Improved Biocatalysts from a Synthetic Circular Permutation Library of the Flavin-Dependent Oxidoreductase Old Yellow Enzyme

2013 ◽  
Vol 135 (38) ◽  
pp. 14425-14432 ◽  
Author(s):  
Ashley B. Daugherty ◽  
Sridhar Govindarajan ◽  
Stefan Lutz
Keyword(s):  
Circular Permutation ◽  
Old Yellow Enzyme

scholarly journals Structural and Functional Consequences of Circular Permutation on the Active Site of Old Yellow Enzyme

ACS Catalysis ◽  
2015 ◽  
Vol 5 (2) ◽  
pp. 892-899 ◽  
Author(s):  
Ashley B. Daugherty ◽  
John R. Horton ◽  
Xiaodong Cheng ◽  
Stefan Lutz
Keyword(s):  
Active Site ◽  
Circular Permutation ◽  
Old Yellow Enzyme ◽  
Functional Consequences

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 CPDB: a database of circular permutation in proteins

2008 ◽  
Vol 37 (suppl_1) ◽  
pp. D328-D332 ◽  
Author(s):  
Wei-Cheng Lo ◽  
Chi-Ching Lee ◽  
Che-Yu Lee ◽  
Ping-Chiang Lyu
Keyword(s):  
Circular Permutation

Circular permutation graphs

Networks ◽  
1982 ◽  
Vol 12 (4) ◽  
pp. 429-437 ◽  
Author(s):  
D. Rotem ◽  
J. Urrutia
Keyword(s):  
Circular Permutation ◽  
Permutation Graphs

scholarly journals Engineering the metal-binding loop at a type 1 copper center by circular permutation

RSC Advances ◽  
2017 ◽  
Vol 7 (88) ◽  
pp. 56093-56098
Author(s):  
Honghui Chen ◽  
Binbin Su ◽  
Tongtong Zhang ◽  
Aiping Huang ◽  
Haiping Liu ◽  
...  
Keyword(s):  
Metal Binding ◽  
Circular Permutation ◽  
Type 1 Copper ◽  
Copper Center ◽  
Binding Loop

Circular permutation of the cupredoxin azurin creates a break on the metal binding loop, highlighting the loop's flexibility.

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