and novel immobilization methods of (bio)catalysts are enhancing the productivity of biocatalytic processes making them suitable for being scalable. The development of multienzymatic protocols and the combination of enzymes with other catalysts are providing a wide range of synthetic possibilities that are expanding the scope of these transformations even at industrial scale. Herein we will describe an overview of recent (chemo)enzymatic deracemizations, focusing on the strategy employed (dynamic kinetic resolution, stereoinversion, cyclic deracemization or enantioconvergent process), the type of substrate (e.g., alcohols, amines, carboxylic acid derivatives or carbonylic compounds), and the biocatalyst(s) used.

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“…While SdsA1 is more reactive towards primary alkyl sulfates than secondary alkyl sulfates, the homolog Pisa1 in Pseudomonas sp. DSM 6611 has been shown to exhibit a strong preference for sec -alkyl sulfates over primary [10, 11]. This Pisa1-catalyzed hydrolysis is highly enantioselective, and mechanistic studies have shown that the reaction catalyzed by both Pisa1 and SdsA1 breaks the sulfate ester C–OS bond, resulting in inversion of stereochemistry at that carbon atom if it is chiral [11].…”

Section: Introductionmentioning

confidence: 99%

“…DSM 6611 has been shown to exhibit a strong preference for sec -alkyl sulfates over primary [10, 11]. This Pisa1-catalyzed hydrolysis is highly enantioselective, and mechanistic studies have shown that the reaction catalyzed by both Pisa1 and SdsA1 breaks the sulfate ester C–OS bond, resulting in inversion of stereochemistry at that carbon atom if it is chiral [11]. The crystal structures of both SdsA1 and Pisa1, as well as the Escherichia coli homolog YjcS, have been determined, and a comparison reveals a high degree of similarity in the binuclear Zn(II)-binding site within their active sites [7, 10, 12].…”

Section: Introductionmentioning

confidence: 99%

The eukaryotic enzyme Bds1 is an alkyl but not an aryl sulfohydrolase

Waddell

Gilmer

Taylor

et al. 2017

Biochemical and Biophysical Research Communications

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The eukaryotic enzyme Bds1 in Saccharomyces cerevisiae is a metallo-β-lactamase-related enzyme evolutionarily originating from bacterial horizontal gene transfer that serves an unknown biological role. Previously, Bds1 was reported to be an alkyl and aryl sulfatase. However, we demonstrate here that Bds1 acts on primary alkyl sulfates (of 6–12 carbon atoms) but not the aryl sulfates p-nitrophenyl sulfate and p-nitrocatechol sulfate. The apparent catalytic rate constant for hydrolysis of the substrate 1-hexyl sulfate by Bds1 is over 100 times lower than that of the reaction catalyzed by its bacterial homolog SdsA1. We show that Bds1 shares a catalytic mechanism with SdsA1 in which the carbon atom of the sulfate ester is the subject of nucleophilic attack, rather than the sulfur atom, resulting in C–O bond lysis. In contrast to SdsA1 and another bacterial homolog with selectivity for secondary alkyl sulfates named Pisa1, Bds1 does not show any substantial activity towards secondary alkyl sulfates. Neither Bds1 nor SdsA1 have any significant activity towards a branched primary alkyl sulfate, primary and secondary steroid sulfates, or phosphate diesters. Therefore, the enzymes homologous to SdsA1 that have been identified and characterized thus far vary in their selectivity towards primary and secondary alkyl sulfates but do not exhibit aryl sulfatase activity.

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A Stereoselective Inverting sec-Alkylsulfatase for the Deracemization of sec-Alcohols

Cited by 34 publications

References 24 publications

Biocatalysis: A Status Report

Biocatalysis: A Status Report

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

The eukaryotic enzyme Bds1 is an alkyl but not an aryl sulfohydrolase

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