Hydrolysis of lysergamide to lysergic acid by Rhodococcus equi A4

Martı́nková, Ludmila; Křen, Vladimı́r; Cvak, Ladislav; Ovesná, Mária; Přepechalová, Irena

doi:10.1016/s0168-1656(00)00332-1

Cited by 13 publications

(6 citation statements)

References 8 publications

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“…In protic solvents, lysergyl derivatives readily form stereoisomers around carbon 8. Martínková et al (2000) found that ergine more rapidly isomerized to erginine than did lysergic acid to isolysergic acid. Reversion to the carbonyl form may take place in such a way as to yield either of two stereoisomers (Fig.…”

Section: Quantificationmentioning

confidence: 98%

Analysis and Modification of Ergot Alkaloid Profiles in Fungi

Panaccione¹,

Ryan²,

Schardl³

et al. 2012

Methods in Enzymology

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Section: Quantificationmentioning

confidence: 98%

Analysis and Modification of Ergot Alkaloid Profiles in Fungi

Panaccione¹,

Ryan²,

Schardl³

et al. 2012

Methods in Enzymology

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“…It has been found that a strain of R. equi was capable of producing an amidase that degraded lysergamide to lysergic acid (Martínková et al 2000) and this may have occurred to the acetylated metabolite of SMX to form an alcohol derivative. R. equi can also produce urethanase, which hydrolyzes anilides, and N-acetyl-phenylethylamine hydrolase which hydrolizes N-acetylated compounds (BRENDA The Comprehensive Enzyme Information System).…”

Section: Individual Bacteriamentioning

confidence: 99%

Biodegradation of sulfamethoxazole by individual and mixed bacteria

Larcher

Yargeau

2011

Appl Microbiol Biotechnol

151

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Antibiotic compounds, like sulfamethoxazole (SMX), have become a concern in the aquatic environment due to the potential development of antibacterial resistances. Due to excretion and disposal, SMX has been frequently detected in wastewaters and surface waters. SMX removal in conventional wastewater treatment plants (WWTPs) ranges from 0% to 90%, and there are opposing results regarding its biodegradability at lab scale. The objective of this research was to determine the ability of pure cultures of individual and mixed consortia of bacteria (Bacillus subtilis, Pseudomonas aeruginosa, Pseudomonas putida, Rhodococcus equi, Rhodococcus erythropolis, Rhodococcus rhodocrous, and Rhodococcus zopfii) known to exist in WWTP activated sludge to remove SMX. Results showed that R. equi alone had the greatest ability to remove SMX leading to 29% removal (with glucose) and the formation of a metabolite. Degradation pathways and metabolite structures have been proposed based on the potential enzymes produced by R. equi. When R. equi was mixed with other microorganisms, a positive synergistic effect was not observed and the maximum SMX removal achieved was 5%. This indicates that pure culture results cannot be extrapolated to mixed culture conditions, and the methodology developed here to study the biodegradability of compounds under controlled mixed culture conditions offers an alternative to conventional studies using pure bacterial cultures or inocula from activated sludge sources consisting of unknown and variable microbial populations.

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“…Although nitrile hydratase shows enantioselectivity with some substrates, such enantioselectivity, is largely due to amidase [43]. Previous research has shown that a large number of amidases hydrolyze (S)-amides bearing an a-stereocenter with high enantioselectivity [14,16,18,45] and some with (R)-enantioselectivity [4,25,29,30]. As for regioselectivity, most amidases recognize an a-stereocenter with high stereoselectivity.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of a recombinant amidase in a complex auto-inducing culture: purification, biochemical characterization, and regio- and stereoselectivity

Xue

Chao

Wang

et al. 2011

J Ind Microbiol Biotechnol

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Rhodococcus erythropolis AJ270 metabolizes a wide range of nitriles via the two-step nitrile hydratase/amidase pathway. In this study, an amidase gene from R. erythropolis AJ270 was cloned and expressed in Escherichia coli BL21 (DE3). The activity reached the highest level of 22.04 U/ml in a complex auto-inducing medium using a simplified process of fermentation operation. The recombinant amidase was purified to more than 95% from the crude lysate using Ni-NTA affinity chromatography and Superose S10-300 gel filtration. The V(max) and K(m) values of the purified enzyme with acetamide (50 mM) were 6.89 μmol/min/mg protein and 4.12 mM, respectively, which are similar to those of the enzyme from the wild-type cell. The enzyme converted racemic α-substituted amides, O-benzylated β-hydroxy amides, and N-benzylated β-amino amides to the corresponding (S)-acids with remarkably high enantioselectivity. The ionic liquid [BMIm][PF₆] (1-butyl-3-methylimidazolium hexafluorophosphate) enhanced the activity by 1.5-fold compared with water. The adequate expression of the enzyme and excellent enantioselectivity of the recombinant amidase to a broad spectrum of amides suggest that the enzyme has prospective industrial-scale practical applications in pharmaceutical chemistry.

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Hydrolysis of lysergamide to lysergic acid by Rhodococcus equi A4

Cited by 13 publications

References 8 publications

Analysis and Modification of Ergot Alkaloid Profiles in Fungi

Analysis and Modification of Ergot Alkaloid Profiles in Fungi

Biodegradation of sulfamethoxazole by individual and mixed bacteria

Overexpression of a recombinant amidase in a complex auto-inducing culture: purification, biochemical characterization, and regio- and stereoselectivity

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