scholarly journals Purification and crystallization of benzoylformate decarboxylase

2008 ◽  
Vol 4 (5) ◽  
pp. 955-959 ◽  
Author(s):  
Miriam S. Hasson ◽  
Gregory A. Petsko ◽  
Dagmar Ringe ◽  
Angelika Muscate ◽  
Gary T.M. Henehan ◽  
...  
Keyword(s):  
Benzoylformate Decarboxylase

Carboligation Reactions Mediated by Benzoylformate Decarboxylase Immobilized on a Magnetic Solid Support

Chirality ◽  
2013 ◽  
Vol 25 (7) ◽  
pp. 415-421 ◽  
Author(s):  
Bilsen Tural ◽  
Servet Tural ◽  
Ayhan S. Demir
Keyword(s):  
Solid Support ◽  
Benzoylformate Decarboxylase ◽  
Magnetic Solid

Enantioselective Syntheses of Hydroxy Ketones via Benzoylformate Decarboxylase- and Benzaldehyde Lyase-Catalyzed C—C Bond Formation

ChemInform ◽  
2004 ◽  
Vol 35 (52) ◽  
Author(s):  
Bettina Lingen ◽  
Martina Pohl ◽  
Ayhan S. Demir ◽  
Andreas Liese ◽  
Michael Mueller
Keyword(s):  
Bond Formation ◽  
Benzoylformate Decarboxylase ◽  
Hydroxy Ketones ◽  
Enantioselective Syntheses

scholarly journals Identification of Novel Benzoylformate Decarboxylases by Growth Selection

2006 ◽  
Vol 72 (12) ◽  
pp. 7510-7517 ◽  
Author(s):  
Helge Henning ◽  
Christian Leggewie ◽  
Martina Pohl ◽  
Michael Müller ◽  
Thorsten Eggert ◽  
...  
Keyword(s):  
Environmental Dna ◽  
Selective Medium ◽  
The Novel ◽  
Selection System ◽  
Dna Library ◽  
Benzoylformate Decarboxylase ◽  
Growth Deficiency ◽  
Growth Selection ◽  
Genes Encoding ◽  
Encoding Genes

ABSTRACT A growth selection system was established using Pseudomonas putida, which can grow on benzaldehyde as the sole carbon source. These bacteria presumably metabolize benzaldehyde via the β-ketoadipate pathway and were unable to grow in benzoylformate-containing selective medium, but the growth deficiency could be restored by expression in trans of genes encoding benzoylformate decarboxylases. The selection system was used to identify three novel benzoylformate decarboxylases, two of them originating from a chromosomal library of P. putida ATCC 12633 and the third from an environmental-DNA library. The novel P. putida enzymes BfdB and BfdC exhibited 83% homology to the benzoylformate decarboxylase from P. aeruginosa and 63% to the enzyme MdlC from P. putida ATCC 12633, whereas the metagenomic BfdM exhibited 72% homology to a putative benzoylformate decarboxylase from Polaromonas naphthalenivorans. BfdC was overexpressed in Escherichia coli, and the enzymatic activity was determined to be 22 U/ml using benzoylformate as the substrate. Our results clearly demonstrate that P. putida KT2440 is an appropriate selection host strain suitable to identify novel benzoylformate decarboxylase-encoding genes. In principle, this system is also applicable to identify a broad range of different industrially important enzymes, such as benzaldehyde lyases, benzoylformate decarboxylases, and hydroxynitrile lyases, which all catalyze the formation of benzaldehyde.

scholarly journals The Mandelate Pathway, an Alternative to the Phenylalanine Ammonia Lyase Pathway for the Synthesis of Benzenoids in Ascomycete Yeasts

2020 ◽  
Vol 86 (17) ◽  
Author(s):  
Maria Jose Valera ◽  
Eduardo Boido ◽  
Juan Carlos Ramos ◽  
Eduardo Manta ◽  
Rafael Radi ◽  
...  
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Aromatic Amino Acids ◽  
Fermentation Medium ◽  
Coumaric Acid ◽  
Content Type ◽  
Benzoylformate Decarboxylase ◽  
Feeding Experiments ◽  
Tyrosine Ammonia Lyase ◽  
Metabolic Reactions ◽  
Level 2

ABSTRACT Benzenoid-derived metabolites act as precursors for a wide variety of products involved in essential metabolic roles in eukaryotic cells. They are synthesized in plants and some fungi through the phenylalanine ammonia lyase (PAL) and tyrosine ammonia lyase (TAL) pathways. Ascomycete yeasts and animals both lack the capacity for PAL/TAL pathways, and metabolic reactions leading to benzenoid synthesis in these organisms have remained incompletely known for decades. Here, we show genomic, transcriptomic, and metabolomic evidence that yeasts use a mandelate pathway to synthesize benzenoids, with some similarities to pathways used by bacteria. We conducted feeding experiments using a synthetic fermentation medium that contained either 13C-phenylalanine or 13C-tyrosine, and, using methylbenzoylphosphonate (MBP) to inhibit benzoylformate decarboxylase, we were able to accumulate intracellular intermediates in the yeast Hanseniaspora vineae. To further confirm this pathway, we tested in separate fermentation experiments three mutants with deletions in the key genes putatively proposed to form benzenoids (Saccharomyces cerevisiae aro10Δ, dld1Δ, and dld2Δ strains). Our results elucidate the mechanism of benzenoid synthesis in yeast through phenylpyruvate linked with the mandelate pathway to produce benzyl alcohol and 4-hydroxybenzaldehyde from the aromatic amino acids phenylalanine and tyrosine, as well as sugars. These results provide an explanation for the origin of the benzoquinone ring, 4-hydroxybenzoate, and suggest that Aro10p has benzoylformate and 4-hydroxybenzoylformate decarboxylase functions in yeast. IMPORTANCE We present here evidence of the existence of the mandelate pathway in yeast for the synthesis of benzenoids. The link between phenylpyruvate- and 4-hydroxyphenlypyruvate-derived compounds with the corresponding synthesis of benzaldehydes through benzoylformate decarboxylation is demonstrated. Hanseniaspora vineae was used in these studies because of its capacity to produce benzenoid derivatives at a level 2 orders of magnitude higher than that produced by Saccharomyces. Contrary to what was hypothesized, neither β-oxidation derivatives nor 4-coumaric acid is an intermediate in the synthesis of yeast benzenoids. Our results might offer an answer to the long-standing question of the origin of 4-hydroxybenzoate for the synthesis of Q10 in humans.

scholarly journals A Theoretical Study of the Benzoylformate Decarboxylase Reaction Mechanism

2018 ◽  
Vol 6 ◽  
Author(s):  
Ferran Planas ◽  
Xiang Sheng ◽  
Michael J. McLeish ◽  
Fahmi Himo
Keyword(s):  
Reaction Mechanism ◽  
Theoretical Study ◽  
Benzoylformate Decarboxylase

scholarly journals Physiological relation between respiration activity and heterologous expression of selected benzoylformate decarboxylase variants in Escherichia coli

2010 ◽  
Vol 9 (1) ◽  
pp. 76 ◽  
Author(s):  
Thomas G Palmen ◽  
Jens Nieveler ◽  
Bettina Frölich ◽  
Wiltrud Treffenfeldt ◽  
Martina Pohl ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heterologous Expression ◽  
Respiration Activity ◽  
Benzoylformate Decarboxylase

Alteration of the Substrate Specificity of Benzoylformate Decarboxylase from Pseudomonas putida by Directed Evolution

ChemBioChem ◽  
2003 ◽  
Vol 4 (8) ◽  
pp. 721-726 ◽  
Author(s):  
Bettina Lingen ◽  
Doris Kolter-Jung ◽  
Pascal Dünkelmann ◽  
Ralf Feldmann ◽  
Joachim Grötzinger ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Pseudomonas Putida ◽  
Directed Evolution ◽  
Benzoylformate Decarboxylase

scholarly journals Enzymes of the mandelate pathway in bacterium N.C.I.B. 8250

1968 ◽  
Vol 107 (4) ◽  
pp. 497-506 ◽  
Author(s):  
S. I. T. Kennedy ◽  
C A Fewson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Benzyl Alcohol ◽  
Benzoylformate Decarboxylase ◽  
Heat Stable ◽  
Enzyme Systems ◽  
Heat Labile ◽  
Hydroxybenzoate Hydroxylase ◽  
Benzaldehyde Dehydrogenase

1. Bacterium N.C.I.B. 8250 was grown on dl-mandelate, benzyl alcohol, benzoyl-formate, benzaldehyde and benzoate and also on 2-hydroxy, 4-hydroxy, 3,4-dihydroxy and 4-hydroxy-3-methoxy analogues of these compounds. The enzymic complements of the cells were determined and the specificities of some of the enzymes examined. 2. Growth on mandelate or benzoylformate induces l-mandelate dehydrogenase, benzoylformate decarboxylase, benzyl alcohol dehydrogenase and a heat-stable as well as a heat-labile benzaldehyde dehydrogenase. Growth on benzyl alcohol or benzaldehyde induces benzyl alcohol dehydrogenase and the heat-labile benzaldehyde dehydrogenase. 3. The enzymes of the mandelate-to-benzoate pathway are non-specifically active on, and induced by, all the substituted analogues that support growth. 4. Benzoate oxidase is induced by growth on benzoate or on 2-hydroxybenzoate. 2-Hydroxybenzoate hydroxylase, 4-hydroxybenzoate hydroxylase and 4-hydroxy-3-methoxybenzoate O-demethylase are induced only by growth on homologous substrates. 5. The results of the investigation are discussed with regard to the possible regulation of the enzyme systems.

Sign in / Sign up

Export Citation Format

Share Document