On the formation of 3‐phenylpropionate and the different stereo‐chemical course of the reduction of cinnamate by <i>Clostridium sporogenes</i> and <i>Peptostreptococcus anaerobius</i>

Giesel, Hermine; Machacek, Gerhard; Bayerl, Josef; Simon, Helmut

doi:10.1016/0014-5793(81)80030-0

Cited by 21 publications

(14 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The formation of ( R )‐2‐hydroxy‐4‐methylpentanoic acid by C. butyricum from l ‐leucine indicates that inversion of configuration on the C‐2 atom is involved. This observation agrees with the results [18] relative to the stereospecificity of 2‐oxo acid reductase (2‐hydroxy acid dehydrogenase). In the case of l ‐isoleucine, the absence of bioconversion does not seem to be due to a steric hindrance on the C‐3 atom since l ‐valine is a substrate in the same conditions.…”

Section: Resultssupporting

confidence: 92%

See 1 more Smart Citation

Bioconversion of 2-amino acids to 2-hydroxy acids byClostridium butyricum

Khelifa

Dugay

Tessedre

et al. 1998

FEMS Microbiology Letters

View full text Add to dashboard Cite

Analysis by gas chromatography‐mass spectrometry (GC‐MS) of 24‐h cultures of Clostridium butyricum type strain in synthetic BMG medium supplemented with various 2‐amino acids (10 mM) revealed the presence of the corresponding 2‐hydroxy acids. C. butyricum was able to bioconvert l‐valine, dl‐norvaline, l‐leucine, dl‐norleucine, l‐methionine and l‐phenylalanine as well as unusual 2‐amino acids, i.e., l‐2‐aminobutyric acid, l‐2‐amino‐4‐pentenoic acid, dl‐2‐aminooctanoic acid, and dl‐2‐amino‐4‐phenylbutanoic acid. l‐Isoleucine and cycloleucine were not converted into their corresponding 2‐hydroxy acids. The bioconversion rate was maximal with dl‐norvaline (6.2%). Chiral GC analysis demonstrated that only d‐2‐hydroxy‐4‐methylpentanoic acid is formed from l‐leucine, indicating that the bioconversion is stereospecific, with inversion of configuration. d‐Leucine and d‐methionine were also converted to the corresponding 2‐hydroxy acids. This observation opens new aspects in the study of C. butyricum and raises questions about the amino acid metabolism by this species.

show abstract

Section: Resultssupporting

confidence: 92%

“…In C. sporogenes , l ‐leucine is oxidized into 3‐methylbutyric acid and reduced into 4‐methylpentanoic acid [16, 17]. Some Clostridium species are able to synthesize a 2‐oxo acid reductase yielding a ( R )‐2‐hydroxy acid [17, 18] but no results are given for C. butyricum .…”

Section: Resultsmentioning

confidence: 99%

Bioconversion of 2-amino acids to 2-hydroxy acids byClostridium butyricum

Khelifa

Dugay

Tessedre

et al. 1998

FEMS Microbiology Letters

View full text Add to dashboard Cite

show abstract

“…The formation of (R)-2-hydroxy-4-methylpentanoic acid by C. butyricum from L-leucine indicates that inversion of con¢guration on the C-2 atom is involved. This observation agrees with the results [18] relative to the stereospeci¢city of 2-oxo acid reductase (2-hydroxy acid dehydrogenase). In the case of L-isoleucine, the absence of bioconversion does not seem to be due to a steric hindrance on the C-3 atom since L-valine is a substrate in the same conditions.…”

Section: Resultssupporting

confidence: 92%

“…In C. sporogenes, L-leucine is oxidized into 3-methylbutyric acid and reduced into 4-methylpentanoic acid [16,17]. Some Clostridium species are able to synthesize a 2-oxo acid reductase yielding a (R)-2-hydroxy acid [17,18] but no results are given for C. butyricum.…”

Section: Resultsmentioning

confidence: 99%

Bioconversion of 2-amino acids to 2-hydroxy acids by Clostridium butyricum

Khelifa¹

1998

FEMS Microbiology Letters

View full text Add to dashboard Cite

Analysis by gas chromatography-mass spectrometry (GC-MS) of 24-h cultures of Clostridium butyricum type strain in synthetic BMG medium supplemented with various 2-amino acids (10 mM) revealed the presence of the corresponding 2-hydroxy acids. C. butyricum was able to bioconvert L-valine, DL-norvaline, L-leucine, DL-norleucine, L-methionine and L-phenylalanine as well as unusual 2-amino acids, i.e., L-2-aminobutyric acid, L-2-amino-4-pentenoic acid, DL-2-aminooctanoic acid, and DL-2-amino-4-phenylbutanoic acid. L-Isoleucine and cycloleucine were not converted into their corresponding 2-hydroxy acids. The bioconversion rate was maximal with DL-norvaline (6.2%). Chiral GC analysis demonstrated that only D-2-hydroxy-4-methylpentanoic acid is formed from L-leucine, indicating that the bioconversion is stereospecific, with inversion of configuration. D-Leucine and D-methionine were also converted to the corresponding 2-hydroxy acids. This observation opens new aspects in the study of C. butyricum and raises questions about the amino acid metabolism by this species. z

show abstract

“…We decided to use Clostridium sporogenes in initial tests for amide reduction as it uses amino acids as respiratory electron acceptors via the Stickland reaction (Buehler et al 1980;Giesel et al 1981;Bader et al 1982;Pitsch & Simon 1982;Bader & Simon 1983;Giesel & Simon 1983), and reduces aromatic and aliphatic nitro groups (Angermaier & Simon 1983a,b). Therefore, the substrate range for N-containing organics is very broad, making C. sporogenes an attractive choice for initial studies.…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic Amide Reduction Using Clostridium sporogenes

2005

View full text Add to dashboard Cite

Washed cells of Clostridium sporogenes reduced benzamide (up to 20 mM: ) to benzylamine in yields up to 73% using H2 as electron donor with less than 10 g biocatalyst/l over 24 h. Product formation exhibited complex kinetics, with a lag before benzylamine production began. Very little substrate was hydrolysed since the maximum yield of benzoic acid was only 9% of the substrate added. Boiled cells were inactivated thus confirming that amide reduction was enzyme-catalysed.

show abstract

On the formation of 3‐phenylpropionate and the different stereo‐chemical course of the reduction of cinnamate by Clostridium sporogenes and Peptostreptococcus anaerobius

Cited by 21 publications

References 9 publications

Bioconversion of 2-amino acids to 2-hydroxy acids byClostridium butyricum

Bioconversion of 2-amino acids to 2-hydroxy acids byClostridium butyricum

Bioconversion of 2-amino acids to 2-hydroxy acids by Clostridium butyricum

Biocatalytic Amide Reduction Using Clostridium sporogenes

Contact Info

Product

Resources

About