scholarly journals Tunable Production of (R)- or (S)-Citronellal from Geraniol via a Bienzymatic Cascade Using a Copper Radical Alcohol Oxidase and Old Yellow Enzyme

ACS Catalysis ◽  
2022 ◽  
pp. 1111-1116
Author(s):  
David Ribeaucourt ◽  
Georg T. Höfler ◽  
Mehdi Yemloul ◽  
Bastien Bissaro ◽  
Fanny Lambert ◽  
...  
Keyword(s):  
Alcohol Oxidase ◽  
Old Yellow Enzyme

scholarly journals Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes.

1976 ◽  
Vol 251 (17) ◽  
pp. 5327-5336
Author(s):  
A S Abramovitz ◽  
V Massey
Keyword(s):  
Charge Transfer ◽  
Charge Transfer Complexes ◽  
Old Yellow Enzyme ◽  
Physical Evidence

scholarly journals Isolation of Old Yellow Enzyme in Free and Complexed Forms

1969 ◽  
Vol 244 (7) ◽  
pp. 1779-1786 ◽  
Author(s):  
R G Matthews ◽  
V Massey
Keyword(s):  
Old Yellow Enzyme

scholarly journals Cascading Old Yellow Enzyme, Alcohol Dehydrogenase and Glucose Dehydrogenase for Selective Reduction of (E/Z)-Citral to (S)-Citronellol

Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 931
Author(s):  
Yunpeng Jia ◽  
Qizhou Wang ◽  
Jingjing Qiao ◽  
Binbin Feng ◽  
Xueting Zhou ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Glucose Dehydrogenase ◽  
Selective Reduction ◽  
Coli Strain ◽  
Severe Reaction ◽  
High Catalytic Activity ◽  
Old Yellow Enzyme ◽  
One Pot ◽  
Nadph Regeneration ◽  
By Products

Citronellol is a kind of unsaturated alcohol with rose-like smell and its (S)-enantiomer serves as an important intermediate for organic synthesis of (-)-cis-rose oxide. Chemical methods are commonly used for the synthesis of citronellol and its (S)-enantiomer, which suffers from severe reaction conditions and poor selectivity. Here, the first one-pot double reduction of (E/Z)-citral to (S)-citronellol was achieved in a multi-enzymatic cascade system: N-ethylmaleimide reductase from Providencia stuartii (NemR-PS) was selected to catalyze the selective reduction of (E/Z)-citral to (S)-citronellal, alcohol dehydrogenase from Yokenella sp. WZY002 (YsADH) performed the further reduction of (S)-citronellal to (S)-citronellol, meanwhile a variant of glucose dehydrogenase from Bacillus megaterium (BmGDHM6), together with glucose, drove efficient NADPH regeneration. The Escherichia coli strain co-expressing NemR-PS, YsADH, and BmGDHM6 was successfully constructed and used as the whole-cell catalyst. Various factors were investigated for achieving high conversion and reducing the accumulation of the intermediate (S)-citronellal and by-products. 0.4 mM NADP+ was essential for maintaining high catalytic activity, while the feeding of the cells expressing BmGDHM6 effectively eliminated the intermediate and by-products and shortened the reaction time. Under optimized conditions, the bio-transformation of 400 mM citral caused nearly complete conversion (>99.5%) to enantio-pure (S)-citronellol within 36 h, demonstrating promise for industrial application.

scholarly journals E. coli Nickel‐Iron Hydrogenase 1 Catalyses Non‐native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme Ene‐reductases

2021 ◽  
Author(s):  
Shiny Joseph Srinivasan ◽  
Sarah Elizabeth Cleary ◽  
Miguel Ramirez ◽  
Holly Reeve ◽  
Caroline Paul ◽  
...  
Keyword(s):  
Old Yellow Enzyme ◽  
Nickel Iron Hydrogenase ◽  
Nickel Iron ◽  
E Coli ◽  
Iron Hydrogenase ◽  
Alkene Hydrogenation

scholarly journals Positive Selection of Novel Peroxisome Biogenesis-Defective Mutants of the Yeast Pichia pastoris

Genetics ◽  
1999 ◽  
Vol 151 (4) ◽  
pp. 1379-1391
Author(s):  
Monique A Johnson ◽  
Hans R Waterham ◽  
Galyna P Ksheminska ◽  
Liubov R Fayura ◽  
Joan Lin Cereghino ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Allyl Alcohol ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeast ◽  
Direct Selection ◽  
Toxic Exposure ◽  
Peroxisome Biogenesis ◽  
Yeast Pichia Pastoris ◽  
Methylotrophic Yeast Pichia Pastoris ◽  
Selection Of

Abstract We have developed two novel schemes for the direct selection of peroxisome-biogenesis-defective (pex) mutants of the methylotrophic yeast Pichia pastoris. Both schemes take advantage of our observation that methanol-induced pex mutants contain little or no alcohol oxidase (AOX) activity. AOX is a peroxisomal matrix enzyme that catalyzes the first step in the methanol-utilization pathway. One scheme utilizes allyl alcohol, a compound that is not toxic to cells but is oxidized by AOX to acrolein, a compound that is toxic. Exposure of mutagenized populations of AOX-induced cells to allyl alcohol selectively kills AOX-containing cells. However, pex mutants without AOX are able to grow. The second scheme utilizes a P. pastoris strain that is defective in formaldehyde dehydrogenase (FLD), a methanol pathway enzyme required to metabolize formaldehyde, the product of AOX. AOX-induced cells of fld1 strains are sensitive to methanol because of the accumulation of formaldehyde. However, fld1 pex mutants, with little active AOX, do not efficiently oxidize methanol to formaldehyde and therefore are not sensitive to methanol. Using these selections, new pex mutant alleles in previously identified PEX genes have been isolated along with mutants in three previously unidentified PEX groups.

scholarly journals Purification of intact old yellow enzyme using an affinity matrix for the sole chromatographic step.

1976 ◽  
Vol 251 (17) ◽  
pp. 5321-5326 ◽  
Author(s):  
A S Abramovitz ◽  
V Massey
Keyword(s):  
Affinity Matrix ◽  
Old Yellow Enzyme

Molecular cloning of the isoamyl alcohol oxidase-encoding gene (mreA) from Aspergillus oryzae

2000 ◽  
Vol 89 (6) ◽  
pp. 522-527 ◽  
Author(s):  
Nobuo Yamashita ◽  
Toru Motoyoshi ◽  
Akira Nishimura
Keyword(s):  
Molecular Cloning ◽  
Aspergillus Oryzae ◽  
Alcohol Oxidase ◽  
Isoamyl Alcohol ◽  
Encoding Gene
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